TBC proteins: GAPs for mammalian small GTPase Rab?

Rab GTPases as coordinators of vesicle traffic

Stenmark, H. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2728 · Cited by 3,413 · see citing works

Rabs and their effectors: achieving specificity in membrane traffic

Grosshans, B. L., Ortiz, D., & Novick, P. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601617103 · Cited by 1,005 · see citing works

Insulin-stimulated Phosphorylation of a Rab GTPase-activating Protein Regulates GLUT4 Translocation

Sano, H., Kane, S., Sano, E., Mı̂inea, C. P., Asara, J. M., Lane, W. S., Garner, C. W., & Lienhard, G. E. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c300063200 · Cited by 964 · see citing works

Regulation of exosome secretion by Rab35 and its GTPase-activating proteins TBC1D10A–C

Hsu, C., Morohashi, Y., Yoshimura, S., Manrique‐Hoyos, N., Jung, S., Lauterbach, M. A., Bakhti, M., Grønborg, M., Möbius, W., Rhee, J., et al. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.200911018 · Cited by 860 · see citing works

Evolution of the rab family of small GTP-binding proteins

Pereira‐Leal, J. B., & Seabra, M. C. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5072 · Cited by 770 · see citing works

A Method to Identify Serine Kinase Substrates

Kane, S., Sano, H., Liu, S. C. H., Asara, J. M., Lane, W. S., Garner, C. C., & Lienhard, G. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200198200 · Cited by 529 · see citing works

Rab GTPases, intracellular traffic and disease

Seabra, M. C., Mules, E. H., & Hume, A. N. (2002) · Trends in Molecular Medicine · doi:10.1016/s1471-4914(01)02227-4 · Cited by 468 · see citing works

AS160, the Akt substrate regulating GLUT4 translocation, has a functional Rab GTPase-activating protein domain

Mîinea, C. P., Sano, H., Kane, S., Sano, E., Fukuda, M., Peränen, J., Lane, W. S., & Lienhard, G. E. (2005) · Biochemical Journal · doi:10.1042/bj20050887 · Cited by 449 · see citing works

Rab GEFs and GAPs

Barr, F. A., & Lambright, D. G. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2010.04.007 · Cited by 412 · see citing works

Functional dissection of Rab GTPases involved in primary cilium formation

Yoshimura, S., Egerer, J., Fuchs, E., Haas, A. K., & Barr, F. A. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200703047 · Cited by 375 · see citing works

Rab10, a Target of the AS160 Rab GAP, Is Required for Insulin-Stimulated Translocation of GLUT4 to the Adipocyte Plasma Membrane

Sano, H., Eguez, L., Teruel, M. N., Fukuda, M., Chuang, T. D., Chavez, J. A., Lienhard, G. E., & McGraw, T. E. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.03.001 · Cited by 374 · see citing works

Rab GTPases at a glance

Schwartz, S. L., Cao, C., Pylypenko, O., Rak, A., & Wandinger‐Ness, A. (2007) · Journal of Cell Science · doi:10.1242/jcs.015909 · Cited by 369 · see citing works

GAPs galore! A survey of putative Ras superfamily GTPase activating proteins in man and Drosophila

Bernards, A. (2003) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/s0304-419x(02)00082-3 · Cited by 362 · see citing works

TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism

Pan, X., Eathiraj, S., Munson, M., & Lambright, D. G. (2006) · Nature · doi:10.1038/nature04847 · Cited by 359 · see citing works

Membrane traffic in the secretory pathway

Fukuda, M. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8351-4 · Cited by 359 · see citing works

Ypt and Rab GTPases: insight into functions through novel interactions

Segev, N. (2001) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00242-8 · Cited by 293 · see citing works

The Eps8 protein coordinates EGF receptor signalling through Rac and trafficking through Rab5

Lanzetti, L., Rybin, V., Malabarba, M. G., Christoforidis, S., Scita, G., Zerial, M., & Fiore, P. P. D. (2000) · Nature · doi:10.1038/35042605 · Cited by 284 · see citing works

