The Cbl interactome and its functions

Cell Signaling by Receptor Tyrosine Kinases

Lemmon, M. A., & Schlessinger, J. (2010) · Cell · doi:10.1016/j.cell.2010.06.011 · Cited by 7,929 · see citing works

Untangling the ErbB signalling network

Yarden, Y., & Sliwkowski, M. X. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35052073 · Cited by 6,974 · see citing works

Cell Signaling by Receptor Tyrosine Kinases

Schlessinger, J. (2000) · Cell · doi:10.1016/s0092-8674(00)00114-8 · Cited by 3,774 · see citing works

Mechanisms Underlying Ubiquitination

Pickart, C. M. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.503 · Cited by 3,731 · see citing works

Rab proteins as membrane organizers

Zerial, M., & McBride, H. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35052055 · Cited by 3,381 · see citing works

Themes and variations on ubiquitylation

Weissman, A. M. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056563 · Cited by 1,472 · see citing works

Protein regulation by monoubiquitin

Hicke, L. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056583 · Cited by 1,213 · see citing works

Proteolysis: from the lysosome to ubiquitin and the proteasome

Ciechanover, A. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1552 · Cited by 1,133 · see citing works

The Tyrosine Kinase Negative Regulator c-Cbl as a RING-Type, E2-Dependent Ubiquitin-Protein Ligase

Joazeiro, C. A. P., Wing, S. S., Huang, H.-K., Leverson, J. D., Hunter, T. R., & Liu, Y. (1999) · Science · doi:10.1126/science.286.5438.309 · Cited by 1,036 · see citing works

Ubiquitin Ligase Activity and Tyrosine Phosphorylation Underlie Suppression of Growth Factor Signaling by c-Cbl/Sli-1

Levkowitz, G., Waterman, H., Ettenberg, S. A., Katz, M., Tsygankov, A. Y., Alroy, I., Lavi, S., Iwaï, K., Reiss, Y., Ciechanover, A. J., et al. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80231-2 · Cited by 1,003 · see citing works

Ligand-Induced, Receptor-Mediated Dimerization and Activation of EGF Receptor

Schlessinger, J. (2002) · Cell · doi:10.1016/s0092-8674(02)00966-2 · Cited by 995 · see citing works

Clathrin-independent endocytosis of ubiquitinated cargos

Sigismund, S., Woelk, T., Puri, C., Maspero, E., Tacchetti, C., Transidico, P., Fiore, P. P. D., & Polo, S. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409817102 · Cited by 830 · see citing works

AIP1/ALIX Is a Binding Partner for HIV-1 p6 and EIAV p9 Functioning in Virus Budding

Strack, B., Calistri, A., Craig, S., Popova, E., & Göttlinger, H. G. (2003) · Cell · doi:10.1016/s0092-8674(03)00653-6 · Cited by 825 · see citing works

The biogenesis of multivesicular endosomes

Gruenberg, J. E., & Stenmark, H. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1360 · Cited by 723 · see citing works

Phosphatidylinositol 4,5-bisphosphate functions as a second messenger that regulates cytoskeleton-plasma membrane adhesion

Raucher, D., Stauffer, T., Chen, W., Shen, K., Guo, S., York, J. D., Sheetz, M. P., & Meyer, T. (2000) · Cell · doi:10.1016/s0092-8674(00)81560-3 · Cited by 675 · see citing works

Negative regulation of lymphocyte activation and autoimmunity by the molecular adaptor Cbl-b

Bachmaier, K., Krawczyk, C. M., Kozieradzki, I., Kong, Y., Sasaki, T., Oliveira-dos-Santos, A., Mariathasan, S., Bouchard, D., Wakeham, A. C., Itié, A., et al. (2000) · Nature · doi:10.1038/35003228 · Cited by 674 · see citing works

Cbl: many adaptations to regulate protein tyrosine kinases

Thien, C. B. F., & Langdon, W. Y. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35067100 · Cited by 628 · see citing works

Cbl-b regulates the CD28 dependence of T-cell activation

Chiang, Y. J., Kole, H. K., Brown, K. E., Naramura, M., Fukuhara, S., Hu, R.-J., Jang, I. K., Gutkind, J. S., Shevach, E. M., & Gu, H. (2000) · Nature · doi:10.1038/35003235 · Cited by 626 · see citing works

Insulin-stimulated GLUT4 translocation requires the CAP-dependent activation of TC10

Chiang, S.-H., Baumann, C. A., Kanzaki, M., Thurmond, D. C., Watson, R. T., Neudauer, C. L., Macara, I. G., Pessin, J. E., & Saltiel, A. R. (2001) · Nature · doi:10.1038/35073608 · Cited by 611 · see citing works

Cbl–CIN85–endophilin complex mediates ligand-induced downregulation of EGF receptors

Soubeyran, P., Kowanetz, K., Szymkiewicz, I., Langdon, W. Y., & Đikić, I. (2002) · Nature · doi:10.1038/416183a · Cited by 584 · see citing works

The Immunological Synapse Balances T Cell Receptor Signaling and Degradation

Lee, K., Dinner, A. R., Tu, C., Campi, G., Raychaudhuri, S., Varma, R., Sims, T. N., Burack, R., Wu, H., Wang, J., et al. (2003) · Science · doi:10.1126/science.1086507 · Cited by 541 · see citing works

The role of phosphoinositides in membrane transport

Simonsen, A., Wurmser, A. E., Emr, S. D., & Stenmark, H. (2001) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00240-4 · Cited by 478 · see citing works

The endophilin–CIN85–Cbl complex mediates ligand-dependent downregulation of c-Met

Petrelli, A., Gilestro, G. F., Lanzardo, S., Comoglio, P. M., Migone, N., & Giordano, S. (2002) · Nature · doi:10.1038/416187a · Cited by 473 · see citing works

Osprey: a network visualization system

Breitkreutz, B., Stark, C., & Tyers, M. (2003) · Genome biology · doi:10.1186/gb-2003-4-3-r22 · Cited by 472 · see citing works

Signaling Networks

Jordan, J. D., Landau, E. M., & Iyengar, R. (2000) · Cell · doi:10.1016/s0092-8674(00)00112-4 · Cited by 459 · see citing works

Nuclear lipid signalling

Irvine, R. F. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1100 · Cited by 403 · see citing works

c-Cbl and Cbl-b regulate T cell responsiveness by promoting ligand-induced TCR down-modulation

Naramura, M., Jang, I. K., Kole, H. K., Huang, F., Haines, D. C., & Gu, H. (2002) · Nature Immunology · doi:10.1038/ni855 · Cited by 396 · see citing works

Modulation of signalling by Sprouty: a developing story

Kim, H. J., & Bar‐Sagi, D. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1400 · Cited by 373 · see citing works

Cbl Associates with Pyk2 and Src to Regulate Src Kinase Activity, αvβ3 Integrin-Mediated Signaling, Cell Adhesion, and Osteoclast Motility

Sanjay, A., Houghton, A., Neff, L., DiDomenico, E., Bardelay, C., Antoine, E., Levy, J. B., Gailit, J. O., Bowtell, D. D. L., Horne, W. C., et al. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.152.1.181 · Cited by 371 · see citing works

Newest findings on the oldest oncogene; how activated src does it

Frame, M. C. (2004) · Journal of Cell Science · doi:10.1242/jcs.01111 · Cited by 369 · see citing works

Tissue Hyperplasia and Enhanced T-Cell Signalling via ZAP-70 in c-Cbl-Deficient Mice

Murphy, M. A., Schnall, R., Venter, D. J., Barnett, L. D., Bertoncello, I., Thien, C. B. F., Langdon, W. Y., & Bowtell, D. D. L. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.8.4872 · Cited by 361 · see citing works

Essential role of the E3 ubiquitin ligase Cbl-b in T cell anergy induction

Jeon, M.-S., Atfield, A., Venuprasad, K., Krawczyk, C., Sarao, R., Elly, C., Yang, C., Arya, S., Bachmaier, K., Su, L., et al. (2004) · Immunity · doi:10.1016/j.immuni.2004.07.013 · Cited by 348 · see citing works

Negative receptor signalling.

Dikič, I., & Giordano, S. (2003) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(03)00004-8 · Cited by 342 · see citing works

Altered thymic positive selection and intracellular signals in Cbl-deficient mice

Naramura, M., Kole, H. K., Hu, R.-J., & Gu, H. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.26.15547 · Cited by 337 · see citing works

Grb2 Regulates Internalization of EGF Receptors through Clathrin-coated Pits

Jiang, X., Huang, F., Marusyk, A., & Sorkin, A. D. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-08-0532 · Cited by 322 · see citing works

v-cbl, an oncogene from a dual-recombinant murine retrovirus that induces early B-lineage lymphomas.

Langdon, W. Y., Hartley, J. W., Klinken, S. P., Ruscetti, S. K., & Morse, H. C. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.4.1168 · Cited by 308 · see citing works

When ubiquitin meets ubiquitin receptors: a signalling connection

Fiore, P. P. D., Polo, S., & Hofmann, K. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1124 · Cited by 306 · see citing works

The GRID: The General Repository for Interaction Datasets

Breitkreutz, B., Stark, C., & Tyers, M. (2003) · Genome biology · doi:10.1186/gb-2003-4-3-r23 · Cited by 294 · see citing works

Similarity of sli-1 , a Regulator of Vulval Development in C. elegans , to the Mammalian Proto-Oncogene c- cbl

Yoon, C. H., Lee, J., Jongeward, G. D., & Sternberg, P. W. (1995) · Science · doi:10.1126/science.7652556 · Cited by 291 · see citing works

c-Cbl is downstream of c-Src in a signalling pathway necessary for bone resorption

Tanaka, S., Amling, M., Neff, L., Peyman, A., Uhlmann, E., Levy, J. B., & Baron, R. (1996) · Nature · doi:10.1038/383528a0 · Cited by 288 · see citing works

Insulin-stimulated GLUT4 Translocation in Adipocytes Is Dependent upon Cortical Actin Remodeling

Kanzaki, M., & Pessin, J. E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m108297200 · Cited by 287 · see citing works

A β1 integrin signaling pathway involving Src‐family kinases, Cbl and PI‐3 kinase is required for macrophage spreading and migration

Meng, F., & Lowell, C. A. (1998) · The EMBO Journal · doi:10.1093/emboj/17.15.4391 · Cited by 279 · see citing works

A Cortactin-CD2-associated Protein (CD2AP) Complex Provides a Novel Link between Epidermal Growth Factor Receptor Endocytosis and the Actin Cytoskeleton

Lynch, D. K., Winata, S. C., Lyons, R. J., Hughes, W. E., Lehrbach, G. M., Wasinger, V. C., Corthals, G. L., Cordwell, S. J., & Daly, R. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211407200 · Cited by 227 · see citing works

E3 ubiquitin ligases as T cell anergy factors

Mueller, D. L. (2004) · Nature Immunology · doi:10.1038/ni1106 · Cited by 224 · cited 1× · see citing works

Cbl-mediated Ubiquitinylation Is Required for Lysosomal Sorting of Epidermal Growth Factor Receptor but Is Dispensable for Endocytosis

Duan, L., Miura, Y., Dimri, M., Majumder, B., Dodge, I. L., Reddi, A. L., Ghosh, A. K., Fernandes, N. D., Zhou, P., Mullane-Robinson, K. P., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304474200 · Cited by 219 · see citing works

Cbl-b Is a Negative Regulator of Receptor Clustering and Raft Aggregation in T Cells

Krawczyk, C. M., Bachmaier, K., Sasaki, T., Jones, R. G., Snapper, S. B., Bouchard, D., Kozieradzki, I., Ohashi, P. S., Alt, F. W., & Penninger, J. M. (2000) · Immunity · doi:10.1016/s1074-7613(00)00046-7 · Cited by 216 · see citing works

All Autophosphorylation Sites of Epidermal Growth Factor (EGF) Receptor and HER2/neu Are Located in Their Carboxyl-terminal Tails

Margolis, B. L., Lax, I., Kris, R., Dombalagian, M., Honegger, A., Howk, R. S., Givol, D., Ullrich, A., & Schlessinger, J. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)81674-x · Cited by 211 · see citing works

Src-catalyzed Phosphorylation of c-Cbl Leads to the Interdependent Ubiquitination of Both Proteins

Yokouchi, M., Kondo, T., Sanjay, A., Houghton, A., Yoshimura, A., Komiya, S., Zhang, H., & Baron, R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102219200 · Cited by 210 · see citing works

Activated Cdc42 Sequesters c-Cbl and Prevents EGF Receptor Degradation

Wu, W. J., Tu, S. S., & Cerione, R. A. (2003) · Cell · doi:10.1016/s0092-8674(03)00688-3 · Cited by 203 · see citing works

CIN85/CMS family of adaptor molecules

Đikić, I. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03188-5 · Cited by 199 · see citing works

Cbl-b, a RING-type E3 Ubiquitin Ligase, Targets Phosphatidylinositol 3-Kinase for Ubiquitination in T Cells

Fang, D., Wang, H.-Y., Fang, N., Altman, Y., Elly, C., & Liu, Y. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008901200 · Cited by 198 · see citing works

Tyrosine Phosphorylation of the c-cbl Proto-oncogene Protein Product and Association with Epidermal Growth Factor (EGF) Receptor upon EGF Stimulation

Galisteo, M. L., Đikić, I., Batzer, A., Langdon, W. Y., & Schlessinger, J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.35.20242 · Cited by 198 · see citing works

Cloning and characterization of cbl-b: a SH3 binding protein with homology to the c-cbl proto-oncogene.

Keane, M. M., Rivero-Lezcano, O. M., Mitchell, J. A., Robbins, K. C., & Lipkowitz, S. (1995) · PubMed · Cited by 182 · see citing works

Direct interaction of Cbl with pTyr 1045 of the EGF receptor (EGFR) is required to sort the EGFR to lysosomes for degradation

Grøvdal, L. M., Stang, E., Sorkin, A. D., & Madshus, I. H. (2004) · Experimental Cell Research · doi:10.1016/j.yexcr.2004.07.003 · Cited by 182 · see citing works

Regulation of ZAP-70 Activation and TCR Signaling by Two Related Proteins, Sts-1 and Sts-2

Carpino, N., Turner, S., Mekala, D. J., Takahashi, Y., Zang, H., Geiger, T. L., Doherty, P. C., & Ihle, J. N. (2004) · Immunity · doi:10.1016/s1074-7613(03)00351-0 · Cited by 169 · see citing works

APS Facilitates c-Cbl Tyrosine Phosphorylation and GLUT4 Translocation in Response to Insulin in 3T3-L1 Adipocytes

Liu, J., Kimura, A., Baumann, C. A., & Saltiel, A. R. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.11.3599-3609.2002 · Cited by 169 · see citing works

Cbl Promotes Ubiquitination of the T Cell Receptor ζ through an Adaptor Function of Zap-70

Wang, H.-Y., Altman, Y., Fang, D., Elly, C., Dai, Y., Shao, Y., & Liu, Y. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010738200 · Cited by 168 · see citing works

Epidermal growth factor receptor signaling intensity determines intracellular protein interactions, ubiquitination, and internalization

Schmidt, M. H. H., Furnari, F. B., Cavenee, W. K., & Bögler, O. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1031790100 · Cited by 164 · see citing works

Complexes of Focal Adhesion Kinase (FAK) and Crk-associated Substrate (p130Cas) Are Elevated in Cytoskeleton-associated Fractions following Adhesion and Src Transformation

Polte, T. R., & Hanks, S. K. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.9.5501 · Cited by 164 · see citing works

Tyrosine Phosphorylation and Translocation of the c-Cbl Protein after Activation of Tyrosine Kinase Signaling Pathways

Tanaka, S., Neff, L., Baron, R., & Levy, J. B. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.24.14347 · Cited by 163 · see citing works

WW Domain HECT E3s Target Cbl RING Finger E3s for Proteasomal Degradation

Magnifico, A., Ettenberg, S. A., Yang, C., Mariano, J. M., Tiwari, S., Fang, S., Lipkowitz, S., & Weissman, A. M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308009200 · Cited by 161 · see citing works

Tyrosine Phosphorylation of Cbl upon Epidermal Growth Factor (EGF) Stimulation and Its Association with EGF Receptor and Downstream Signaling Proteins

Fukazawa, T., Miyake, S., Band, V., & Band, H. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.24.14554 · Cited by 161 · see citing works

Fyn, Yes, and Syk Phosphorylation Sites in c-Cbl Map to the Same Tyrosine Residues That Become Phosphorylated in Activated T Cells

Feshchenko, E. A., Langdon, W. Y., & Tsygankov, A. Y. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.14.8323 · Cited by 160 · see citing works

Coupling of the c-Cbl protooncogene product to ErbB-1/EGF-receptor but not to other ErbB proteins.

