Rab18 regulates focal adhesion dynamics by interacting with kinectin-1 at the endoplasmic reticulum.

ABSTRACT: The members of the Rab family of small GTPases are molecular switches that regulate distinct steps in different membrane traffic pathways. In addition to this canonical function, Rabs can play a role in other processes, such as cell adhesion and motility. Here, we reveal the role of the small GTPase Rab18 as a positive regulator of directional migration in chemotaxis, and the underlying mechanism. We show that knockdown of Rab18 reduces the size of focal adhesions (FAs) and influences their dynamics. Furthermore, we found that Rab18, by directly interacting with the endoplasmic reticulum (ER)-resident protein kinectin-1, controls the anterograde kinesin-1-dependent transport of the ER required for the maturation of nascent FAs and protrusion orientation toward a chemoattractant. Altogether

SUBMITTER: Guadagno NA 

PROVIDER: S-EPMC7337506 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature