PT  - JOURNAL ARTICLE
AU  - Etoh, Kan
AU  - Fukuda, Mitsunori
TI  - Rab10 regulates tubular endosome formation through KIF13A and KIF13B motors
AID  - 10.1242/jcs.226977
DP  - 2019 Mar 01
TA  - Journal of Cell Science
PG  - jcs226977
VI  - 132
IP  - 5
4099  - http://jcs.biologists.org/content/132/5/jcs226977.short
4100  - http://jcs.biologists.org/content/132/5/jcs226977.full
SO  - J. Cell Sci.2019 Mar 01; 132
AB  - Recycling endosomes are stations that sort endocytic cargoes to their appropriate destinations. Tubular endosomes have been characterized as a recycling endosomal compartment for clathrin-independent cargoes. However, the molecular mechanism by which tubular endosome formation is regulated is poorly understood. In this study, we identified Rab10 as a novel protein localized at tubular endosomes by using a comprehensive localization screen of EGFP-tagged Rab small GTPases. Knockout of Rab10 completely abolished tubular endosomal structures in HeLaM cells. We also identified kinesin motors KIF13A and KIF13B as novel Rab10-interacting proteins by means of in silico screening. The results of this study demonstrated that both the Rab10-binding homology domain and the motor domain of KIF13A are required for Rab10-positive tubular endosome formation. Our findings provide insight into the mechanism by which the Rab10–KIF13A (or KIF13B) complex regulates tubular endosome formation. This article has an associated First Person interview with the first author of the paper.