WIPI2B通过结合ATG16L1将磷脂酰肌醇-3-磷酸（PtdIns3P）与LC3脂化连接起来。
WIPI2B links PtdIns3P to LC3 lipidation through binding ATG16L1.
作者信息
Dooley Hannah C, Wilson Michael I, Tooze Sharon A
机构信息
a London Research Institute; Cancer Research UK ; London , UK.
出版信息
Autophagy. 2015;11(1):190-1. doi: 10.1080/15548627.2014.996029.
Abstract
WIPI proteins, phosphatidylinositol 3-phosphate (PtdIns3P) binding proteins with β-propeller folds, are recruited to the omegasome following PtdIns3P production. The functions of the WIPI proteins in autophagosome formation are poorly understood. In a recent study, we reported that WIPI2B directly binds ATG16L1 and functions by recruiting the ATG12-ATG5-ATG16L1 complex to forming autophagosomes during starvation- or pathogen-induced autophagy. Our model of WIPI2 function provides an explanation for the PtdIns3P-dependent recruitment of the ATG12-ATG5-ATG16L1 complex during initiation of autophagy.
摘要
WIPI蛋白是一类具有β-螺旋桨结构域且能结合磷脂酰肌醇3-磷酸（PtdIns3P）的蛋白质，在PtdIns3P产生后被募集到吞噬体前体上。目前对WIPI蛋白在自噬体形成过程中的功能了解甚少。在最近的一项研究中，我们报道WIPI2B直接结合ATG16L1，并通过在饥饿或病原体诱导的自噬过程中将ATG12-ATG5-ATG16L1复合物募集到正在形成的自噬体上发挥作用。我们的WIPI2功能模型为自噬起始过程中ATG12-ATG5-ATG16L1复合物的PtdIns3P依赖性募集提供了解释。
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