期刊
JOURNAL OF CELL SCIENCE
卷 132, 期 5, 页码 -出版社
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.226977
关键词
Rab10; Membrane trafficking; Organelle biogenesis; Small GTPase Rab; Tubular endosome
类别
资金
- Ministry of Education, Culture, Sports, Science and Technology (MEXT) of Japan [15H04367]
- MEXT [17H05682]
- Japan Science and Technology Agency (JST) CREST [JPMJCR17H4]
- Japan Society for the Promotion of Science
- Tohoku University Division for interdisciplinary Advanced Research and Education
- Grants-in-Aid for Scientific Research [17H05682] Funding Source: KAKEN
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.
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