Glucose transporter 4: cycling, compartments and controversies

Dugani, S. B., & Klip, A. (2005) · EMBO Reports · doi:10.1038/sj.embor.7400584 · Cited by 229 · see citing works

A GTPase-activating protein controls Rab5 function in endocytic trafficking

Haas, A. K., Fuchs, E., Kopajtich, R., & Barr, F. A. (2005) · Nature Cell Biology · doi:10.1038/ncb1290 · Cited by 228 · see citing works

Bridging the GAP between insulin signaling and GLUT4 translocation

Watson, R. T., & Pessin, J. E. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.02.007 · Cited by 219 · see citing works

Tbc1d1 mutation in lean mouse strain confers leanness and protects from diet-induced obesity

Chadt, A., Leicht, K., Deshmukh, A. S., Jiang, L. Q., Scherneck, S., Bernhardt, U., Dreja, T., Vogel, H., Schmolz, K., Kluge, R., et al. (2008) · Nature Genetics · doi:10.1038/ng.244 · Cited by 201 · see citing works

Analysis of GTPase-activating proteins: Rab1 and Rab43 are key Rabs required to maintain a functional Golgi complex in human cells

Haas, A. K., Yoshimura, S.-I., Stephens, D. J., Preisinger, C., Fuchs, E., & Barr, F. A. (2007) · Journal of Cell Science · doi:10.1242/jcs.014225 · Cited by 201 · see citing works

Isolation and Characterization of a GTPase Activating Protein Specific for the Rab3 Subfamily of Small G Proteins

Fukui, K., Sasaki, T., Imazumi, K., Matsuura, Y., Nakanishi, H., & Takai, Y. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.8.4655 · Cited by 192 · see citing works

Substrate specificity and effect on GLUT4 translocation of the Rab GTPase-activating protein Tbc1d1

Roach, W. G., Chavez, J. A., Mı̂inea, C. P., & Lienhard, G. E. (2007) · Biochemical Journal · doi:10.1042/bj20061798 · Cited by 192 · see citing works

Isolation and Characterization of a GDP/GTP Exchange Protein Specific for the Rab3 Subfamily Small G Proteins

Wada, M., Nakanishi, H., Satoh, A., Hirano, H., Obaishi, H., Matsuura, Y., & Takai, Y. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.7.3875 · Cited by 179 · see citing works

A Rab GAP cascade defines the boundary between two Rab GTPases on the secretory pathway

Rivera-Molina, F. E., & Novick, P. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0906536106 · Cited by 170 · see citing works

Specific Rab GTPase-activating proteins define the Shiga toxin and epidermal growth factor uptake pathways

Fuchs, E., Haas, A. K., Spooner, R. A., Yoshimura, S., Lord, J. M., & Barr, F. A. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200612068 · Cited by 161 · see citing works

Screening for target Rabs of TBC (Tre‐2/Bub2/Cdc16) domain‐containing proteins based on their Rab‐binding activity

Itoh, T., Satoh, M., Kanno, E., & Fukuda, M. (2006) · Genes to Cells · doi:10.1111/j.1365-2443.2006.00997.x · Cited by 158 · see citing works

TBC1D24, an ARF6-Interacting Protein, Is Mutated in Familial Infantile Myoclonic Epilepsy

Falace, A., Filipello, F., Padula, V. L., Vanni, N., Madia, F., Tonelli, D. D. P., de Falco, F. A., Striano, P., Bricarelli, F. D., Minetti, C., et al. (2010) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2010.07.020 · Cited by 152 · see citing works

Characterization of GAPCenA, a GTPase activating protein for Rab6, part of which associates with the centrosome

Cuif, M., Possmayer, F., Zander, H., Bordes, N., Jollivet, F., Couëdel-Courteille, A., Janoueix‐Lerosey, I., Langsley, G., Bornens, M., & Goud, B. (1999) · The EMBO Journal · doi:10.1093/emboj/18.7.1772 · Cited by 145 · see citing works

