title: A modification switch on a molecular switch: Phosphoregulation of Rab7 during endosome maturation.
abstract: Rab GTPases, the highly conserved members of Ras GTPase superfamily are the pivotal regulators of vesicle-mediated trafficking. Rab GTPases, each with a specific subcellular localization, exert tremendous control over various aspects of vesicular transport, identity and dynamics. Several lines of research have established that GDI, GEFs and GAPs are the critical players to orchestrate Rab GTPase activity and function. The importance of post translational modifications in Rab GTPase functional regulation is poorly or not yet been addressed except for prenylation. Our recent study has revealed a novel dephosphorylation dependent regulatory mechanism for Rab7 activity and function. We have shown the importance of PTEN mediated dephosphorylation of Rab7 on highly conserved S72 and Y183 residues, which is essential for its GDI mediated membrane targeting and further activation by GEF. In conclusion, our study highlighted the importance of a phosphorylation/dephosphorylation switch in controlling timely Rab7 localization and activity on endosomes.
authors.affiliation: a Laboratory of Cell Death & Cell Survival, Centre for DNA Fingerprinting and Diagnostics (CDFD), Nampally , Hyderabad , India.|b Graduate Studies, Manipal University , Manipal , India.
authors.forename: Swapnil Rohidas
authors.initials: SR
authors.lastname: Shinde
authors.affiliation: a Laboratory of Cell Death & Cell Survival, Centre for DNA Fingerprinting and Diagnostics (CDFD), Nampally , Hyderabad , India.
authors.forename: Subbareddy
authors.initials: S
authors.lastname: Maddika
mesh_terms: D011992:Endosomes / Q000378:metabolism*; D006801:Humans; D010766:Phosphorylation; D020691:rab GTP-Binding Proteins / Q000378:metabolism*; D000090802:rab7 GTP-Binding Proteins
chemical_list: D000090802:rab7 GTP-Binding Proteins; C000716463:rab7 GTP-binding proteins, human; D020691:rab GTP-Binding Proteins
keywords: PTEN; Rab7; endosome; membrane trafficking; phosphorylation