Cited by 395Protein Kinase Regulation and GTPase SignalingUbiquitin and proteasome pathwaysProtein Tyrosine Phosphatases

The DOI matches its Crossref record; 125 of the 126 references it cites were found in a registry or an index.

The Cbl interactome and its functions

Schmidt, Mirko H.H., Dikic, Ivan·2005·Nature Reviews Molecular Cell Biology

DOI 10.1038/nrm1762

Open this paper in CoChat — free account

Abstract

Cbl proteins are ubiquitin ligases and multifunctional adaptor proteins that are implicated in the regulation of signal transduction in various cell types and in response to different stimuli. Cbl-associated proteins can assemble together at a given time or space inside the cell, and such an interactome can form signal competent networks that control many physiological processes. Dysregulation of spatial or temporal constraints in the Cbl interactome results in the development of human pathologies such as immune diseases, diabetes and cancer.

Integrity signals

Registry

Crossref · 10.1038/nrm1762

Cites

125 of 125 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

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
Untangling the ErbB signalling network
Yarden, Y., & Sliwkowski, M. X. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35052073 · Cited by 6,974
Cell Signaling by Receptor Tyrosine Kinases
Schlessinger, J. (2000) · Cell · doi:10.1016/s0092-8674(00)00114-8 · Cited by 3,774
Rab proteins as membrane organizers
Zerial, M., & McBride, H. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35052055 · Cited by 3,381
Mechanisms Underlying Ubiquitination
Pickart, C. M. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.503 · Cited by 3,184
Themes and variations on ubiquitylation
Weissman, A. M. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056563 · Cited by 1,507
Protein regulation by monoubiquitin
Hicke, L. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056583 · Cited by 1,227
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
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
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

Flagged first, then by citations

Show all 126 references

1 of the 126 references couldn’t be matched to a known paper.

Sorted by citations

Items 101–200 of 394

Regulation of stem cell function by protein ubiquitylation
Strikoudis, A., Guillamot, M., & Aifantis, I. (2014) · EMBO Reports · doi:10.1002/embr.201338373 · Cited by 55
High hematocrit as a risk factor for venous thrombosis. Cause or innocent bystander?
Schreijer, A., Reitsma, P. H., & Cannegieter, S. C. (2010) · Haematologica · doi:10.3324/haematol.2009.017285 · Cited by 53
Ataxin-2 Modulates the Levels of Grb2 and Src but Not Ras Signaling
Drost, J., Nonis, D., Eich, F., Leske, O., Damrath, E., Brunt, E. R. P., Lastres‐Becker, I., Heumann, R., Nowock, J., & Auburger, G. W. J. (2013) · Journal of Molecular Neuroscience · doi:10.1007/s12031-012-9949-4 · Cited by 53
Regulation of hematopoietic stem cell fate by the ubiquitin proteasome system
Moran-Crusio, K., Reavie, L. B., & Aifantis, I. (2012) · Trends in Immunology · doi:10.1016/j.it.2012.01.009 · Cited by 55
Chapter 1 Cell and Molecular Biology of Invadopodia
Caldieri, G., Ayala, I., Attanasio, F., & Buccione, R. (2009) · International review of cytology · doi:10.1016/s1937-6448(09)75001-4 · Cited by 54
EphrinA2 Regulates Clathrin Mediated KSHV Endocytosis in Fibroblast Cells by Coordinating Integrin-Associated Signaling and c-Cbl Directed Polyubiquitination
Dutta, D., Chakraborty, S., Bandyopadhyay, C., Veettil, M. V., Ansari, M. A., Singh, V. V., & Chandran, B. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003510 · Cited by 52
Cell Density-Dependent Inhibition of Epidermal Growth Factor Receptor Signaling by p38α Mitogen-Activated Protein Kinase via Sprouty2 Downregulation
Swat, A., Dolado, I., Rojas, J. M., & Nebreda, Á. R. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01955-08 · Cited by 52
c-Cbl Facilitates Endocytosis and Lysosomal Degradation of Cystic Fibrosis Transmembrane Conductance Regulator in Human Airway Epithelial Cells
Ye, S., Cihil, K. M., Stolz, D. B., Pilewski, J. M., Stanton, B. A., & Swiatecka‐Urban, A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.139881 · Cited by 51
Co-recruitment analysis of the CBL and CBLB signalosomes in primary T cells identifies CD5 as a key regulator of TCR-induced ubiquitylation
Voisinne, G., García‐Blesa, A., Chaoui, K., Fiore, F., Bergot, E., Girard, L., Malissen, M., Burlet‐Schiltz, O., Gonzalez de Peredo, A., Malissen, B., et al. (2016) · Molecular Systems Biology · doi:10.15252/msb.20166837 · Cited by 50
YC ‐1 inhibits proliferation of breast cancer cells by down‐regulating EZH 2 expression via activation of c‐ C bl and ERK
Chang, L., Lin, H., Tsai, M., Chou, R., Lee, F., Teng, C., Hsieh, M., Hung, H., Huang, L., Yu, Y., et al. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12708 · Cited by 50
Chapter Six - The Ubiquitin Network in the Control of EGFR Endocytosis and Signaling
Conte, A., & Sigismund, S. (2016) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2016.03.002 · Cited by 53
Negative Regulation of EGFR-Vav2 Signaling Axis by Cbl Ubiquitin Ligase Controls EGF Receptor-mediated Epithelial Cell Adherens Junction Dynamics and Cell Migration
Duan, L., Raja, S. M., Chen, G., Virmani, S., Williams, S. H., Clubb, R. J., Mukhopadhyay, C., Rainey, M. A., Ying, G., Dimri, M., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.188086 · Cited by 49
Mutant Cbl proteins as oncogenic drivers in myeloproliferative disorders
Naramura, M., Nadeau, S. A., Mohapatra, B. C., Ahmad, G., Mukhopadhyay, C., Sattler, M., Raja, S. M., Natarajan, A., Band, V., & Band, H. (2011) · Oncotarget · doi:10.18632/oncotarget.233 · Cited by 49
miRNA-122-5p stimulates the proliferation and DNA synthesis and inhibits the early apoptosis of human spermatogonial stem cells by targeting CBL and competing with lncRNA CASC7
Zhou, F., Chen, W., Cui, Y., Liu, B., Yuan, Q., Li, Z., & He, Z. (2020) · Aging · doi:10.18632/aging.104158 · Cited by 49
Aberrant Receptor Signaling and Trafficking as Mechanisms in Oncogenesis
Rusten, T. E., Haglund, K., & Stenmark, H. (2007) · Critical Reviews™ in Oncogenesis · doi:10.1615/critrevoncog.v13.i1.20 · Cited by 50
M-CSF Regulates the Cytoskeleton via Recruitment of a Multimeric Signaling Complex to c-Fms Tyr-559/697/721
Faccio, R., Takeshita, S., Colaianni, G., Chappel, J. C., Zallone, A. Z., Teitelbaum, S. L., & Ross, F. P. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610937200 · Cited by 49
E3 ligase–defective Cbl mutants lead to a generalized mastocytosis and myeloproliferative disease
Bandi, S. R., Brandts, C., Rensinghoff, M., Grundler, R., Tickenbrock, L., Köhler, G., Duyster, J., Berdel, W. E., Müller‐Tidow, C., Serve, H. L., et al. (2009) · Blood · doi:10.1182/blood-2008-12-190934 · Cited by 50
c‐Cbl regulates MICA‐ but not ULBP2‐induced NKG2D down‐modulation in human NK cells
Molfetta, R., Quatrini, L., Capuano, C., Gasparrini, F., Zitti, B., Zingoni, A., Galandrini, R., Santoni, A., & Paolini, R. (2014) · European Journal of Immunology · doi:10.1002/eji.201444512 · Cited by 51
EphA2 Signaling Following Endocytosis: Role of Tiam1
Boissier, P., Chen, J., & Huynh‐Do, U. (2013) · Traffic · doi:10.1111/tra.12123 · Cited by 48
The Role of the Ubiquitin Proteasome System in Glioma: Analysis Emphasizing the Main Molecular Players and Therapeutic Strategies Identified in Glioblastoma Multiforme
Maksoud, S. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02339-4 · Cited by 48
Cbl-b Regulates Antigen-Induced TCR Down-Regulation and IFN-γ Production by Effector CD8 T Cells without Affecting Functional Avidity
Shamim, M. H., Nanjappa, S. G., Singh, A., Plisch, E. H., LeBlanc, S. E., Walent, J. H., Svaren, J. P., Seroogy, C. M., & Suresh, M. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.11.7233 · Cited by 48
Promotion of Osteoblast Differentiation in Mesenchymal Cells Through Cbl-Mediated Control of STAT5 Activity
Dieudonné, F., Sévère, N., Duplan, M. B., Weng, J.-J., Su, Y., & Marie, P. J. (2013) · Stem Cells · doi:10.1002/stem.1380 · Cited by 48
Cbl escapes Cdc42-mediated inhibition by downregulation of the adaptor molecule βPix
Schmidt, M. H. H., Husnjak, K., Szymkiewicz, I., Haglund, K., & Đikić, I. (2005) · Oncogene · doi:10.1038/sj.onc.1209329 · Cited by 47
Self-citation
LFA-1 signals to promote actin polymerization and upstream migration in T cells
Roy, N. H., Kim, S. H. J., Buffone, A., Blumenthal, D., Huang, B., Agarwal, S., Schwartzberg, P. L., Hammer, D. A., & Burkhardt, J. K. (2020) · Journal of Cell Science · doi:10.1242/jcs.248328 · Cited by 47
c-Cbl Interacts with CD38 and Promotes Retinoic Acid–Induced Differentiation and G0 Arrest of Human Myeloblastic Leukemia Cells
Shen, M., & Yen, A. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-1058 · Cited by 46
Global proteomics of Ubqln2-based murine models of ALS
Whiteley, A. M., Prado, M. A., de Poot, S. A. H., Paulo, J. A., Ashton, M., Domínguez, S. L., Weber, M., Ngu, H., Szpyt, J., Jedrychowski, M. P., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.015960 · Cited by 50
Reversal of P‐glycoprotein‐mediated multi‐drug resistance by the E3 ubiquitin ligase Cbl‐b in human gastric adenocarcinoma cells
Zhang, Y., Qu, X., Hu, X., Yang, X., Hou, K., Teng, Y., Zhang, J., Sada, K., & Liu, Y. (2009) · The Journal of Pathology · doi:10.1002/path.2533 · Cited by 46
Genetic Ablation of the c-Cbl Ubiquitin Ligase Domain Results in Increased Energy Expenditure and Improved Insulin Action
Molero, J. C., Turner, N. A., Thien, C. B. F., Langdon, W. Y., James, D. E., & Cooney, G. J. (2006) · Diabetes · doi:10.2337/db06-0955 · Cited by 47
Decreased glucocerebrosidase activity in Gaucher disease parallels quantitative enzyme loss due to abnormal interaction with TCP1 and c-Cbl
Lu, J., Chiang, J. Y., Iyer, R. R., Thompson, E., Kaneski, C. R., Xu, D. S., Yang, C., Chen, M., Hodes, R. J., Lonser, R. R., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1014376107 · Cited by 45
Ligand Binding Induces Cbl‐Dependent EphB1 Receptor Degradation Through the Lysosomal Pathway
Fasen, K., Cerretti, D. P., & Huynh‐Do, U. (2007) · Traffic · doi:10.1111/j.1600-0854.2007.00679.x · Cited by 45
c-Cbl-Mediated Selective Virus-Receptor Translocations into Lipid Rafts Regulate Productive Kaposi's Sarcoma-Associated Herpesvirus Infection in Endothelial Cells
Chakraborty, S., Veettil, M. V., Sadagopan, S., Paudel, N., & Chandran, B. (2011) · Journal of Virology · doi:10.1128/jvi.05953-11 · Cited by 45
Clonal hematopoiesis: Pre-cancer PLUS
Silver, A. J., & Jaiswal, S. (2019) · Advances in cancer research · doi:10.1016/bs.acr.2018.12.003 · Cited by 46
The c-Cbl Ubiquitin Ligase Regulates Nuclear β-Catenin and Angiogenesis by Its Tyrosine Phosphorylation Mediated through the Wnt Signaling Pathway