Large Scale Screening for Novel Rab Effectors Reveals Unexpected Broad Rab Binding Specificity*S

Fukuda, M., Kanno, E., Ishibashi, K., & Itoh, T. (2008) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m700569-mcp200 · Cited by 140 · see citing works

Differential Effects of TBC1D15 and Mammalian Vps39 on Rab7 Activation State, Lysosomal Morphology, and Growth Factor Dependence

Peralta, E. R., Martin, B. C., & Edinger, A. L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.111633 · Cited by 132 · see citing works

TBC1D20 Is a Rab1 GTPase-activating Protein That Mediates Hepatitis C Virus Replication

Sklan, E. H., Serrano, R., Einav, S., Pfeffer, S. R., Lambright, D. G., & Glenn, J. S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705221200 · Cited by 126 · see citing works

Comprehensive Screening for Novel Rab-Binding Proteins by GST Pull-Down Assay Using 60 Different Mammalian Rabs‡

Kanno, E., Ishibashi, K., Kobayashi, H., Matsui, T., Ohbayashi, N., & Fukuda, M. (2010) · Traffic · doi:10.1111/j.1600-0854.2010.01038.x · Cited by 122 · see citing works

A novel transcriptional unit of the tre oncogene widely expressed in human cancer cells.

Nakamura, T., Hillová, J., Mariage, R., Onno, M., Huebner, K., Cannizzaro, L. A., Boghosian-Sell, L., Croce, C. M., & Hill, M. (1992) · PubMed · Cited by 118 · see citing works

Rab10 in insulin-stimulated GLUT4 translocation

Sano, H., Roach, W. G., Peck, G. R., Fukuda, M., & Lienhard, G. E. (2008) · Biochemical Journal · doi:10.1042/bj20071318 · Cited by 117 · see citing works

GLUT4 Vesicle Recruitment and Fusion Are Differentially Regulated by Rac, AS160, and Rab8A in Muscle Cells

Randhawa, V. K., Ishikura, S., Talior‐Volodarsky, I., Cheng, A. W.-P., Patel, N., Hartwig, J. H., & Klip, A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804282200 · Cited by 115 · see citing works

Broad-Minded Links Cell Cycle-Related Kinase to Cilia Assembly and Hedgehog Signal Transduction

Ko, H. W., Norman, R. X., Tran, J., Fuller, K. P., Fukuda, M., & Eggenschwiler, J. T. (2010) · Developmental Cell · doi:10.1016/j.devcel.2009.12.014 · Cited by 113 · see citing works

A Focal Epilepsy and Intellectual Disability Syndrome Is Due to a Mutation in TBC1D24

Corbett, M. A., Bahlo, M., Jolly, L. A., Afawi, Z., Gardner, A. E., Oliver, K. L., Tan, S., Coffey, A., Mulley, J. C., Dibbens, L. M., et al. (2010) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2010.08.001 · Cited by 112 · see citing works

A truncation mutation in TBC1D4 in a family with acanthosis nigricans and postprandial hyperinsulinemia

Dash, S., Sano, H., Rochford, J. J., Semple, R. K., Yeo, G. S. H., Hyden, C. S. S., Soos, M. A., Clark, J., Rodin, A., Langenberg, C., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900909106 · Cited by 108 · see citing works

TBC domain family, member 15 is a novel mammalian Rab GTPase-activating protein with substrate preference for Rab7

Zhang, X., Walsh, B., Mitchell, C. A., & Rowe, T. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.07.070 · Cited by 101 · see citing works

Armus Is a Rac1 Effector that Inactivates Rab7 and Regulates E-Cadherin Degradation

Frasa, M. A. M., Maximiano, F. C., Smolarczyk, K., Francis, R. E., Betson, M., Lozano, E., Goldenring, J. R., Seabra, M. C., Rak, A., Ahmadian, M. R., et al. (2010) · Current Biology · doi:10.1016/j.cub.2009.12.053 · Cited by 100 · see citing works

PRC17, a novel oncogene encoding a Rab GTPase-activating protein, is amplified in prostate cancer.

