TBC1D15 accelerates GTP hydrolysis by RAB7

Stable Identifier
Reaction [transition]
Homo sapiens
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The small GTPase Rab7 promotes fusion events between late endosomes and lysosomes. TBC domain family, member 15 (TAB1CD15) is ubiquitously expressed and localized predominantly to the cytosol. TBC1D15 stimulates the intrinsic GTPase activity of Rab7, reducing Rab7 binding to its effector protein RILP, fragmenting the lysosome, and conferring resistance to growth factor withdrawal-induced cell death (Zhang et al. 2005, Peralta et al. 2010).

Literature References
PubMed ID Title Journal Year
16055087 TBC domain family, member 15 is a novel mammalian Rab GTPase-activating protein with substrate preference for Rab7

Mitchell, CA, Zhang, XM, Walsh, B, Rowe, T

Biochem. Biophys. Res. Commun. 2005
20363736 Differential effects of TBC1D15 and mammalian Vps39 on Rab7 activation state, lysosomal morphology, and growth factor dependence

Martin, BC, Peralta, ER, Edinger, AL

J. Biol. Chem. 2010
Catalyst Activity

GTPase activity of RAB7:GTP [lysosomal membrane]

This event is regulated
Positively by
Orthologous Events
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