Levkowitz, G., Klapper, L. N., Tzahar, E., Freywald, A., Sela, M., & Yarden, Y. (1996) · PubMed · Cited by 154 · see citing works

sli-1, a negative regulator of let-23-mediated signaling in C. elegans.

Jongeward, G. D., Clandinin, T. R., & Sternberg, P. W. (1995) · Genetics · doi:10.1093/genetics/139.4.1553 · Cited by 149 · see citing works

Tal, a Tsg101-specific E3 ubiquitin ligase, regulates receptor endocytosis and retrovirus buddingPreprint

Amit, I., Yakir, L., Katz, M., Zwang, Y., Marmor, M. D., Citri, A., Shtiegman, K., Alroy, I., Tuvia, S., Reiss, Y., et al. (2004) · Genes & Development · doi:10.1101/gad.294904 · Cited by 148 · see citing works

Suppressors of T-cell Receptor Signaling Sts-1 and Sts-2 Bind to Cbl and Inhibit Endocytosis of Receptor Tyrosine Kinases

Kowanetz, K., Crosetto, N., Haglund, K., Schmidt, M. H. H., Heldin, C.-H., & Dikic, I. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403759200 · Cited by 147 · see citing works

Distinct Tyrosine Phosphorylation Sites in ZAP-70 Mediate Activation and Negative Regulation of Antigen Receptor Function

Kong, G., Dalton, M., Wardenburg, J. B., Straus, D. B., Kurosaki, T., & Chan, A. C. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.9.5026 · Cited by 145 · see citing works

Cbl-b Negatively Regulates B Cell Antigen Receptor Signaling in Mature B Cells through Ubiquitination of the Tyrosine Kinase Syk

Sohn, H. W., Gu, H., & Pierce, S. K. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20021686 · Cited by 142 · see citing works

Negative regulation of PI 3‐kinase by Ruk, a novel adaptor protein

Gout, I. T., Middleton, G., Adu, J., Ninkina, N. N., Дробот, Л. Б., Filonenko, V., Matsuka, G., Davies, A. M., Waterfield, M. D., & Buchman, V. L. (2000) · The EMBO Journal · doi:10.1093/emboj/19.15.4015 · Cited by 142 · see citing works

Src promotes destruction of c-Cbl: Implications for oncogenic synergy between Src and growth factor receptors

Bao, J., Gur, G., & Yarden, Y. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0437945100 · Cited by 136 · see citing works

The non‐receptor tyrosine kinase Syk is a target of Cbl‐mediated ubiquitylation upon B‐cell receptor stimulation

Rao, N., Ghosh, A. K., Ota, S., Zhou, P., Reddi, A. L., Hakezi, K., Druker, B. J., Wu, J., & Band, H. (2001) · The EMBO Journal · doi:10.1093/emboj/20.24.7085 · Cited by 135 · see citing works

Serine Phosphorylation of Cbl Induced by Phorbol Ester Enhances Its Association with 14-3-3 Proteins in T Cells via a Novel Serine-rich 14-3-3-binding Motif

Liu, Y., Liu, Y., Elly, C., Yoshida, H., Lipkowitz, S., & Altman, A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.15.9979 · Cited by 135 · see citing works

CIN85 Associates with Multiple Effectors Controlling Intracellular Trafficking of Epidermal Growth Factor Receptors

Kowanetz, K., Husnjak, K., Höller, D., Kowanetz, M., Soubeyran, P., Hirsch, D., Schmidt, M. H. H., Pavelic, K., De Camilli, P., Randazzo, P. A., et al. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-09-0683 · Cited by 128 · see citing works

Activation of R-Ras by Ras-Guanine Nucleotide-releasing Factor

Gotoh, T., Niino, Y. S., Tokuda, M., Hatase, O., Nakamura, S., Matsuda, M., & Hattori, S. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.30.18602 · Cited by 125 · see citing works

Alix/AIP1 Antagonizes Epidermal Growth Factor Receptor Downregulation by the Cbl-SETA/CIN85 Complex

Schmidt, M. H. H., Hoeller, D., Yu, J., Furnari, F. B., Cavenee, W. K., Đikić, I., & Bögler, O. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.20.8981-8993.2004 · Cited by 121 · see citing works

cbl-3: a new mammalian cbl family protein

Keane, M., Ettenberg, S. A., Nau, M. M., Banerjee, P., Cuello, M. A., Penninger, J. M., & Lipkowitz, S. (1999) · Oncogene · doi:10.1038/sj.onc.1202753 · Cited by 120 · see citing works

Coordinated Regulation of the Tyrosine Phosphorylation of Cbl by Fyn and Syk Tyrosine Kinases

Deckert, M., Elly, C., Altman, A., & Liu, Y. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.15.8867 · Cited by 116 · see citing works

A Role for CAP, a Novel, Multifunctional Src Homology 3 Domain-containing Protein in Formation of Actin Stress Fibers and Focal Adhesions

Ribon, V., Herrera, R., Kay, B. K., & Saltiel, A. R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.7.4073 · Cited by 116 · see citing works

Phosphotyrosine Binding Domain-Dependent Upregulation of the Platelet-Derived Growth Factor Receptor α Signaling Cascade by Transforming Mutants of Cbl: Implications for Cbl’s Function and Oncogenicity

Bonita, D. P., Miyake, S., Lupher, M., Langdon, W. Y., & Band, H. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.8.4597 · Cited by 114 · see citing works

Scaffolding of antigen receptors for immunogenic versus tolerogenic signaling

Jun, J. E., & Goodnow, C. C. (2003) · Nature Immunology · doi:10.1038/ni1001 · Cited by 106 · see citing works

SETA/CIN85/Ruk and its binding partner AIP1 associate with diverse cytoskeletal elements, including FAKs, and modulate cell adhesion

Schmidt, M. H. H., Chen, B., Randazzo, L., & Bögler, O. (2003) · Journal of Cell Science · doi:10.1242/jcs.00522 · Cited by 104 · see citing works

Cbl signaling networks in the regulation of cell function

Đikić, I., Szymkiewicz, I., & Soubeyran, P. (2003) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-003-3029-4 · Cited by 96 · see citing works

Coupling of the Proto-oncogene Product c-Cbl to the Epidermal Growth Factor Receptor

Meisner, H. M., & Czech, M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.43.25332 · Cited by 96 · see citing works

Compartmentalization of growth factor receptor signalling

Hoeller, D., Volarević, S., & Đikić, I. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.01.001 · Cited by 95 · see citing works

Recruitment of Pyk2 and Cbl to lipid rafts mediates signals important for actin reorganization in growing neurites

Haglund, K., Ivanković-Dikić, I., Shimokawa, N., Kruh, G. D., & Đikić, I. (2004) · Journal of Cell Science · doi:10.1242/jcs.01148 · Cited by 95 · see citing works

The Proto-oncogene Product p120 Links c-Src and Phosphatidylinositol 3′-Kinase to the Integrin Signaling Pathway

Ojaniemi, M., Martin, S. S., Dolfi, F., Olefsky, J. M., & Vuori, K. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.6.3780 · Cited by 91 · see citing works

20 years of Ins(1,4,5)P3, and 40 years before

Irvine, R. F. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1152 · Cited by 89 · see citing works

Cbl-b interacts with ubiquitinated proteins; differential functions of the UBA domains of c-Cbl and Cbl-b

Davies, G., Ettenberg, S. A., Coats, A. O., Mussante, M., Ravichandran, S., Collins, J., Nau, M. M., & Lipkowitz, S. (2004) · Oncogene · doi:10.1038/sj.onc.1207952 · Cited by 89 · see citing works

Physical and functional association of the cbl protooncogen product with an src-family protein tyrosine kinase, p53/56lyn, in the B cell antigen receptor-mediated signaling.