Pei, L., Yue, P., Yang, Y., Ling, X. B., van Eyndhoven, W., Nguyen, K. C. Q., Rubin, M. A., Hoey, T., Powers, S., & Li, J. (2002) · PubMed · Cited by 96 · see citing works

RUN domains: a new family of domains involved in Ras-like GTPase signaling

Callebaut, I., Jean, de Gunzburg, Goud, B., & Mornon, J.-P. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01730-8 · Cited by 96 · see citing works

Insulin-stimulated Phosphorylation of the Rab GTPase-activating Protein TBC1D1 Regulates GLUT4 Translocation

Peck, G. R., Chavez, J. A., Roach, W. G., Budnik, B. A., Lane, W. S., Karlsson, H. K. R., Zierath, J. R., & Lienhard, G. E. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.035568 · Cited by 95 · see citing works

TBC-2 Regulates RAB-5/RAB-7-mediated Endosomal Trafficking in Caenorhabditis elegans

Chotard, L., Mishra, A. K., Sylvain, M.-A., Tuck, S., Lambright, D. G., & Rocheleau, C. E. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-11-0947 · Cited by 89 · see citing works

Identification of EPI64 as a GTPase-activating Protein Specific for Rab27A

Itoh, T., & Fukuda, M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603808200 · Cited by 84 · see citing works

Identification of Epi64, a Tbc/Rabgap Domain–Containing Microvillar Protein That Binds to the First PDZ Domain of Ebp50 and E3karp

Reczek, D., & Bretscher, A. P. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.1.191 · Cited by 83 · see citing works

The GAP activity of Msb3p and Msb4p for the Rab GTPase Sec4p is required for efficient exocytosis and actin organization

Gao, X., Albert, Š., Cheperegin, S. E., Burd, C. G., Gallwitz, D., & Bi, E. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200302038 · Cited by 80 · see citing works

EPI64 regulates microvillar subdomains and structure

Hanono, A., Garbett, D., Reczek, D., Chambers, D. N., & Bretscher, A. P. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200604046 · Cited by 77 · see citing works

The TBC (Tre-2/Bub2/Cdc16) Domain Protein TRE17 Regulates Plasma Membrane-Endosomal Trafficking through Activation of Arf6

Martinu, L., Robens, J., Robertson, S. E., Santy, L. C., Casanova, J. E., & Chou, M. M. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.22.9752-9762.2004 · Cited by 76 · see citing works

A Rab-GAP TBC Domain Protein Binds Hepatitis C Virus NS5A and Mediates Viral Replication

Sklan, E. H., Staschke, K. A., Oakes, T. M. M., Elazar, M., Winters, M. A., Aroeti, B., Danieli, T., & Glenn, J. S. (2007) · Journal of Virology · doi:10.1128/jvi.01249-07 · Cited by 74 · see citing works

Feedback inhibition of calcineurin and Ras by a dual inhibitory protein Carabin

Pan, F., Sun, L., Kardian, D., Whartenby, K. A., Pardoll, D. M., & Liu, J. O. (2007) · Nature · doi:10.1038/nature05476 · Cited by 72 · see citing works

Molecular cloning of a cDNA with a novel domain present in the tre-2 oncogene and the yeast cell cycle regulators BUB2 and cdc16.

Richardson, P. M., & Zon, L. I. (1995) · PubMed · Cited by 67 · see citing works

C. elegansRab GTPase activating protein TBC-2 promotes cell corpse degradation by regulating the small GTPase RAB-5

Li, W., Zou, W., Zhao, D., Yan, J., Zhu, Z., Lu, J., & Wang, X. (2009) · Development · doi:10.1242/dev.035949 · Cited by 65 · see citing works

Identification of three novel proteins (SGSM1, 2, 3) which modulate small G protein (RAP and RAB)-mediated signaling pathway

Yang, H., Sasaki, T., Minoshima, S., & Shimizu, N. (2007) · Genomics · doi:10.1016/j.ygeno.2007.03.013 · Cited by 59 · see citing works

Novel Rab GAP-like Protein, CIP85, Interacts with Connexin43 and Induces Its Degradation

Zheng, L., Kurata, W. E., Martyn, K. D., Jin, C., & Lau, A. F. (2005) · Biochemistry · doi:10.1021/bi048306w · Cited by 55 · see citing works

The Primate-specific Protein TBC1D3 Is Required for Optimal Macropinocytosis in a Novel ARF6-dependent Pathway

Frittoli, E., Palamidessi, A., Pizzigoni, A., Lanzetti, L., Garrè, M., Troglio, F., Troilo, A., Fukuda, M., Fiore, P. P. D., Scita, G., et al. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-06-0594 · Cited by 54 · see citing works

Identification and characterization of a novel Tre‐2/Bub2/Cdc16 (TBC) protein that possesses Rab3A‐GAP activity

Ishibashi, K., Kanno, E., Itoh, T., & Fukuda, M. (2008) · Genes to Cells · doi:10.1111/j.1365-2443.2008.01251.x · Cited by 52 · see citing works

Activation of an oncogenic TBC1D7 (TBC1 domain family, member 7) protein in pulmonary carcinogenesis

Sato, N., Koinuma, J., Ito, T., Tsuchiya, E., Kondo, S., Nakamura, Y., & Daigo, Y. (2010) · Genes Chromosomes and Cancer · doi:10.1002/gcc.20747 · Cited by 41 · see citing works

Serological Cloning of PARIS-1: A New TBC Domain-Containing, Immunogenic Tumor Antigen from a Prostate Cancer Cell Line

Zhou, Y., Toth, M., Hamman, M. S., Monahan, S. J., Lodge, P. A., Boynton, A. L., & Salgaller, M. L. (2002) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.6257 · Cited by 35 · see citing works

RN-tre identifies a family of tre-related proteins displaying a novel potential protein binding domain.

Matoskova, B., Wt, W., Seki, N., Nagase, T., Nomura, N., Robbins, K. C., & Fiore, D. (1996) · PubMed · Cited by 30 · see citing works

Proviral integrations at the Evi5 locus disrupt a novel 90 kDa protein with homology to the Tre2 oncogene and cell-cycle regulatory proteins

Liao, X.-B., Du, Y., Morse, H. C., Jenkins, N. A., & Copeland, N. G. (1997) · Oncogene · doi:10.1038/sj.onc.1200929 · Cited by 28 · see citing works

How can mammalian Rab small GTPases be comprehensively analyzed?: Development of new tools to comprehensively analyze mammalian Rabs in membrane traffic.

Fukuda, M. (2010) · PubMed · doi:10.14670/hh-25.1473 · Cited by 27 · see citing works

Ornithine aminotransferase-related sequences map to two nonadjacent intervals on the human X chromosome short arm

Lafrenière, R. G., Geraghty, M. T., Valle, D. L., Shows, T. B., & Willard, H. F. (1991) · Genomics · doi:10.1016/0888-7543(91)90512-d · Cited by 18 · see citing works

RABGAP1L gene rearrangement resulting from a der(Y)t(Y;1)(q12;q25) in acute myeloid leukemia arising in a child with Klinefelter syndrome

Roberti, M. C., Starza, R. L., Surace, C., Sirleto, P., Pinto, R. M., Pierini, V., Crescenzi, B., Mecucci, C., & Angioni, A. (2009) · Archiv für Pathologische Anatomie und Physiologie und für Klinische Medicin · doi:10.1007/s00428-009-0732-z · Cited by 16 · see citing works

Identification of a Novel Nurr1-Interacting Protein

Luo, Y., Xing, F., Guiliano, R., & Federoff, H. J. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.3021-08.2008 · Cited by 14 · see citing works

