title: A new V-ATPase regulatory mechanism mediated by the Rab interacting lysosomal protein (RILP).
abstract: Progressive luminal acidification of intracellular compartments is important for their functions. Proton transport into the organelle's lumen is mediated by vacuolar ATPases (V-ATPases) large multi-subunit proton pumps organized into 2 domains, V0 and V1, working together as a rotary machine. The interaction of each subunit with specific partners plays a crucial role in controlling V-ATPase activity. Recently, we have shown that RILP, a Rab7 effector regulating late endocytic traffic and biogenesis of multivesicular bodies (MVBs), is a specific interactor of the V-ATPase subunit V1G1, a fundamental component of the peripheral stalk for correct V-ATPase assembly. RILP controls V1G1 stability and localization affecting V-ATPase assembly and function at the level of endosomes and lysosomes. The discovery of this new regulatory mechanism for V-ATPase opens new scenario to the comprehension of organelle's pH regulation and reveals a key role of RILP in controlling different aspects of endosome to lysosome transport.
authors: Department of Biological and Environmental Sciences and Technologies (DiSTeBA); University of Salento ; Lecce, Italy.
authors: Maria
authors: M
authors: De Luca
authors: Department of Biological and Environmental Sciences and Technologies (DiSTeBA); University of Salento ; Lecce, Italy.
authors: Cecilia
authors: C
authors: Bucci
keywords: Endocytosis; Membrane traffic; RILP; Rab proteins; Rab7; Ubiquitin; V-ATPase; V1G1; atp6v1g1