Shivanna, S., Harrold, I., Shashar, M., Meyer, R., Kiang, C., Francis, J. M., Zhao, Q., Feng, H., Edelman, E. R., Rahimi, N., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.616623 · Cited by 44
Germline Mutation of CBL Is Associated With Moyamoya Disease in a Child With Juvenile Myelomonocytic Leukemia and Noonan Syndrome‐Like Disorder
Hyakuna, N., Muramatsu, H., Higa, T., Chinen, Y., Wang, X., & Kojima, S. (2014) · Pediatric Blood & Cancer · doi:10.1002/pbc.25271 · Cited by 43
Regulation of peripheral T cell tolerance by the E3 ubiquitin ligase Cbl-b
Loeser, S., & Penninger, J. M. (2007) · Seminars in Immunology · doi:10.1016/j.smim.2007.02.004 · Cited by 43
The co-crystal structure of Cbl-b and a small-molecule inhibitor reveals the mechanism of Cbl-b inhibition
Kimani, S., Perveen, S., Szewczyk, M. M., Zeng, H., Dong, A., Li, F., Ghiabi, P., Li, Y., Chau, I., Arrowsmith, C. H., et al. (2023) · Communications Biology · doi:10.1038/s42003-023-05655-8 · Cited by 42
Role of CBL Mutations in Cancer and Non-Malignant Phenotype
Leardini, D., Messelodi, D., Muratore, E., Baccelli, F., Bertuccio, S. N., Anselmi, L., Pession, A., & Masetti, R. (2022) · Cancers · doi:10.3390/cancers14030839 · Cited by 42
Suppressor of T‐cell receptor signalling 1 and 2 differentially regulate endocytosis and signalling of receptor tyrosine kinases
Raguz, J., Wagner, S., Đikić, I., & Hoeller, D. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.08.077 · Cited by 42
Cbl-b Is a Negative Regulator of Inflammatory Cytokines Produced by IgE-Activated Mast Cells
Gustin, S. E., Thien, C. B. F., & Langdon, W. Y. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.9.5980 · Cited by 41
CBL enhances breast tumor formation by inhibiting tumor suppressive activity of TGF-β signaling
Kang, J. M., Park, S., Kim, S. J., Hong, H. Y., Jeong, J., Kim, H.-S., & Kim, S.-J. (2012) · Oncogene · doi:10.1038/onc.2012.18 · Cited by 41
De novo mutations in CBL causing early-onset paediatric moyamoya angiopathy
Guey, S., Grangeon, L., Brunelle, F., Bergametti, F., Amiel, J., Lyonnet, S., Delaforge, A., Arnould, M., Desnous, B., Bellesme, C., et al. (2017) · Journal of Medical Genetics · doi:10.1136/jmedgenet-2016-104432 · Cited by 40
Transcriptomic responses in mouse brain exposed to chronic excess of the neurotransmitter glutamate
Wang, X., Bao, X., Pal, R., Aǵbaş, A., & Michaelis, E. K. (2010) · BMC Genomics · doi:10.1186/1471-2164-11-360 · Cited by 42
c-Cbl Ubiquitin Ligase Regulates Focal Adhesion Protein Turnover and Myofibril Degeneration Induced by Neutrophil Protease Cathepsin G
Rafiq, K., Guo, J., Vlasenko, L., Guo, X., Kolpakov, M. A., Sanjay, A., Houser, S. R., & Sabri, A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.307009 · Cited by 39
Down-Regulation of Ubiquitin Ligase Cbl Induced by Twist Haploinsufficiency in Saethre-Chotzen Syndrome Results in Increased PI3K/Akt Signaling and Osteoblast Proliferation
Guénou, H., Kaabeche, K., Dufour, C., Miraoui, H., & Marie, P. J. (2006) · American Journal Of Pathology · doi:10.2353/ajpath.2006.060102 · Cited by 39
Suppression of the Ligand-mediated Down-regulation of Epidermal Growth Factor Receptor by Ymer, a Novel Tyrosine-phosphorylated and Ubiquitinated Protein
Tashiro, K., Konishi, H., Sano, E., Nabeshi, H., Yamauchi, E., & Taniguchi, H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604184200 · Cited by 39
Androgen-dependent apoptosis in male germ cells is regulated through the proto-oncoprotein Cbl
Chami, N., Ikhlef, F., Kaszas, K., Yakoub, S., Tabone, É., Siddeek, B., Cunha, S., Beaudoin, C., Morel, L., Benahmed, M., et al. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200507076 · Cited by 40
JAK2 mutants (e.g., JAK2V617F) and their importance as drug targets in myeloproliferative neoplasms
Gäbler, K., Behrmann, I., & Haan, C. (2013) · JAK-STAT · doi:10.4161/jkst.25025 · Cited by 39
A cross-tissue transcriptome-wide association study identifies novel susceptibility genes for lung cancer in Chinese populations
Zhu, M., Fan, J., Zhang, C., Xu, J., Yin, R. H., Zhang, E., Wang, Y., Ji, M., Sun, Q., Dai, J., et al. (2021) · Human Molecular Genetics · doi:10.1093/hmg/ddab119 · Cited by 40
New insights into the role of the ubiquitin-proteasome pathway in the regulation of apoptosis.