Antisense Display: A New Method for Functional Gene Screen and Its Application to Angiogenesis‐Related Gene Isolation

Yonekura, H., Yasui, K., Sakurai, S., LI, H., Yamamoto, Y., & Yamamoto, H. (2001) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2001.tb03968.x · Cited by 5 · see citing works

Exercise, GLUT4, and skeletal muscle glucose uptake

Richter, E. A., & Hargreaves, M. (2013) · Physiological Reviews · doi:10.1152/physrev.00038.2012 · Cited by 1,407 · see citing works

Regulation of Small GTPases by GEFs, GAPs, and GDIs

Cherfils, J., & Zeghouf, M. (2013) · Physiological Reviews · doi:10.1152/physrev.00003.2012 · Cited by 1,245 · see citing works

Molecular mechanisms of ROS production and oxidative stress in diabetes

Newsholme, P., Cruzat, V. F., Keane, K. N., Carlessi, R., & de Bittencourt, P. I. H. (2016) · Biochemical Journal · doi:10.1042/bcj20160503c · Cited by 878 · see citing works

Rab family of small GTPases: an updated view on their regulation and functions

Homma, Y., Hiragi, S., & Fukuda, M. (2020) · FEBS Journal · doi:10.1111/febs.15453 · Cited by 468 · see citing works

Multiple Roles of the Small GTPase Rab7

Guerra, F., & Bucci, C. (2016) · Cells · doi:10.3390/cells5030034 · Cited by 394 · see citing works

Rab GTPase regulation of membrane identity

Pfeffer, S. R. (2013) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2013.04.002 · Cited by 319 · see citing works

Mitochondrial Rab GAPs govern autophagosome biogenesis during mitophagy

Yamano, K., Fogel, A. I., Wang, C., van der Bliek, A. M., & Youle, R. J. (2014) · eLife · doi:10.7554/elife.01612 · Cited by 307 · see citing works

AMPK: energy sensor and survival mechanism in the ischemic heart

Qi, D., & Young, L. H. (2015) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2015.05.010 · Cited by 285 · see citing works

Rab27 Effectors, Pleiotropic Regulators in Secretory Pathways

Fukuda, M. (2013) · Traffic · doi:10.1111/tra.12083 · Cited by 235 · see citing works

Molecular control of Rab activity by GEFs, GAPs and GDI

Müller, M. P., & Goody, R. S. (2017) · Small GTPases · doi:10.1080/21541248.2016.1276999 · Cited by 229 · see citing works

Illuminating the functional and structural repertoire of human TBC/RABGAPs

Frasa, M. A. M., Koessmeier, K. T., Ahmadian, M. R., & Braga, V. M. M. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3267 · Cited by 182 · see citing works

OATL1, a novel autophagosome-resident Rab33B-GAP, regulates autophagosomal maturation

Itoh, T., Kanno, E., Uemura, T., Waguri, S., & Fukuda, M. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201008107 · Cited by 174 · see citing works

Fis1 acts as a mitochondrial recruitment factor for TBC1D15 that is involved in regulation of mitochondrial morphology

Onoue, K., Jofuku, A., Ban-Ishihara, R., Ishihara, T., Maeda, M., Koshiba, T., Itoh, T., Fukuda, M., Otera, H., Oka, T., et al. (2012) · Journal of Cell Science · doi:10.1242/jcs.111211 · Cited by 158 · see citing works

The Paradox of Akt-mTOR Interactions

Vadlakonda, L., Dash, A., Pasupuleti, M., Kumar, K. A., & Reddanna, P. (2013) · Frontiers in Oncology · doi:10.3389/fonc.2013.00165 · Cited by 149 · see citing works

The role of ALFY in selective autophagy

Isakson, P., Holland, P., & Simonsen, A. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.66 · Cited by 129 · see citing works

A Bacterial Pathogen Targets a Host Rab-Family GTPase Defense Pathway with a GAP

Spanò, S., Gao, X., Hannemann, S., Lara-Tejero, M., & Galán, J. E. (2016) · Cell Host & Microbe · doi:10.1016/j.chom.2016.01.004 · Cited by 126 · see citing works

<i>TBC1D24</i> genotype–phenotype correlation: Epilepsies and other neurologic features

Balestrini, S., Milh, M., Castiglioni, C., Lüthy, K., Finelli, M. J., Verstreken, P., Cardon, A., Stražišar, B. G., Holder, J. L., Lesca, G., et al. (2016) · Neurology · doi:10.1212/wnl.0000000000002807 · Cited by 124 · see citing works

Insulin and AMPK regulate FA translocase/CD36 plasma membrane recruitment in cardiomyocytes via Rab GAP AS160 and Rab8a Rab GTPase

Samovski, D., Su, X., Xu, Y., Abumrad, N. A., & Stahl, P. D. (2012) · Journal of Lipid Research · doi:10.1194/jlr.m023424 · Cited by 120 · see citing works

SKIP‐HOPS recruits TBC1D15 for a Rab7‐to‐Arl8b identity switch to control late endosome transport

Jongsma, M. L. M., Bakker, J., Cabukusta, B., Liv, N., van Elsland, D. M., Fermie, J., Akkermans, J. J. L. L., Kuijl, C. P., van der Zanden, S. Y., Janssen, L., et al. (2020) · The EMBO Journal · doi:10.15252/embj.2019102301 · Cited by 113 · see citing works

DUBs, the regulation of cell identity and disease

Heideker, J., & Wertz, I. E. (2014) · Biochemical Journal · doi:10.1042/bj20140496 · Cited by 100 · see citing works

TBC1D23 is a bridging factor for endosomal vesicle capture by golgins at the trans-Golgi

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The interplay between the Rab27A effectors Slp4-a and MyRIP controls hormone-evoked Weibel-Palade body exocytosis

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TBC1D15-Drp1 interaction-mediated mitochondrial homeostasis confers cardioprotection against myocardial ischemia/reperfusion injury

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Glucose transporter 4: Insulin response mastermind, glycolysis catalyst and treatment direction for cancer progression

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The G2019S variant of leucine-rich repeat kinase 2 (LRRK2) alters endolysosomal trafficking by impairing the function of the GTPase RAB8A

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Connecting rules from paired miRNA and mRNA expression data sets of HCV patients to detect both inverse and positive regulatory relationships

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Evi5 promotes collective cell migration through its Rab-GAP activity

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Genome-wide Investigation of the Rab Binding Activity of RUN Domains: Development of a Novel Tool that Specifically Traps GTP-Rab35

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Recessive Inactivating Mutations in TBCK, Encoding a Rab GTPase-Activating Protein, Cause Severe Infantile Syndromic Encephalopathy

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Optineurin mediates negative regulation of Rab8 function by TBC1D17, a GTPase activating protein

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Homozygous Mutations in TBC1D23 Lead to a Non-degenerative Form of Pontocerebellar Hypoplasia

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A Rab11a-Rab8a-Myo5B network promotes stretch-regulated exocytosis in bladder umbrella cells

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Connecdenn 3/DENND1C binds actin linking Rab35 activation to the actin cytoskeleton

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Homozygous Truncating Variants in TBC1D23 Cause Pontocerebellar Hypoplasia and Alter Cortical Development

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TBC1D9B functions as a GTPase-activating protein for Rab11a in polarized MDCK cells

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TBC1D8B Loss-of-Function Mutations Lead to X-Linked Nephrotic Syndrome via Defective Trafficking Pathways

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AMPK-mediated phosphorylation enhances the auto-inhibition of TBC1D17 to promote Rab5-dependent glucose uptake

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Specific TBC Domain-Containing Proteins Control the ER-Golgi-Plasma Membrane Trafficking of GPCRs

