GPI-anchored proteins are delivered to recycling endosomes via a distinct cdc42-regulated, clathrin-independent pinocytic pathway
GPI-anchored proteins are delivered to recycling endosomes via a distinct cdc42-regulated, clathrin-independent pinocytic pathway
复制标题
DOI：
10.1016/s1534-5807(02)00145-4
复制
发表时间：
2002-04-01
影响因子：
11.8
通讯作者：
Mayor, S
中科院分区：
文献类型：
--
作者：
Sabharanjak, S;Sharma, P;Mayor, S
细胞表面蛋白通过特定途径的内吞作用对其功能至关重要。我们发现，多个糖基磷脂酰肌醇锚定蛋白（GPI-AP）被内吞到回收内体室，但不是通过非网格蛋白，noncaveolae介导的途径到高尔基体。GPI锚定是一个积极的信号，内化到rab 5独立的管状囊泡内体也负责一个主要部分的液相摄取;分子只是缺乏细胞质的延伸不包括在内。与抗洗涤剂膜（DRM）相关的白细胞介素2受体的内化不同，DRM相关的GPI-AP的内吞作用不受RhoA或动力蛋白2活性抑制的影响。抑制Rho家族GT3 cdc 42而非Rac 1，可减少液相摄取并将GPI-AP重新分配至网格蛋白介导的通路。这些结果描述了一个独特的组成性胞饮途径，具体由cdc 42调节。
Endocytosis of cell-surface proteins via specific pathways is critical for their function. We show that multiple glycosylphosphatidylinositol-anchored proteins (GPI-APs) are endocytosed to the recycling endosomal compartment but not to the Golgi via a nonclathrin, noncaveolae mediated pathway. GPI anchoring is a positive signal for internalization into rab5-independent tubular-vesicular endosomes also responsible for a major fraction of fluid-phase uptake; molecules merely lacking cytoplasmic extensions are not included. Unlike the internalization of detergent-resistant membrane (DRM)-associated interleukin 2 receptor, endocytosis of DRM-associated GPI-APs is unaffected by inhibition of RhoA or dynamin 2 activity. Inhibition of Rho family GTPase cdc42, but not Rac1, reduces fluid-phase uptake and redistributes GPI-APs to the clathrin-mediated pathway. These results describe a distinct constitutive pinocytic pathway, specifically regulated by cdc42.