Liu, C., Goldberg, A. L., & Qiu, X. (2007) · PubMed · Cited by 38
Signaling-mediated control of ubiquitin ligases in endocytosis
Polo, S. (2012) · BMC Biology · doi:10.1186/1741-7007-10-25 · Cited by 38
Stabilization of AURKA by the E3 ubiquitin ligase CBLC in lung adenocarcinoma
Hong, S., Lu, Y., Hsiao, S.-H., Kao, Y.-R., Lee, M.-H., Lin, Y.-P., Wang, C., & Wu, C. (2022) · Oncogene · doi:10.1038/s41388-022-02180-6 · Cited by 37
The N Terminus of Cbl-c Regulates Ubiquitin Ligase Activity by Modulating Affinity for the Ubiquitin-conjugating Enzyme
Ryan, P. E., Sivadasan-Nair, N., Nau, M. M., Nicholas, S., & Lipkowitz, S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.091157 · Cited by 37
Balancing Protein Stability and Activity in Cancer: A New Approach for Identifying Driver Mutations Affecting CBL Ubiquitin Ligase Activation
Li, M., Kales, S. C., Ma, K., Shoemaker, B. A., Crespo-Barreto, J., Cangelosi, A. L., Lipkowitz, S., & Panchenko, A. R. (2015) · Cancer Research · doi:10.1158/0008-5472.can-14-3812 · Cited by 38
Molecular and alternative methods for diagnosis of acute myeloid leukemia with mutated NPM1: flexibility may help
Falini, B., Martelli, M. P., Pileri, S. A., & Mecucci, C. (2010) · Haematologica · doi:10.3324/haematol.2009.017822 · Cited by 37
Childhood Myelodysplastic Syndrome: Focus on the Approach to Diagnosis and Treatment of Juvenile Myelomonocytic Leukemia
Loh, M. L. (2010) · Hematology · doi:10.1182/asheducation-2010.1.357 · Cited by 37
The gradient of Gurken, a long-range morphogen, is directly regulated by Cbl-mediated endocytosis
Chang, W., Liou, W., Pen, H.-C., Chou, H.-Y., Chang, Y.-W., Li, W.-H., Chiang, W., & Pai, L. (2008) · Development · doi:10.1242/dev.017103 · Cited by 37
Notch: Implications of endogenous inhibitors for therapy
Đikić, I., & Schmidt, M. H. H. (2010) · BioEssays · doi:10.1002/bies.200900140 · Cited by 37
Self-citation
Septin 9 negatively regulates ubiquitin-dependent downregulation of epidermal growth factor receptor
Diesenberg, K., Beerbaum, M., Fink, U., Schmieder, P., & Krauss, M. I. (2014) · Journal of Cell Science · doi:10.1242/jcs.162206 · Cited by 39
A combination of two antibodies recognizing non‐overlapping epitopes of HER 2 induces kinase activity‐dependent internalization of HER 2
Szymańska, M., Wium, A. M. F., Nikolaysen, F., Pedersen, M. W., Grandal, M. M., Stang, E., & Bertelsen, V. (2016) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.12899 · Cited by 36
From clonal hematopoiesis to myeloid leukemia and what happens in between: Will improved understanding lead to new therapeutic and preventive opportunities?
Bewersdorf, J. P., Ardasheva, A., Podoltsev, N. A., Singh, A., Biancon, G., Halene, S., & Zeidan, A. M. (2019) · Blood Reviews · doi:10.1016/j.blre.2019.100587 · Cited by 37
Processing Temporal Growth Factor Patterns by an Epidermal Growth Factor Receptor Network Dynamically Established in Space
Koseska, A., & Bastiaens, P. I. H. (2020) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-013020-103810 · Cited by 39
Pathways driving the endocytosis of mutant and wild-type EGFR in cancer
Hampton, K. K., & Craven, R. J. (2014) · Oncoscience · doi:10.18632/oncoscience.67 · Cited by 35
Reggie-1/Flotillin-2 regulates integrin trafficking and focal adhesion turnover via Rab11a
Hülsbusch, N., Solis, G. P., Katanaev, V. L., & Stuermer, C. A. O. (2015) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2015.07.003 · Cited by 35
Malfunctions within the Cbl interactome uncouple receptor tyrosine kinases from destructive transport
Đikić, I., & Schmidt, M. H. H. (2007) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2007.04.005 · Cited by 38
Self-citation
Deregulated Intracellular Signaling by Mutated c-CBL in Myeloid Neoplasms
Ogawa, S., Shih, L., Suzuki, T., Otsu, M., Nakauchi, H., Koeffler, H. P., & Sanada, M. (2010) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-09-2341 · Cited by 35
E3 ubiquitin ligase Casitas B lineage lymphoma-b and its potential therapeutic implications for immunotherapy
Jafari, D., Mousavi, M. J., Shahbaz, S. K., Jafarzadeh, L., Tahmasebi, S., Spoor, J. K. H., & Esmaeilzadeh, A. (2020) · Clinical & Experimental Immunology · doi:10.1111/cei.13560 · Cited by 36
Activating CBL mutations are associated with a distinct MDS/MPN phenotype