Tezuka, T., Umemori, H., Fusaki, N., Yagi, T., Takata, M., Kurosaki, T., & Yamamoto, T. S. (1996) · The Journal of Experimental Medicine · doi:10.1084/jem.183.2.675 · Cited by 87 · see citing works

TULA: an SH3- and UBA-containing protein that binds to c-Cbl and ubiquitin

Feshchenko, E. A., Smirnova, E. V., Swaminathan, G., Teckchandani, A. M., Agrawal, R., Band, H., Zhang, X., Annan, R. S., Carr, S. A., & Tsygankov, A. Y. (2004) · Oncogene · doi:10.1038/sj.onc.1207627 · Cited by 86 · see citing works

Cbl Suppresses B Cell Receptor–Mediated Phospholipase C (Plc)-γ2 Activation by Regulating B Cell Linker Protein–Plc-γ2 Binding

Yasuda, T., Maeda, A., Kurosaki, M., Tezuka, T., Hironaka, K., Yamamoto, T. S., & Kurosaki, T. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.191.4.641 · Cited by 86 · see citing works

The Adapter Type Protein CMS/CD2AP Binds to the Proto-oncogenic Protein c-Cbl through a Tyrosine Phosphorylation-regulated Src Homology 3 Domain Interaction

Kirsch, K. H., Georgescu, M.-M., Shishido, T., Langdon, W. Y., Birge, R. B., & Hanafusa, H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m005784200 · Cited by 85 · see citing works

Characterization of the CIN85 Adaptor Protein and Identification of Components Involved in CIN85 Complexes

Watanabe, S., Take, H., Takeda, K., Yu, Z., Iwata, N., & Kajigaya, S. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3760 · Cited by 81 · see citing works

SLAP, a dimeric adapter protein, plays a functional role in T cell receptor signaling

Tang, J., Sawasdikosol, S., Chang, J., & Burakoff, S. J. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.17.9775 · Cited by 78 · see citing works

The protein product of the c-cbl oncogene rapidly complexes with the EGF receptor and is tyrosine phosphorylated following EGF stimulation.

Bowtell, D. D. L., & Langdon, W. Y. (1995) · PubMed · Cited by 78 · see citing works

c-Cbl localizes to actin lamellae and regulates lamellipodia formation and cell morphology

Scaife, R. M., & Langdon, W. Y. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.2.215 · Cited by 77 · see citing works

Src Phosphorylation of Alix/AIP1 Modulates Its Interaction with Binding Partners and Antagonizes Its Activities

Schmidt, M. H. H., Dikic, I., & Bögler, O. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m409839200 · Cited by 76 · see citing works

Sprouty2 acts at the Cbl/CIN85 interface to inhibit epidermal growth factor receptor downregulation

Haglund, K., Schmidt, M. H. H., Wong, E. S. M., Guy, G. R., & Đikić, I. (2005) · EMBO Reports · doi:10.1038/sj.embor.7400453 · Cited by 70 · see citing works

Cbl-ArgBP2 complex mediates ubiquitination and degradation of c-Abl

Soubeyran, P., Barac, A., Szymkiewicz, I., & Đikić, I. (2003) · Biochemical Journal · doi:10.1042/bj20021539 · Cited by 69 · see citing works

Cbl-mediated Ubiquitinylation and Negative Regulation of Vav

Miura-Shimura, Y., Duan, L., Rao, N. L., Reddi, A. L., Shimura, H., Rottapel, R. K., Druker, B. J., Tsygankov, A. Y., Band, V., & Band, H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305656200 · Cited by 62 · see citing works

Molecular controls of antigen receptor clustering and autoimmunity

Krawczyk, C. M., & Penninger, J. M. (2001) · Trends in Cell Biology · doi:10.1016/s0962-8924(01)01981-x · Cited by 61 · see citing works

Molecular cloning and characterization of a novel cbl-family gene, cbl-c

Kim, M., Tezuka, T., Suziki, Y., Sugano, S., Hirai, M., & Yamamoto, T. S. (1999) · Gene · doi:10.1016/s0378-1119(99)00356-x · Cited by 60 · see citing works

Regulation of β1-integrin-mediated cell adhesion by the CbI adaptor protein

Zell, T., Warden, C. S., Chan, A. S. H., Cook, M. E., Dell, C. L., Hunt, S. W., & Shimizu, Y. (1998) · Current Biology · doi:10.1016/s0960-9822(98)70323-9 · Cited by 56 · see citing works

Cbl-b Positively Regulates Btk-mediated Activation of Phospholipase C-γ2 in B Cells

Yasuda, T., Tezuka, T., Maeda, A., Inazu, T., Yamanashi, Y., Gu, H., Kurosaki, T., & Yamamoto, T. S. (2002) · The Journal of Experimental Medicine · doi:10.1084/jem.20020068 · Cited by 53 · see citing works

Cbl-3-Deficient Mice Exhibit Normal Epithelial Development

Griffiths, E. K., Sanchez, O. H., Mill, P., Krawczyk, C. M., Hojilla, C. V., Rubin, E., Nau, M. M., Khokha, R., Lipkowitz, S., Hui, C., et al. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.21.7708-7718.2003 · Cited by 53 · see citing works

p210BCR/ABL induces formation of complexes containing focal adhesion proteins and the protooncogene product p120c-Cbl.

Salgia, R., Sattler, M., Pisick, E. P., Li, J., & Griffin, J. D. (1996) · PubMed · Cited by 53 · see citing works

A Mouse with a Loss-of-function Mutation in the c-Cbl TKB Domain Shows Perturbed Thymocyte Signaling without Enhancing the Activity of the ZAP-70 Tyrosine Kinase

Thien, C. B. F., Scaife, R. M., Papadimitriou, J. M., Murphy, M. A., Bowtell, D. D. L., & Langdon, W. Y. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20021498 · Cited by 50 · see citing works

Receptor endocytosis via ubiquitin-dependent and -independent pathways

Holler, D. A., & Đikić, I. (2004) · Biochemical Pharmacology · doi:10.1016/j.bcp.2004.01.003 · Cited by 45 · see citing works

Phosphorylation- and Activation-independent Association of the Tyrosine Kinase Syk and the Tyrosine Kinase Substrates Cbl and Vav with Tubulin in B-Cells

Fernandez, J. A., Keshvara, L. M., Peters, J. D., Furlong, M. T., Harrison, M. L., & Geahlen, R. L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.3.1401 · Cited by 43 · see citing works

Protein Kinase C Activation Inhibits Tyrosine Phosphorylation of Cbl and Its Recruitment of Src Homology 2 Domain-Containing Proteins

Liu, Y., Liu, Y., Meller, N., Giampa, L., Elly, C., Doyle, M., & Altman, A. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.162.12.7095 · Cited by 40 · see citing works

The cbl oncogene: a novel substrate of protein tyrosine kinases

Langdon, W. Y. (1995) · Australian and New Zealand Journal of Medicine · doi:10.1111/j.1445-5994.1995.tb02892.x · Cited by 39 · see citing works

The multi-adaptor proto-oncoprotein Cbl is a key regulator of Rac and actin assembly

Scaife, R. M., Courtneidge, S. A., & Langdon, W. Y. (2002) · Journal of Cell Science · doi:10.1242/jcs.00244 · Cited by 35 · see citing works

Rapid Microtubule-dependent Induction of Neurite-like Extensions in NIH 3T3 Fibroblasts by Inhibition of ROCK and Cbl

Scaife, R. M., Job, D., & Langdon, W. Y. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-11-0739 · Cited by 32 · see citing works

Interaction of thec-cblProto-oncogene Product with the Tyk-2 Protein Tyrosine Kinase

Shahab Uddin, M. S., Gardziola, C., Dangat, A., Yi, T., & Platanias, L. C. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.1259 · Cited by 31 · see citing works

Adaptor proteins in lymphocyte activation

Janssen, E., & Zhang, W. (2003) · Current Opinion in Immunology · doi:10.1016/s0952-7915(03)00044-x · Cited by 30 · see citing works

Tyrosine phosphorylation of the product of the c-cbl protooncogene is [corrected] induced after integrin stimulation.

