Linked Life Data

19859085

Source:http://linkedlifedata.com/resource/pubmed/id/19859085

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2010-2-1
pubmed:abstractText
FcalphaR, 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 FcalphaR. However, the underlying mechanism remains unclear. Here, we investigated the endocytic pathway of FcalphaR in monocytic cell line, U937, that naturally express FcalphaR 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 FcalphaR was through a clathrin-mediated pathway. The endocytosed FcalphaR went into Rab5- and Rab11-positive endosomes. However, endocytosis of FcalphaR could not be blocked by a dominant-negative mutant of Rab5. We also demonstrated that endocytosis of FcalphaR was dynamin-dependent by overexpressing a dominant-negative mutant of dynamin. The potential endocytic motif for FcalphaR was also examined. Unexpectedly, we found that the entire cytoplasmic domain of FcalphaR was not required for the endocytic process of FcalphaR. We conclude that endocytosis of FcalphaR is clathrin- and dynamin-dependent, but is not regulated by Rab5, and the endocytic motif is not located in the cytoplasmic domain of FcalphaR.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1748-7838
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
223-37
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Endocytosis of FcalphaR is clathrin and dynamin dependent, but its cytoplasmic domain is not required.
pubmed:affiliation
Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences, School of Basic Medicine, Peking Union Medical College, Beijing 100005, China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't