Schwaab, J., Ernst, T., Erben, P., Rinke, J., Schnittger, S., Ströbel, P., Metzgeroth, G., Mossner, M., Haferlach, T., Cross, N. C. P., et al. (2012) · Annals of Hematology · doi:10.1007/s00277-012-1521-3 · Cited by 35
Rac1-mediated cytoskeleton rearrangements induced by intersectin-1s deficiency promotes lung cancer cell proliferation, migration and metastasis
Jeganathan, N., Predescu, D. N., Zhang, J., Sha, F., Bardita, C., Patel, M., Wood, S. J., Borgia, J. A., BALK, R. A., & Predescu, S. A. (2016) · Molecular Cancer · doi:10.1186/s12943-016-0543-1 · Cited by 34
FTO represses NLRP3 ‐mediated pyroptosis and alleviates myocardial ischemia–reperfusion injury via inhibiting CBL ‐mediated ubiquitination and degradation of β‐catenin
Sun, F., An, C., Liu, C., Hu, Y., Su, Y., Guo, Z., Che, H., & Ge, S. (2023) · The FASEB Journal · doi:10.1096/fj.202201793rr · Cited by 33
New Regulatory Roles of Galectin-3 in High-Affinity IgE Receptor Signaling
Bambousková, M., Polakovičová, I., Hálová, I., Goel, G., Dráberová, L., Bugajev, V., Doan, A., Utekal, P., Gardet, A., Xavier, R. J., et al. (2016) · Molecular and Cellular Biology · doi:10.1128/mcb.00064-16 · Cited by 33
The Casitas B Lineage Lymphoma (Cbl) Mutant G306E Enhances Osteogenic Differentiation in Human Mesenchymal Stromal Cells in Part by Decreased Cbl-mediated Platelet-derived Growth Factor Receptor α and Fibroblast Growth Factor Receptor 2 Ubiquitination
Sévère, N., Miraoui, H., & Marie, P. J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.197525 · Cited by 33
TCR signaling promotes formation of an STS1-Cbl-b complex with pH-sensitive phosphatase activity that suppresses T cell function in acidic environments
Tsai, Y.-L., Arias-Badia, M., Kadlecek, T. A., Lwin, Y. M., Srinath, A., Shah, N. H., Wang, Z., Barber, D. L., Kuriyan, J., Fong, L. H., et al. (2023) · Immunity · doi:10.1016/j.immuni.2023.11.010 · Cited by 33
Mutations of c-Cbl in myeloid malignancies
Katzav, S., & Schmitz, M. L. (2015) · Oncotarget · doi:10.18632/oncotarget.3986 · Cited by 33
The Src-like adaptor protein regulates PDGF-induced actin dorsal ruffles in a c-Cbl-dependent manner
Sirvent, A., Leroy, C., Boureux, A., Simon, V., & Roche, S. (2008) · Oncogene · doi:10.1038/sj.onc.1211011 · Cited by 22
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
Releasing the Brake: Targeting Cbl-b to Enhance Lymphocyte Effector Functions
Wallner, S., Gruber, T., Baier, G., & Wolf, D. G. F. (2012) · Clinical and Developmental Immunology · doi:10.1155/2012/692639 · Cited by 31
Interferon-α sensitizes human gastric cancer cells to TRAIL-induced apoptosis via activation of the c-CBL-dependent MAPK/ERK pathway
Qu, J., Zhao, M., Teng, Y., Zhang, Y., Hou, K., Jiang, Y., Yang, X., Shang, H., Qu, X., & Liu, Y. (2011) · Cancer Biology & Therapy · doi:10.4161/cbt.12.6.15973 · Cited by 31
Low Expression of the E3 Ubiquitin Ligase CBL Confers Chemoresistance in Human Pancreatic Cancer and Is Targeted by Epidermal Growth Factor Receptor Inhibition
Kadera, B. E., Toste, P. A., Wu, N., Li, L., Nguyen, A. H., Dawson, D. W., & Donahue, T. R. (2014) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-0610 · Cited by 30
More than kin and less than kind
Shannon, K., & Loh, M. L. (2009) · Nature · doi:10.1038/460804a · Cited by 29
Patterns of Transposable Element Expression and Insertion in Cancer
Clayton, E. A., Wang, L., Rishishwar, L., Wang, J., McDonald, J. F., & Jordan, I. K. (2016) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2016.00076 · Cited by 30
CFBP Is a Novel Tyrosine-phosphorylated Protein That Might Function as a Regulator of CIN85/CD2AP
Konishi, H., Tashiro, K., Murata, Y., Nabeshi, H., Yamauchi, E., & Taniguchi, H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605693200 · Cited by 29
A High Occurrence of Acquisition and/or Expansion of C-CBL Mutant Clones in the Progression of High-Risk Myelodysplastic Syndrome to Acute Myeloid Leukemia
Kao, H., Sanada, M., Liang, D., Lai, C., Lee, E., Kuo, M., Lin, T., Shih, Y., Wu, J., Huang, C., et al. (2011) · Neoplasia · doi:10.1593/neo.111192 · Cited by 28
Distinct functions of human MVB12A and MVB12B in the ESCRT-I dependent on their posttranslational modifications
Tsunematsu, T., Yamauchi, E., Shibata, H., Maki, M., Ohta, T., & Konishi, H. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.07.060 · Cited by 29