Manié, S. N., Sattler, M., Astier, A., Phifer, J. S., Canty, T., Morimoto, C., Druker, B. J., Salgia, R., Griffin, J. D., & Freedman, A. S. (1997) · PubMed · Cited by 29 · see citing works

LET‐23‐mediated signal transduction during Caenorhabditis elegans development

Sternberg, P. W., Lesa, G. M., Lee, J., Katz, W. S., Yoon, C. H., Clandinin, T. R., Huang, L. S., Chamberlin, H., & Jongeward, G. D. (1995) · Molecular Reproduction and Development · doi:10.1002/mrd.1080420422 · Cited by 28 · see citing works

SLP-76-Cbl-Grb2-Shc Interactions in FcγRI Signaling

Chu, J., Liu, Y., Koretzky, G. A., & Durden, D. L. (1998) · Blood · doi:10.1182/blood.v92.5.1697 · Cited by 25 · see citing works

Cbl Competitively Inhibits Epidermal Growth Factor-induced Activation of Phospholipase C-γ1

Choi, J. H., Bae, S. S., Park, J. B., Ha, S. H., Song, H., Kim, J. H., Cocco, L., Ryu, S. H., & Suh, P. (2003) · Molecules and Cells · doi:10.1016/s1016-8478(23)13734-4 · Cited by 17 · see citing works

Membrane traffic: Cycling lipids

Stenmark, H. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00279-7 · Cited by 17 · see citing works

Requirements for pYXXM Motifs in Cbl for Binding to the p85 Subunit of Phosphatidylinositol 3-Kinase and Crk, and Activation of Atypical Protein Kinase C and Glucose Transport during Insulin Action in 3T3/L1 Adipocytes

Standaert, M. L., Sajan, M. P., Miura, A., Bandyopadhyay, G. K., & Farese, R. V. (2004) · Biochemistry · doi:10.1021/bi049222q · Cited by 16 · see citing works

Cbl PYXXM Motifs Activate the P85 Subunit of Phosphatidylinositol 3-Kinase, Crk, Atypical Protein Kinase C, and Glucose Transport during Thiazolidinedione Action in 3T3/L1 and Human Adipocytes

Miura, A., Sajan, M. P., Standaert, M. L., Bandyopadhyay, G. K., Franklin, D. M., Lea-Currie, R., & Farese, R. V. (2003) · Biochemistry · doi:10.1021/bi034808i · Cited by 11 · see citing works

70Z/3 Cbl induces PLCγ1 activation in T lymphocytes via an alternate Lat- and Slp-76-independent signaling mechanism

Graham, L. J., Verı́, M.-C., DeBell, K. E., Noviello, C., Rawat, R., Jen, S., Bonvini, E., & Rellahan, B. L. (2003) · Oncogene · doi:10.1038/sj.onc.1206318 · Cited by 7 · see citing works

Erratum: TULA: an SH3- and UBA-containing protein that binds to c-Cbl and ubiquitin

Feshchenko, E. A., Smirnova, E. V., Swaminathan, G., Teckchandani, A. M., Agrawal, R., Band, H., Zhang, X., Annan, R. S., Carr, S. A., & Tsygankov, A. Y. (2004) · Oncogene · doi:10.1038/sj.onc.1208320 · Cited by 1 · see citing works

Ubiquitination in disease pathogenesis and treatment

Popovic, D., Vucic, D., & Đikić, I. (2014) · Nature Medicine · doi:10.1038/nm.3739 · Cited by 1,405 · see citing works

Post-translational modifications in signal integration

Deribe, Y. L., Pawson, T., & Dikic, I. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1842 · Cited by 876 · see citing works

Ubiquitin-Binding Proteins: Decoders of Ubiquitin-Mediated Cellular Functions

Husnjak, K., & Đikić, I. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-051810-094654 · Cited by 755 · see citing works

Protein posttranslational modifications in health and diseases: Functions, regulatory mechanisms, and therapeutic implications

Zhong, Q., Xiao, X., Qiu, Y., Xu, Z., Chen, C., Chong, B., Zhao, X., Hai, S., Li, S., An, Z., et al. (2023) · MedComm · doi:10.1002/mco2.261 · Cited by 442 · see citing works

Noonan syndrome and clinically related disorders

Tartaglia, M., Gelb, B. D., & Zenker, M. (2011) · Best Practice & Research Clinical Endocrinology & Metabolism · doi:10.1016/j.beem.2010.09.002 · Cited by 420 · see citing works

Fibroblast growth factor signaling in skeletal development and diseasePreprint

Ornitz, D. M., & Marie, P. J. (2015) · Genes & Development · doi:10.1101/gad.266551.115 · Cited by 419 · see citing works

RINGs of good and evil: RING finger ubiquitin ligases at the crossroads of tumour suppression and oncogenesis

Lipkowitz, S., & Weissman, A. M. (2011) · Nature reviews. Cancer · doi:10.1038/nrc3120 · Cited by 415 · see citing works

Ubiquitin and ubiquitin-like proteins in cancer pathogenesis

Hoeller, D., Hecker, C.-M., & Đikić, I. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1994 · Cited by 409 · see citing works

Gain-of-function of mutated C-CBL tumour suppressor in myeloid neoplasms

Sanada, M., Suzuki, T., Shih, L., Otsu, M., Kato, M., Yamazaki, S., Tamura, A., Honda, H., Sakata‐Yanagimoto, M., Kumano, K., et al. (2009) · Nature · doi:10.1038/nature08240 · Cited by 401 · see citing works

New mutations and pathogenesis of myeloproliferative neoplasms

Vainchenker, W., Delhommeau, F., Constantinescu, S. N., & Bernard, O. (2011) · Blood · doi:10.1182/blood-2011-02-292102 · Cited by 395 · see citing works

Frequent CBL mutations associated with 11q acquired uniparental disomy in myeloproliferative neoplasms

Grand, F., Hidalgo-Curtis, C., Ernst, T., Zoi, K., Zoi, C., McGuire, C., Kreil, S., Jones, A. V., Score, J., Metzgeroth, G., et al. (2009) · Blood · doi:10.1182/blood-2008-12-194548 · Cited by 379 · see citing works

The switchable integrin adhesome

Zaidel‐Bar, R., & Geiger, B. (2010) · Journal of Cell Science · doi:10.1242/jcs.066183 · Cited by 350 · see citing works

The role of ubiquitylation in receptor endocytosis and endosomal sorting

Haglund, K., & Đikić, I. (2012) · Journal of Cell Science · doi:10.1242/jcs.091280 · Cited by 310 · see citing works

Gastric cancer exosomes promote tumour cell proliferation through PI3K/Akt and MAPK/ERK activation

Qu, J.-L., Qu, X.-J., Zhao, M.-F., Teng, Y.-E., Zhang, Y., Hou, K., Jiang, Y.-H., Yang, X., & Liu, Y.-P. (2009) · Digestive and Liver Disease · doi:10.1016/j.dld.2009.04.006 · Cited by 303 · see citing works

The Cbl family proteins: Ring leaders in regulation of cell signaling

Swaminathan, G., & Tsygankov, A. Y. (2006) · Journal of Cellular Physiology · doi:10.1002/jcp.20694 · Cited by 289 · see citing works

Mutations in CBL occur frequently in juvenile myelomonocytic leukemia

Loh, M. L., Sakai, D. S., Flotho, C., Kang, M. W., Fliegauf, M., Archambeault, S., Mullighan, C. G., Chen, L., Bergsträßer, E., Bueso-Ramos, C., et al. (2009) · Blood · doi:10.1182/blood-2009-01-198416 · Cited by 287 · see citing works

Induction of Siglec-G by RNA Viruses Inhibits the Innate Immune Response by Promoting RIG-I Degradation

Chen, W., Han, C., Xie, B., Hu, X., Yu, Q., Shi, L., Wang, Q., Li, D., Wang, J., Zheng, P., et al. (2013) · Cell · doi:10.1016/j.cell.2013.01.011 · Cited by 274 · see citing works

Heterozygous germline mutations in the CBL tumor-suppressor gene cause a Noonan syndrome-like phenotype

Martinelli, S., De Luca, A., Stellacci, E., Rossi, C., Checquolo, S., Lepri, F., Caputo, V., Silvano, M., Buscherini, F., Consoli, F., et al. (2010) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2010.06.015 · Cited by 259 · see citing works

Protein interaction screening by quantitative immunoprecipitation combined with knockdown (QUICK)

Selbach, M., & Mann, M. (2006) · Nature Methods · doi:10.1038/nmeth972 · Cited by 240 · see citing works

Mutations of E3 Ubiquitin Ligase Cbl Family Members Constitute a Novel Common Pathogenic Lesion in Myeloid Malignancies

Makishima, H., Cazzolli, H., Szpurka, H., Dunbar, A. J., Tiu, R. V., Huh, J., Muramatsu, H., O’Keefe, C. L., Hsi, E. D., PAQUETTE, R. L., et al. (2009) · Journal of Clinical Oncology · doi:10.1200/jco.2009.23.7503 · Cited by 219 · see citing works

14-3-3 proteins as potential oncogenes

Tzivion, G., Gupta, V. S., Kaplun, L., & Balan, V. (2006) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2006.03.004 · Cited by 218 · see citing works

Flt3-dependent transformation by inactivating c-Cbl mutations in AML

Sargin, B., Choudhary, C., Crosetto, N., Schmidt, M. H. H., Grundler, R., Rensinghoff, M., Thiessen, C., Tickenbrock, L., Schwäble, J., Brandts, C., et al. (2007) · Blood · doi:10.1182/blood-2007-01-066076 · Cited by 216 · see citing works

Integrative Survival-Based Molecular Profiling of Human Pancreatic Cancer

Donahue, T. R., Tran, L. M., Hill, R., Li, Y., Kovochich, A., Calvopina, J. H., Patel, S. G., Wu, N., Hindoyan, A. A., Farrell, J. J., et al. (2012) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-11-1539 · Cited by 212 · see citing works

Structural basis for autoinhibition and phosphorylation-dependent activation of c-Cbl

Dou, H., Buetow, L., Hock, A., Sibbet, G. J., Vousden, K. H., & Huang, D. T. C. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2231 · Cited by 211 · see citing works

H19non coding RNA-derived miR-675 enhances tumorigenesis and metastasis of breast cancer cells by downregulating c-Cbl and Cbl-b

Vennin, C., Spruyt, N., Dahmani, F. Z., Julien, S., Bertucci, F., Finetti, P., Chassat, T., Bourette, R. P., Bourhis, X. L., & Adriaenssens, É. (2015) · Oncotarget · doi:10.18632/oncotarget.4976 · Cited by 202 · see citing works

Intra-endosomal membrane traffic

van der Goot, F. G., & Grüenberg, J. (2006) · Trends in Cell Biology · doi:10.1016/j.tcb.2006.08.003 · Cited by 196 · see citing works

When ubiquitination meets phosphorylation: a systems biology perspective of EGFR/MAPK signalling

Nguyen, L. K., Kölch, W., & Kholodenko, B. Ν. (2013) · Cell Communication and Signaling · doi:10.1186/1478-811x-11-52 · Cited by 192 · see citing works

Threshold‐controlled ubiquitination of the EGFR directs receptor fate

Sigismund, S., Algisi, V., Nappo, G., Conte, A., Pascolutti, R., Cuomo, A., Bonaldi, T., Argenzio, E., Verhoef, L. G. G. C., Maspero, E., et al. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.149 · Cited by 172 · see citing works

Recent advances in the pathogenesis and treatment of juvenile myelomonocytic leukaemia

Loh, M. L. (2011) · British Journal of Haematology · doi:10.1111/j.1365-2141.2010.08525.x · Cited by 159 · see citing works

c-Cbl-Mediated Neddylation Antagonizes Ubiquitination and Degradation of the TGF-β Type II Receptor

Zuo, W., Huang, F., Chiang, Y. J., Li, M., Du, J. C., Ding, Y., Zhang, T., Lee, H. W., Jeong, L. S., Chen, Y., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2012.12.002 · Cited by 157 · see citing works

Molecular Mechanisms of SH2- and PTB-Domain-Containing Proteins in Receptor Tyrosine Kinase SignalingPreprint

Wagner, M. J., Stacey, M. M., Liu, B. A., & Pawson, T. J. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008987 · Cited by 155 · see citing works

Molecular Basis of Signaling Specificity of Insulin and IGF Receptors: Neglected Corners and Recent Advances

Siddle, K. (2012) · Frontiers in Endocrinology · doi:10.3389/fendo.2012.00034 · Cited by 154 · see citing works

Germline mutations of the CBL gene define a new genetic syndrome with predisposition to juvenile myelomonocytic leukaemia

Perez, B., Mechinaud, F. M., Galambrun, C., Romdhane, N. B., Isidor, B., Philip, N., Derain-Court, J., Cassinat, B., Lachenaud, J., Kaltenbach, S., et al. (2010) · Journal of Medical Genetics · doi:10.1136/jmg.2010.076836 · Cited by 149 · see citing works

miR-216a rescues dexamethasone suppression of osteogenesis, promotes osteoblast differentiation and enhances bone formation, by regulating c-Cbl-mediated PI3K/AKT pathway

Li, H., Li, T., Fan, J., Li, T., Fan, L., Wang, S., Weng, X., Han, Q., & Zhao, R. C. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2015.99 · Cited by 139 · see citing works

Sprouty proteins: modified modulators, matchmakers or missing links?

Guy, G. R., Jackson, R. A., Yusoff, P., & Chow, S. Y. (2009) · Journal of Endocrinology · doi:10.1677/joe-09-0110 · Cited by 128 · see citing works

The Roles of the Ubiquitin–Proteasome System in the Endoplasmic Reticulum Stress Pathway

Qu, J., Zou, T., & Lin, Z. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22041526 · Cited by 128 · see citing works

Proteostatic and Metabolic Control of Stemness

García‐Prat, L., Sousa‐Victor, P., & Muñoz‐Cánoves, P. (2017) · Cell stem cell · doi:10.1016/j.stem.2017.04.011 · Cited by 123 · see citing works

Mutations of an E3 ubiquitin ligase c-Cbl but not TET2 mutations are pathogenic in juvenile myelomonocytic leukemia

Muramatsu, H., Makishima, H., Jankowska, A. M., Cazzolli, H., O’Keefe, C. L., Yoshida, N., Xu, Y., Nishio, N., Hama, A., Yagasaki, H., et al. (2009) · Blood · doi:10.1182/blood-2009-06-226340 · Cited by 115 · see citing works

The E3 ubiquitin ligase c-Cbl restricts development and functions of hematopoietic stem cellsPreprint

Rathinam, C., Thien, C. B. F., Langdon, W. Y., Gu, H., & Flavell, R. A. (2008) · Genes & Development · doi:10.1101/gad.1651408 · Cited by 114 · see citing works

Bedside to bench in juvenile myelomonocytic leukemia: insights into leukemogenesis from a rare pediatric leukemia

Chang, T. Y., Dvorak, C. C., & Loh, M. L. (2014) · Blood · doi:10.1182/blood-2014-03-300319 · Cited by 109 · see citing works

Ubc4/5 and c-Cbl Continue to Ubiquitinate EGF Receptor after Internalization to Facilitate Polyubiquitination and Degradation

Umebayashi, K., Stenmark, H., & Yoshimori, T. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-10-0988 · Cited by 108 · see citing works

Kaposi’s sarcoma-associated herpesvirus interacts with EphrinA2 receptor to amplify signaling essential for productive infection

Chakraborty, S., Veettil, M. V., Bottero, V., & Chandran, B. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1119592109 · Cited by 105 · see citing works

A Restricted Spectrum of Mutations in the SMAD4 Tumor-Suppressor Gene Underlies Myhre Syndrome

Caputo, V., Cianetti, L., Niceta, M., Carta, C., Ciolfi, A., Bocchinfuso, G., Carrani, E., Dentici, M. L., Biamino, E., Belligni, E. F., et al. (2012) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2011.12.011 · Cited by 105 · see citing works

Neutrophil activation via β2 integrins (CD11/CD18): Molecular mechanisms and clinical implications

Schymeinsky, J., Mócsai, A., & Walzog, B. (2007) · Thrombosis and Haemostasis · doi:10.1160/th07-02-0156 · Cited by 103 · see citing works

Abl Tyrosine Kinase Regulates Endocytosis of the Epidermal Growth Factor Receptor

Tanos, B. E., & Pendergast, A. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603126200 · Cited by 103 · see citing works

Molecular Pathways: Cbl Proteins in Tumorigenesis and Antitumor Immunity—Opportunities for Cancer Treatment

Liyasova, M., Ma, K., & Lipkowitz, S. (2014) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-13-2490 · Cited by 102 · see citing works

miR-124-3p functions as a tumor suppressor in breast cancer by targeting CBL

Wang, Y., Chen, L., Wu, Z., Wang, M., Jin, F., Wang, N., Hu, X., Liu, Z., Zhang, C., Zen, K., et al. (2016) · BMC Cancer · doi:10.1186/s12885-016-2862-4 · Cited by 102 · see citing works

