| Literature DB >> 26987402 |
Ximing Shao1, Yi Liu1,2,3, Qian Yu1,2, Zhihao Ding1, Wenyu Qian2,4, Lei Zhang1, Jianchao Zhang1, Nan Jiang2,5, Linfei Gui1, Zhiheng Xu6, Yang Hong7, Yifan Ma1, Yanjie Wei1, Xiaoqing Liu4, Changan Jiang1,2, Minyan Zhu4, Hongchang Li1, Huashun Li4,8.
Abstract
Numb is an endocytic protein that plays crucial roles in diverse cellular processes such as asymmetric cell division, cell migration and differentiation. However, the molecular mechanism by which Numb regulates endocytic trafficking is poorly understood. Here, we demonstrate that Numb is a docking regulator for homotypic fusion of early endosomes (EEs). Numb depletion causes clustered but unfused EEs, which can be rescued by overexpressing cytosolic Numb 65 and Numb 71 but not plasma membrane-attached Numb 66 or Numb 72. Time-lapse analysis reveals that paired vesicles tend to tether but not fuse with each other in the absence of Numb. We further show that Numb binds to another docking regulator, Mon1b, and is required for the recruitment of cytosolic Mon1b to the EE membrane. Consistent with this, deletion of Mon1b causes similar defects in EE fusion. Our study thus identifies a novel mechanism by which Numb regulates endocytic sorting by mediating EE fusion.Entities:
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Year: 2016 PMID： 26987402 PMCID： PMC4856763 DOI： 10.1038/cr.2016.34
Source DB: PubMed Journal: Cell Res ISSN： 1001-0602 Impact factor: 25.617