Abi-1 forms an epidermal growth factor-inducible complex with Cbl: Role in receptor endocytosis
Tanos, B. E., & Pendergast, A. M. (2007) · Cellular Signalling · doi:10.1016/j.cellsig.2007.02.008 · Cited by 28
Proteomic Landscape of Extracellular Vesicles for Diffuse Large B-Cell Lymphoma Subtyping
Carvalho, A. S., Baeta, H., Henriques, A. F. A., Ejtehadifar, M., Tranfield, E. M., Sousa, A. L., Farinho, A., Costa‐Silva, B., Cabeçadas, J., Gameiro, P., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222011004 · Cited by 27
Adipose-specific deletion of the cation channel TRPM7 inhibits TAK1 kinase-dependent inflammation and obesity in male mice
Zhong, W., Ma, M., Xie, J., Huang, C., Li, X., & Gao, M. (2023) · Nature Communications · doi:10.1038/s41467-023-36154-3 · Cited by 27
Ubiquitination and endocytosis of the high affinity receptor for IgE
Molfetta, R., Gasparrini, F., Santoni, A., & Paolini, R. (2010) · Molecular Immunology · doi:10.1016/j.molimm.2010.06.003 · Cited by 27
Diacylglycerol Kinase δ and Protein Kinase Cα Modulate Epidermal Growth Factor Receptor Abundance and Degradation through Ubiquitin-specific Protease 8
Cai, J., Crotty, T. M., Reichert, E. C., Carraway Kermit, L., Stafforini, D. M., & Topham, M. K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.055731 · Cited by 26
c-Cbl mediates the degradation of tumorigenic nuclear β-catenin contributing to the heterogeneity in Wnt activity in colorectal tumors
Shashar, M., Siwak, J. F., Tapan, Ü., Lee, S. Y., Meyer, R., Parrack, P. H., Tan, J. N. M., Khatami, F., Francis, J. M., Zhao, Q., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.12107 · Cited by 26
Targeting the E3 ubiquitin casitas B-lineage lymphoma decreases osteosarcoma cell growth and survival and reduces tumorigenesis
Sévère, N., Dieudonné, F., Marty, C., Modrowski, D., Patiño‐García, A., Lecanda, F., Fromigué, O., & Marie, P. J. (2012) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.1667 · Cited by 26
The Insect Peptide CopA3 Increases Colonic Epithelial Cell Proliferation and Mucosal Barrier Function to Prevent Inflammatory Responses in the Gut
Kim, D. H., Hwang, J. S., Lee, I. H., Nam, S. T., Hong, J., Zhang, P., Li, L., Lee, J., Seok, H., Pothoulakis, C., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.682856 · Cited by 26
Casitas B-lineage lymphoma linker helix mutations found in myeloproliferative neoplasms affect conformation
Buetow, L., Tria, G., Ahmed, S. F., Hock, A., Dou, H., Sibbet, G. J., Svergun, D. I., & Huang, D. T. C. (2016) · BMC Biology · doi:10.1186/s12915-016-0298-6 · Cited by 26
The Cbl-b RING finger domain has a limited role in regulating inflammatory cytokine production by IgE-activated mast cells
Oksvold, M. P., Dagger, S. A., Thien, C. B. F., & Langdon, W. Y. (2007) · Molecular Immunology · doi:10.1016/j.molimm.2007.08.002 · Cited by 26
Enigma Prevents Cbl-c-Mediated Ubiquitination and Degradation of RETMEN2A
Kales, S. C., Nau, M. M., Merchant, A. S., & Lipkowitz, S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0087116 · Cited by 25
Cbl E3 Ligase Mediates the Removal of Nectin-1 from the Surface of Herpes Simplex Virus 1-Infected Cells
Deschamps, T., Dogrammatzis, C., Mullick, R., & Kalamvoki, M. (2017) · Journal of Virology · doi:10.1128/jvi.00393-17 · Cited by 25
Immunoproteasome Function in Normal and Malignant Hematopoiesis
Santamaría, N. T., Ebstein, F., Heidel, F. H., & Krüger, E. (2021) · Cells · doi:10.3390/cells10071577 · Cited by 25
c-Cbl is not required for ERK1/2-dependent degradation of BimEL
Wiggins, C. M., Band, H., & Cook, S. J. (2007) · Cellular Signalling · doi:10.1016/j.cellsig.2007.08.008 · Cited by 26
Cbl-b promotes cell detachment via ubiquitination of focal adhesion kinase
Fan, Y., Qu, X., Ma, Y., Liu, Y., & Hu, X. (2016) · Oncology Letters · doi:10.3892/ol.2016.4730 · Cited by 24
Cbl and Cbl-b independently regulate EGFR through distinct receptor interaction modes
Pinilla‐Macua, I., & Sorkin, A. D. (2023) · Molecular Biology of the Cell · doi:10.1091/mbc.e23-02-0058 · Cited by 24
c-Cbl Tyrosine Kinase-binding Domain Mutant G306E Abolishes the Interaction of c-Cbl with CD38 and Fails to Promote Retinoic Acid-induced Cell Differentiation and G0 Arrest
Shen, M., & Yen, A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.014241 · Cited by 24

