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

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

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

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 916

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 795

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

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 473

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

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 433

Membrane traffic in the secretory pathway

Fukuda, M. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8351-4 · Cited by 403

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 383

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 379

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 374

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

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 340

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

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

Glucose transporter 4: cycling, compartments and controversies

Dugani, S. B., & Klip, A. (2005) · EMBO Reports · doi:10.1038/sj.embor.7400584 · Cited by 232

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 226

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 222

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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 106

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 105

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

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

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

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

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 90

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 85

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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 482

Multiple Roles of the Small GTPase Rab7

Guerra, F., & Bucci, C. (2016) · Cells · doi:10.3390/cells5030034 · Cited by 414

The critical roles of TBC proteins in human diseases.

Shi, M., Zhang, Y., & Zhou, G. (2018) · PubMed · doi:10.16288/j.yczz.17-343 · Cited by 10

TBC Proteins: Miraculous Regulators of Rabs GTPase Molecular Switches

Yan, J., Zheng, Y., Han, S. H., Yin, J., Li, Y., Chen, T.-X., Peng, B., & Liu, W. (2021) · Biomedical and health research · doi:10.3233/bhr210034 · Cited by 1

First crystallographic models of human TBC domains in the context of a family‐wide structural analysis

Tempel, W., Tong, Y., Dimov, S., Bochkarev, A. V., & Park, H. (2008) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21885 · Cited by 10

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

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