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Endophilin plays a central role in endocytic pathway without calthrin

 

Endocytosis is a process that internalize molecules, mostly are large polar molecules, and turnover membrane components. One of the important protein in this process is called endophilin ,which is well-known in clathrin-denpendent endocytosis. Recently, Boucrot et al. demonstrated this protein also participates in a clathrin-independent endocytic pathway, as a central component. The article was published online in Nature.

 

The calthrin-independent endocytic pathway controlled by endophilin is called fast-acting tubulovesicular endocytic (FEME) pathway. The FEME is activated by ligand binding receptors which are recruited by interacting with SH3 domain of endophilin. Other two essential characteristics of endophilin are BAR domain, which act as membrane curvature effector, and multiple amphipathic helices, which enable to scissor membrane with the aid of dynamin. The recruitment of endophilin at plasma membrane is triggered by lamelliphdin, which in turn is mediated by PtdIns(3,4)P2, generated by SHIP1/2 from PtdIns(3,4,5)P3. In addition, the endophilin-mediated FEME pathway can be inhibited by inhibitors of multiple targets including dynamin, Rac, phosphatidylinositol-3-OH kinase, PAK1 and actin polymerization, and be activated by cargoes chalera, shiga toxins and IL-2R. The FEME pathway reveals a role of calthrin-independent pathway in the process of cell endocysis.

 

Reference:
Nature. 2014 Dec 17. 10.1038/nature14067.

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