Authors: Schmidt, M. H. H., & Dikic, I.
Affiliations: Goethe University Frankfurt (DE)
ORCID: Schmidt, Mirko H.H.
Venue: Nature Reviews Molecular Cell Biology
Publisher: Springer Science and Business Media LLC
Published: 2005-10-14
Volume: 6
Issue: 12
Pages: 907-919
ISSN: 1471-0072 (ISSN-L)
1471-0080
DOI: 10.1038/nrm1762
OpenAlex: W2059037016
Cited by: 395
References: 126
Citations by year: 2026: 6 · 2025: 8 · 2024: 8 · 2023: 15 · 2022: 15 · 2021: 9 · 2020: 11 · 2019: 10 · 2018: 12 · 2017: 13 · 2016: 21 · 2015: 23 · 2014: 24 · 2013: 34 · 2012: 38
FWCI: 1.54
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature Reviews Molecular Cell Biology (publishedVersion)
PubMed (publishedVersion)
Funders: European Molecular Biology Organization
Deutsche Forschungsgemeinschaft
Boehringer Ingelheim Stiftung
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Keywords: ubiquitin ligase, protein-protein interaction network, adaptor proteins, signal transduction regulation, protein complex formation, immune disorders, diabetes mellitus, cancer
MeSH terms: Actins, Animals, Endocytosis, Humans, Lymphocytes, Signal Transduction, Receptor Protein-Tyrosine Kinases, Multiprotein Complexes, Proto-Oncogene Proteins c-cbl

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

The Cbl interactome and its functions

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks