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

The Ras-RasGAP Complex: Structural Basis for GTPase Activation and Its Loss in Oncogenic Ras Mutants

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Rab GTPases as coordinators of vesicle traffic

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

GEFs and GAPs: Critical Elements in the Control of Small G Proteins

Bos, J. L., Rehmann, H., & Wittinghofer, A. (2007) · Cell · doi:10.1016/j.cell.2007.05.018 · Cited by 1,903

Role of Rab GTPases in Membrane Traffic and Cell Physiology

Hutagalung, A. H., & Novick, P. J. (2011) · Physiological Reviews · doi:10.1152/physrev.00059.2009 · Cited by 1,460

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

Membrane recruitment of the cargo-selective retromer subcomplex is catalysed by the small GTPase Rab7 and inhibited by the Rab-GAP TBC1D5

Seaman, M. N. J., Harbour, M. E., Tattersall, D., Read, E., & Bright, N. (2009) · Journal of Cell Science · doi:10.1242/jcs.048686 · Cited by 375

Family-wide characterization of the DENN domain Rab GDP-GTP exchange factors

Yoshimura, S.-I., Gerondopoulos, A., Linford, A., Rigden, D. J., & Barr, F. A. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201008051 · Cited by 317

The cargo-selective retromer complex is a recruiting hub for protein complexes that regulate endosomal tubule dynamics

Harbour, M. E., Breusegem, S. Y. A., Antrobus, R., Freeman, C., Reid, E., & Seaman, M. N. J. (2010) · Journal of Cell Science · doi:10.1242/jcs.071472 · Cited by 246

TBC proteins: GAPs for mammalian small GTPase Rab?

Fukuda, M. (2011) · Bioscience Reports · doi:10.1042/bsr20100112 · Cited by 207

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

The Rap–RapGAP complex: GTP hydrolysis without catalytic glutamine and arginine residues

Scrima, A., Thomas, C., Deaconescu, D., & Wittinghofer, A. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.30 · Cited by 127

Structural and mechanistic insights into regulation of the retromer coat by TBC1d5

Jia, D., Zhang, J.-S., Li, F., Wang, J., Deng, Z., White, M. A., Osborne, D. G., Phillips-Krawczak, C., Gomez, T. S., Li, H., et al. (2016) · Nature Communications · doi:10.1038/ncomms13305 · Cited by 118

Rab35: GEFs, GAPs and Effectors

Chaineau, M., Ioannou, M. S., & McPherson, P. S. (2013) · Traffic · doi:10.1111/tra.12096 · Cited by 114

Inhibition of TBC1D5 activates Rab7a and can enhance the function of the retromer cargo-selective complex

Seaman, M. N. J., Mukadam, A. S., & Breusegem, S. Y. (2018) · Journal of Cell Science · doi:10.1242/jcs.217398 · Cited by 79

Identification of Rab11 as a small GTPase binding protein for the Evi5 oncogene

Westlake, C. J., Junutula, J. R., Simon, G. C., Pilli, M., Prekeris, R., Scheller, R. H., Jackson, P. K., & Eldridge, A. G. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0610500104 · Cited by 64

Skywalker-TBC1D24 has a lipid-binding pocket mutated in epilepsy and required for synaptic function

Fischer, B., Lüthy, K., Paesmans, J., De Koninck, C., Maes, I., Swerts, J., Kuenen, S., Uytterhoeven, V., Verstreken, P., & Versées, W. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3297 · Cited by 62

TBC1D13 is a RAB35 Specific GAP that Plays an Important Role in GLUT4 Trafficking in Adipocytes

Davey, J. R., Humphrey, S. J., Junutula, J. R., Mishra, A. K., Lambright, D. G., James, D. E., & Stöckli, J. (2012) · Traffic · doi:10.1111/j.1600-0854.2012.01397.x · Cited by 53

TBCK Influences Cell Proliferation, Cell Size and mTOR Signaling Pathway

Liu, Y., Yan, X., & Zhou, T. (2013) · PLoS ONE · doi:10.1371/journal.pone.0071349 · Cited by 51

TBC1D5 controls the GTPase cycle of Rab7b

Borg Distefano, M., Hofstad Haugen, L., Wang, Y., Perdreau-Dahl, H., Kjos, I., Jia, D., Morth, J. P., Neefjes, J., Bakke, O., & Progida, C. (2018) · Journal of Cell Science · doi:10.1242/jcs.216630 · Cited by 45

TBC1D16 is a Rab4A GTPase activating protein that regulates receptor recycling and EGF receptor signaling

Goueli, B. S., Powell, M. B., Finger, E. C., & Pfeffer, S. R. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1204540109 · Cited by 41

Structural Basis of the Interaction between Tuberous Sclerosis Complex 1 (TSC1) and Tre2-Bub2-Cdc16 Domain Family Member 7 (TBC1D7)

Qin, J., Wang, Z., Hoogeveen-Westerveld, M., Shen, G., Gong, W., Nellist, M., & Xu, W. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.701870 · Cited by 37

TBC-8, a putative RAB-2 GAP, regulates dense core vesicle maturation in Caenorhabditis elegans

Hannemann, M., Sasidharan, N., Hegermann, J., Kutscher, L. M., Koenig, S., & Eimer, S. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002722 · Cited by 32

Crystal Structures of Human TBC1D1 and TBC1D4 (AS160) RabGTPase-activating Protein (RabGAP) Domains Reveal Critical Elements for GLUT4 Translocation

Park, S.-Y., Jin, W., Woo, J. R., & Shoelson, S. E. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.217323 · Cited by 25

A pathogen effector co-opts a host RabGAP protein to remodel pathogen interface and subvert defense-related secretion

(2024) · doi:10.1126/sciadv.ado9516 · Cited by 19