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The Findings of Prof. SHI Anbing Featured in the Special Edition of JCB

Author: Source: Date:July 15, 2019 Cilk Times:[]

In July 2019, the Journal of Cell Biology (JCB) published a special edition of highlights: Lipids and Membrane Biology, which selects the cutting-edge research of 27 corresponding authors in the field of international membrane Biology in recent 3 years. Three are 3 authors from China, among whom is Prof. SHI Anbing from Tongji Medical College of HUST.

This special edition takes "number of international peer requests for download, reading feedback, and dissemination of research topics" as objective selection criteria, covering the latest frontier developments in organelle dynamics and function, membrane transport, organelle interactions, protein sorting, lipid homeostasis and transport.Prof. SHI Anbing’s paper“LET-413/Erbin acts as a RAB-5 effector to promote RAB-10 activationduring endocytic recycling”was selected.

The following is the abstract of the paper: RAB-10/Rab10 is a master regulator of endocytic recycling in epithelial cells. To better understand the regulation of RAB-10 activity, we sought to identify RAB-10(GDP)–interacting proteins. One novel RAB-10(GDP)–binding partner that we identified, LET-413, is the Caenorhabditis elegans homologue of Scrib/Erbin. Here, we focus on the mechanistic role of LET-413 in the regulation of RAB-10 within theC. elegansintestine. We show that LET-413 is a RAB-5 effector and colocalizes with RAB-10 on endosomes, and the overlap of LET-413 with RAB-10 is RAB-5 dependent. Notably, LET-413 enhances the interaction of DENN-4 with RAB-10(GDP) and promotes DENN-4 guanine nucleotide exchange factor activity toward RAB-10. Loss of LET-413 leads to cytosolic dispersion of the RAB-10 effectors TBC-2 and CNT-1. Finally, we demonstrate that the loss of RAB-10 or LET-413 results in abnormal overextensions of lateral membrane. Hence, our studies indicate that LET-413 is required for DENN-4–mediated RAB-10 activation, and the LET-413–assisted RAB-5 to RAB-10 cascade contributes to the integrity ofC. elegansintestinal epithelia.


Paper linkage:http://jcb.rupress.org/content/217/1/299?cct=2104

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