Genetic predispositions to childhood leukemia

Stieglitz, E., & Loh, M. L. (2013) · Therapeutic Advances in Hematology · doi:10.1177/2040620713498161 · Cited by 101 · see citing works

Myeloid Leukemia Development in c-Cbl RING Finger Mutant Mice Is Dependent on FLT3 Signaling

Rathinam, C., Thien, C. B. F., Flavell, R. A., & Langdon, W. Y. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.09.008 · Cited by 99 · see citing works

Essential Role of E3 Ubiquitin Ligase Activity in Cbl-b–Regulated T Cell Functions

Paolino, M., Thien, C. B. F., Gruber, T., Hinterleitner, R., Baier, G., Langdon, W. Y., & Penninger, J. M. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1003390 · Cited by 98 · see citing works

Kaposi’s Sarcoma Associated Herpesvirus Entry into Target Cells

Chakraborty, S., Veettil, M. V., & Chandran, B. (2012) · Frontiers in Microbiology · doi:10.3389/fmicb.2012.00006 · Cited by 94 · see citing works

Quiescence Entry, Maintenance, and Exit in Adult Stem Cells

Mohammad, K., Dakik, P., Medkour, Y., Mitrofanova, D., & Titorenko, V. I. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20092158 · Cited by 90 · see citing works

Modulation of Immune Cell Functions by the E3 Ligase Cbl-b

Lutz‐Nicoladoni, C., Wolf, D. G. F., & Sopper, S. (2015) · Frontiers in Oncology · doi:10.3389/fonc.2015.00058 · Cited by 90 · see citing works

Chemically Diverse Toxicants Converge on Fyn and c-Cbl to Disrupt Precursor Cell Function

Li, Z., Dong, T., Pröschel, C., & Noble, M. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050035 · Cited by 90 · see citing works

The Multiple Layers of Ubiquitin-Dependent Cell Cycle Control

Wickliffe, K. E., Williamson, A. P., Jin, L., & Rapé, M. (2009) · Chemical Reviews · doi:10.1021/cr800414e · Cited by 89 · see citing works

Interaction of KSHV with Host Cell Surface Receptors and Cell Entry

Veettil, M. V., Bandyopadhyay, C., Dutta, D., & Chandran, B. (2014) · Viruses · doi:10.3390/v6104024 · Cited by 83 · see citing works

c-Cbl-Dependent Monoubiquitination and Lysosomal Degradation of gp130

Tanaka, Y., Tanaka, N., Saeki, Y., Tanaka, K., Murakami, M., Hirano, T., Ishii, N., & Sugamura, K. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01784-07 · Cited by 82 · see citing works

EGFR Trafficking in Physiology and Cancer

Caldieri, G., Malabarba, M. G., Fiore, P. P. D., & Sigismund, S. (2018) · Progress in molecular and subcellular biology · doi:10.1007/978-3-319-96704-2_9 · Cited by 80 · see citing works

Quantitative analysis reveals how EGFR activation and downregulation are coupled in normal but not in cancer cells

Capuani, F., Conte, A., Argenzio, E., Marchetti, L., Priami, C., Polo, S., Fiore, P. P. D., Sigismund, S., & Ciliberto, A. (2015) · Nature Communications · doi:10.1038/ncomms8999 · Cited by 79 · see citing works

Association with HSP90 Inhibits Cbl-Mediated Down-regulation of Mutant Epidermal Growth Factor Receptors

Yang, S., Qu, S., Perez-Tores, M., Sawai, A., Rosen, N. X., Solit, D. B., & Arteaga, C. L. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-1042 · Cited by 79 · see citing works

E3 ubiquitin ligase-mediated regulation of bone formation and tumorigenesis

Sévère, N., Dieudonné, F., & Pj, M. (2013) · Cell Death and Disease · doi:10.1038/cddis.2012.217 · Cited by 79 · see citing works

Ubiquitin-dependent regulation of G protein-coupled receptor trafficking and signaling

Marchese, A., & Trejo, J. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.11.024 · Cited by 78 · see citing works

Cytoplasmic Relaxation of Active Eph Controls Ephrin Shedding by ADAM10

Janes, P. W., Wimmer-Kleikamp, S. H., Frangakis, A. S., Treble, K., Griesshaber, B., Sabet, O., Grabenbauer, M., Ting, A. Y., Säftig, P., Bastiaens, P. I. H., et al. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000215 · Cited by 78 · see citing works

Epigenome-wide association study of rheumatoid arthritis identifies differentially methylated loci in B cells

Julià, A., Absher, D., Lasanta, M. L., Palau, N., Pluma, A., Jones, L. W., Glossop, J. R., Farrell, W. E., Myers, R., & Marsal, S. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx177 · Cited by 77 · see citing works

Genetic and epigenetic alterations of myeloproliferative disorders

Feenstra, J. D. M., & Královics, R. (2012) · International Journal of Hematology · doi:10.1007/s12185-012-1235-2 · Cited by 76 · see citing works

A TNF- and c-Cbl-dependent FLIPS-degradation pathway and its function in Mycobacterium tuberculosis–induced macrophage apoptosis

Kundu, M., Pathak, S. K., Kumawat, K., Basu, S., Chatterjee, G., Pathak, S., Noguchi, T., Takeda, K., Ichijo, H., Thien, C. B. F., et al. (2009) · Nature Immunology · doi:10.1038/ni.1754 · Cited by 74 · see citing works

Bag1 directly routes immature BCR-ABL for proteasomal degradation

Tsukahara, F., & Maru, Y. (2010) · Blood · doi:10.1182/blood-2009-10-249623 · Cited by 73 · see citing works

Interaction of c-Cbl with Myosin IIA Regulates Bleb Associated Macropinocytosis of Kaposi's Sarcoma-Associated Herpesvirus

Veettil, M. V., Sadagopan, S., Kerur, N., Chakraborty, S., & Chandran, B. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1001238 · Cited by 71 · see citing works

From T‐cell activation signals to signaling control of anti‐cancer immunity

Cronin, S. J. F., & Penninger, J. M. (2007) · Immunological Reviews · doi:10.1111/j.1600-065x.2007.00570.x · Cited by 71 · see citing works

c-Cbl targets PD-1 in immune cells for proteasomal degradation and modulates colorectal tumor growth

Lyle, C., Richards, S., Yasuda, K., Napoleon, M. A., Walker, J., Arinze, N. V., Belghasem, M., Vellard, I., Yin, W., Ravid, J. D., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-56208-1 · Cited by 70 · see citing works

Roles of E3 ubiquitin ligases in cell adhesion and migration

Huang, C. (2010) · Cell Adhesion & Migration · doi:10.4161/cam.4.1.9834 · Cited by 70 · see citing works

c-Cbl, a Ubiquitin E3 Ligase That Targets Active β-Catenin

Chitalia, V. C., Shivanna, S., Martorell, J., Meyer, R., Edelman, E. R., & Rahimi, N. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.473801 · Cited by 69 · see citing works

KSHV Entry and Trafficking in Target Cells—Hijacking of Cell Signal Pathways, Actin and Membrane Dynamics

Kumar, B., & Chandran, B. (2016) · Viruses · doi:10.3390/v8110305 · Cited by 69 · see citing works

Non-proteolytic ubiquitylation in cellular signaling and human disease

Liao, Y., Sumara, I., & Pangou, E. (2022) · Communications Biology · doi:10.1038/s42003-022-03060-1 · Cited by 66 · see citing works

Whole-exome analysis reveals novel somatic genomic alterations associated with outcome in immunochemotherapy-treated diffuse large B-cell lymphoma

Novak, A. J., Asmann, Y. W., Maurer, M. J., Wang, C., Slager, S. L., Hodge, L. S., Manske, M. K., Price-Troska, T. L., Yang, Z.-Z., Zimmermann, M. T., et al. (2015) · Blood Cancer Journal · doi:10.1038/bcj.2015.69 · Cited by 66 · see citing works

Structural basis for a novel intrapeptidyl H‐bond and reverse binding of c‐Cbl‐TKB domain substrates

Ng, C., Jackson, R. A., Buschdorf, J. P., Sun, Q., Guy, G. R., & Sivaraman, J. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.18 · Cited by 66 · see citing works

Intersectin Regulates Epidermal Growth Factor Receptor Endocytosis, Ubiquitylation, and Signaling

Martin, N. P., Mohney, R. P., Dunn, S., Das, M., Scappini, E., & O’Bryan, J. P. (2006) · Molecular Pharmacology · doi:10.1124/mol.106.028274 · Cited by 66 · see citing works

Fbxw7 Controls Angiogenesis by Regulating Endothelial Notch Activity

Izumi, N., Helker, C. S., Ehling, M., Behrens, A., Herzog, W., & Adams, R. H. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041116 · Cited by 65 · see citing works

JAK2V617F and beyond: role of genetics and aberrant signaling in the pathogenesis of myeloproliferative neoplasms

Oh, S. T., & Gotlib, J. R. (2010) · Expert Review of Hematology · doi:10.1586/ehm.10.28 · Cited by 65 · see citing works

Ligand-induced EpoR internalization is mediated by JAK2 and p85 and is impaired by mutations responsible for primary familial and congenital polycythemia

Sulahian, R., Cleaver, O. B., & Huang, L. J.-S. (2009) · Blood · doi:10.1182/blood-2008-09-179572 · Cited by 64 · see citing works

CIN85, a Cbl‐interacting protein, is a component of AMAP1‐mediated breast cancer invasion machinery

Nam, J., Onodera, Y., Mazaki, Y., Miyoshi, H., Hashimoto, S., & Sabe, H. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601534 · Cited by 64 · see citing works

UBASH3B/Sts-1-CBL axis regulates myeloid proliferation in human preleukemia induced by AML1-ETO

Goyama, S., Schibler, J., Gasilina, A., Shrestha, M., Lin, S., Link, K. A., Chen, J., Whitman, S. P., Bloomfield, C. D., Nicolet, D., et al. (2015) · Leukemia · doi:10.1038/leu.2015.275 · Cited by 64 · see citing works

Characterization of Multiple Multivesicular Body Sorting Determinants within Sna3: A Role for the Ubiquitin Ligase Rsp5

Oestreich, A. J., Aboian, M., Lee, J. R. E., Azmi, I. F., Payne, J. A., Issaka, R. B., Davies, B. A., & Katzmann, D. J. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-08-0680 · Cited by 64 · see citing works

Clonal Hematopoiesis: Somatic Mutations in Blood Cells and Atherosclerosis

Natarajan, P., Jaiswal, S., & Kathiresan, S. (2018) · Circulation Genomic and Precision Medicine · doi:10.1161/circgen.118.001926 · Cited by 63 · see citing works

Upregulation of E3 Ubiquitin Ligase CBLC Enhances EGFR Dysregulation and Signaling in Lung Adenocarcinoma

Hong, S., Kao, Y.-R., Lee, T., & Wu, C. (2018) · Cancer Research · doi:10.1158/0008-5472.can-17-3858 · Cited by 63 · see citing works

RIN1 orchestrates the activation of RAB5 GTPases and ABL tyrosine kinases to determine the fate of EGFR

Balaji, K., Mooser, C. K., Janson, C., Bliss, J. M., Hojjat, H., & Colicelli, J. (2012) · Journal of Cell Science · doi:10.1242/jcs.113688 · Cited by 61 · see citing works

Cbl-b in T-cell activation

Paolino, M., & Penninger, J. M. (2010) · Seminars in Immunopathology · doi:10.1007/s00281-010-0197-9 · Cited by 60 · see citing works

Molecular basis of juvenile myelomonocytic leukemia

de Vries, A. C. H., Zwaan, C. M., & van den Heuvel‐Eibrink, M. M. (2010) · Haematologica · doi:10.3324/haematol.2009.016865 · Cited by 60 · see citing works

Proteomic snapshot of the EGF‐induced ubiquitin network

Argenzio, E., Bange, T., Oldrini, B., Bianchi, F., Peesari, R., Mari, S., Fiore, P. P. D., Mann, M., & Polo, S. (2011) · Molecular Systems Biology · doi:10.1038/msb.2010.118 · Cited by 59 · see citing works

Advances in the Genetics of High-Risk Childhood B-Progenitor Acute Lymphoblastic Leukemia and Juvenile Myelomonocytic Leukemia: Implications for Therapy

Loh, M. L., & Mullighan, C. G. (2012) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-11-1936 · Cited by 59 · see citing works

INTERSECTINg Pathways in Cell Biology

O’Bryan, J. P. (2010) · Science Signaling · doi:10.1126/scisignal.3152re10 · Cited by 58 · see citing works

Macromolecular juggling by ubiquitylation enzymes

Lorenz, S., Cantor, A. J., Rapé, M., & Kuriyan, J. (2013) · BMC Biology · doi:10.1186/1741-7007-11-65 · Cited by 57 · see citing works

c-Cbl Inhibition Improves Cardiac Function and Survival in Response to Myocardial Ischemia

Rafiq, K., Kolpakov, M. A., Seqqat, R., Guo, J., Guo, X., Zhao, Q., Yu, D., Mohapatra, B. C., Zutshi, N., An, W., et al. (2014) · Circulation · doi:10.1161/circulationaha.113.007004 · Cited by 57 · see citing works

FGFR2-Cbl interaction in lipid rafts triggers attenuation of PI3K/Akt signaling and osteoblast survival

Dufour, C., Guénou, H., Kaabeche, K., Bouvard, D., Sanjay, A., & Marie, P. J. (2008) · Bone · doi:10.1016/j.bone.2008.02.009 · Cited by 56 · see citing works

ANXA1 Binds and Stabilizes EphA2 to Promote Nasopharyngeal Carcinoma Growth and Metastasis

Feng, J., Lu, S., Xiao, T., Huang, W. C., Yi, H. L., Zhu, W., Fan, S., Feng, X., Li, J.-Y., Yu, Z.-Z., et al. (2020) · Cancer Research · doi:10.1158/0008-5472.can-20-0560 · Cited by 56 · see citing works

K63-linked ubiquitin chains are a global signal for endocytosis and contribute to selective autophagy in plants

Saeed, B., Deligne, F., Brillada, C., Dünser, K., Ditengou, F. A., Turek, I., Allahham, A., Grujic, N., Dagdas, Y., Ott, T., et al. (2023) · Current Biology · doi:10.1016/j.cub.2023.02.024 · Cited by 55 · see citing works

Rapidly fatal myeloproliferative disorders in mice with deletion of Casitas B-cell lymphoma (Cbl) and Cbl-b in hematopoietic stem cells

Naramura, M., Nandwani, N., Gu, H., Band, V., & Band, H. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1007575107 · Cited by 55 · see citing works

ESCRT and Membrane Protein Ubiquitination

Migliano, S. M., & Teis, D. (2018) · Progress in molecular and subcellular biology · doi:10.1007/978-3-319-96704-2_4 · Cited by 55 · see citing works

CTEN Prolongs Signaling by EGFR through Reducing Its Ligand-Induced Degradation

Hong, S., Shih, Y.-P., Li, T., Carraway, K. L., & Lo, S. H. (2013) · Cancer Research · doi:10.1158/0008-5472.can-12-4441 · Cited by 54 · see citing works

Ubiquitylation in immune disorders and cancer: from molecular mechanisms to therapeutic implications

Fulda, S., Rajalingam, K., & Đikić, I. (2012) · EMBO Molecular Medicine · doi:10.1002/emmm.201100707 · Cited by 54 · see citing works

Cbl signaling networks in the regulation of cell function

Đikić, I., Szymkiewicz, I., & Soubeyran, P. (2003) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-003-3029-4 · Cited by 96 · see citing works

Regulating the regulator: negative regulation of Cbl ubiquitin ligases

Ryan, P. E., Davies, G., Nau, M. M., & Lipkowitz, S. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2005.12.004 · Cited by 93 · see citing works

Regulation of immune system development and function by Cbl‐mediated ubiquitination

Li, X., Gong, L., & Gu, H. (2019) · Immunological Reviews · doi:10.1111/imr.12789 · Cited by 32 · see citing works

The Cbl family proteins: Ring leaders in regulation of cell signaling

Swaminathan, G., & Tsygankov, A. Y. (2006) · Journal of Cellular Physiology · doi:10.1002/jcp.20694 · Cited by 289 · see citing works

Molecular Pathways: Cbl Proteins in Tumorigenesis and Antitumor Immunity—Opportunities for Cancer Treatment

Liyasova, M., Ma, K., & Lipkowitz, S. (2014) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-13-2490 · Cited by 102 · see citing works