TBC1D2A accelerates GTP hydrolysis by RAB7

Stable Identifier
Reaction [transition]
Homo sapiens
TBC1D2A accerlates GTP hydrolysis by RAB7
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RAB7, a small GTPase of the Rab family is associated with both endosomes and lysosomes. It facilitates endosomal maturation, transport from late endosomes to lysosomes, and the positioning of endosomes and lysosomes via regulating their movement along the cytoskeleton. RAB7 is inactivated through hydrolysis of bound GTP into GDP by its intrinsic GTPase activity, which is catalysed by the activity of a GAP (GTPase activating protein).
TBC1 domain family member 2A (TBC1D2A also referred as ARMUS for variant c; PARIS1 for variant a) is a member of the TBC/RabGAP family (Tre2/Bub2/Cdc16; TBC domain) that specifically inactivates RAB7 by accelerating its GTPase activity. TBC1D2A binds specifically to activated Rac1 and its C-terminal TBC/RabGAP domain inactivates RAB7 to promote ARF6-induced E-Cadherin degradation (Frasa et al. 2010). During the regulation of autophagy, TBC1D2A is recruited to autophagosomes by interacting with LC3, a core autophagy regulator, thereby inhibiting RAB7 (Carroll et al. 2013)
Literature References
PubMed ID Title Journal Year
23562278 The TBC/RabGAP Armus coordinates Rac1 and Rab7 functions during autophagy

Mohd-Naim, N, Frasa, MA, Braga, VM, Dikic, I, Perdios, L, Finelli, M, McCormack, J, Futter, C, Carroll, B, Maximiano, F, Francis, RE, Daigaku, R, Thoresen, SB

Dev. Cell 2013
20116244 Armus is a Rac1 effector that inactivates Rab7 and regulates E-cadherin degradation

Seabra, MC, Smolarczyk, K, Rak, A, Frasa, MA, Braga, VM, Ahmadian, MR, Betson, ME, Maximiano, FC, Francis, RE, Goldenring, J, Lozano, E

Curr. Biol. 2010
Catalyst Activity

GTPase activity of RAB7A:GTP [lysosomal membrane]

This event is regulated
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