Volume 20, No 2, Feb 2010

ISSN: 1001-0602 
EISSN: 1748-7838 2018 
impact factor 17.848* 
(Clarivate Analytics, 2019)

Volume 20 Issue 2, February 2010: 223-237

ORIGINAL ARTICLES

Endocytosis of FcαR is clathrin and dynamin dependent, but its cytoplasmic domain is not required

Min Peng, Na Yin and Wei Zhang

Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences, School of Basic Medicine, Peking Union Medical College, Beijing 100005, China Correspondence: Wei Zhang,(wzhang@pumc.edu.cn )

FcαR, the Fc receptor for IgA, is essential for IgA-mediated immune responses. Previous studies have shown that IgA and IgA immune complexes can be rapidly endocytosed by FcαR. However, the underlying mechanism remains unclear. Here, we investigated the endocytic pathway of FcαR in monocytic cell line, U937, that naturally express FcαR and in transfected Chinese hamster ovary (CHO), COS-7 and Hela cells. By using selective chemical inhibitors of different endocytic pathways, overexpression of dominant-negative mutants of Eps15 and knockdown of clathrin heavy chain (CHC) via RNA interference, we demonstrated that endocytosis of FcαR was through a clathrin-mediated pathway. The endocytosed FcαR went into Rab5- and Rab11-positive endosomes. However, endocytosis of FcαR could not be blocked by a dominant-negative mutant of Rab5. We also demonstrated that endocytosis of FcαR was dynamin-dependent by overexpressing a dominant-negative mutant of dynamin. The potential endocytic motif for FcαR was also examined. Unexpectedly, we found that the entire cytoplasmic domain of FcαR was not required for the endocytic process of FcαR. We conclude that endocytosis of FcαR is clathrin- and dynamin-dependent, but is not regulated by Rab5, and the endocytic motif is not located in the cytoplasmic domain of FcαR.

Cell Research (2010) 20:223-237. doi: 10.1038/cr.2009.120; published online 27 October 2009

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