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Rabex-5 Protein Regulates Dendritic Localization of Small GTPase Rab17 and Neurite Morphogenesis in Hippocampal Neurons

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Cardiac contraction-induced GLUT4 translocation requires dual signaling input

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Ablating the protein TBC1D1 impairs contraction-induced sarcolemmal glucose transporter 4 redistribution but not insulin-mediated responses in rats

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RUTBC1 Functions as a GTPase-activating Protein for Rab32/38 and Regulates Melanogenic Enzyme Trafficking in Melanocytes

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TBC1D8B Mutations Implicate RAB11-Dependent Vesicular Trafficking in the Pathogenesis of Nephrotic Syndrome

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Inter-Organelle Membrane Contact Sites and Mitochondrial Quality Control during Aging: A Geroscience View

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The taming of a Rab GTPase byLegionella pneumophila

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TBC1D18 is a Rab5-GAP that coordinates endosome maturation together with Mon1

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Free cholesterol accumulation in liver sinusoidal endothelial cells exacerbates acetaminophen hepatotoxicity via TLR9 signaling

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Small GTPases of the Rab and Arf Families: Key Regulators of Intracellular Trafficking in Neurodegeneration

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Deficiency of the Tbc1d21 gene causes male infertility with morphological abnormalities of the sperm mitochondria and flagellum in mice

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The LMTK1-TBC1D9B-Rab11A Cascade Regulates Dendritic Spine Formation via Endosome Trafficking

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The phenotypic landscape of a Tbc1d24 mutant mouse includes convulsive seizures resembling human early infantile epileptic encephalopathy

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LRRK2-Related Parkinson’s Disease Due to Altered Endolysosomal Biology With Variable Lewy Body Pathology: A Hypothesis

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Collagen secretion screening in Drosophila supports a common secretory machinery and multiple Rab requirements

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The BLOC-3 subunit HPS4 is required for activation of Rab32/38 GTPases in melanogenesis, but its Rab9 activity is dispensable for melanogenesis

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FgSpa2 recruits FgMsb3, a Rab8 GAP, to the polarisome to regulate polarized trafficking, growth and pathogenicity in Fusarium graminearum

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Glucose Uptake in the Human Pathogen Schistosoma mansoni Is Regulated Through Akt/Protein Kinase B Signaling

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A tumor-specific modulation of heterogeneous ribonucleoprotein A0 promotes excessive mitosis and growth in colorectal cancer cells

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Nephrotic Syndrome Gene TBC1D8B Is Required for Endosomal Maturation and Nephrin Endocytosis in Drosophila

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The GTPase-deficient Rab27A(Q78L) Mutant Inhibits Melanosome Transport in Melanocytes through Trapping of Rab27A Effector Protein Slac2-a/Melanophilin in Their Cytosol

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EPI64 interacts with Slp1/JFC1 to coordinate Rab8a and Arf6 membrane trafficking

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Expression pattern and signalling pathways in neutrophil like HL-60 cells after treatment with estrogen receptor selective ligands

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EVI5 is an oncogene that regulates the proliferation and metastasis of NSCLC cells

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Porcine reproductive and respiratory syndrome virus 2 hijacks CMA-mediated lipolysis through upregulation of small GTPase RAB18

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Small GTPases in peroxisome dynamics

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Calcium signaling recruits substrate transporters GLUT4 and CD36 to the sarcolemma without increasing cardiac substrate uptake

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Novel Host Protein TBC1D16, a GTPase Activating Protein of Rab5C, Inhibits Prototype Foamy Virus Replication

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TBC1D3 regulates the payload and biological activity of extracellular vesicles that mediate tissue repair

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Dysfunction of RAB39B‐ Mediated Vesicular Trafficking in Lewy Body Diseases

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TBC1D12 is a novel Rab11-binding protein that modulates neurite outgrowth of PC12 cells

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Deletion of the Rab GAP Tbc1d1 modifies glucose, lipid, and energy homeostasis in mice

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