RhoD Binds the Rab5 Effector Rabankyrin‐5 and has a Role in Trafficking of the Platelet‐derived Growth Factor Receptor. (10th October 2013)

• Record Type: Journal Article
• Authors: Nehru, Vishal; Voytyuk, Oleksandr; Lennartsson, Johan; Aspenström, Pontus
• Is Part Of: Traffic. Volume 14:Number 12(2013:Dec.)
• Page Start: 1242
• Page End: 1254
• Publication Date: 2013-10-10
• Subjects: Endosome -- PDGF receptor -- Rho GTPases -- RhoD -- Rab5 -- Rabankyrin‐5; Biological transport -- Periodicals; 571.6
• DOI: 10.1111/tra.12121
• Languages: English
• ISSNs: 1398-9219

Abstract

Abstract : We discovered that RhoD binds to the Rab5 effector Rabankyrin‐5, and RhoD and Rabankyrin‐5 colocalize to Rab5‐positive endosomes, which suggests a role for Rabankyrin‐5 in the coordination of RhoD and Rab5 in endosomal trafficking. Depletion of RhoD using siRNA techniques interfered with the internalization of the PDGF β receptor and the subsequent activation of the downstream signaling cascades. Our data implicate that RhoD and Rabankyrin‐5 have important roles in coordinating RhoD and Rab activities during trafficking of the PDGF β receptor. Abstract : RhoD is a member of the classical Rho GTPases and it has essential roles in the regulation of actin dynamics. RhoD localizes to early endosomes and recycling endosomes, which indicates its important role in the regulation of endosome trafficking. Here, we show that RhoD binds to the Rab5 effector Rabankyrin‐5, and RhoD and Rabankyrin‐5 colocalize to Rab5‐positive endosomes, which suggests a role for Rabankyrin‐5 in the coordination of RhoD and Rab5 in endosomal trafficking. Interestingly, depletion of RhoD using siRNA techniques interfered with the internalization of the PDGFβ receptor and the subsequent activation of the downstream signaling cascades. Our data suggest that RhoD and Rabankyrin‐5 have important roles in coordinating RhoD and Rab activities during internalization and trafficking of activated tyrosine kinase receptors .