Vav and Rac Activation in B Cell Antigen Receptor Endocytosis Involves Vav Recruitment to the Adapter Protein LAB

被引:28
作者
Malhotra, Shikha [1 ,2 ]
Kovats, Susan [3 ]
Zhang, Weiguo [4 ]
Coggeshall, K. Mark [1 ,2 ]
机构
[1] Univ Oklahoma, Immunobiol & Canc Program, Oklahoma Med Res Fdn, Oklahoma City, OK 73104 USA
[2] Univ Oklahoma, Dept Cell Biol, Oklahoma City, OK 73104 USA
[3] Oklahoma Med Res Fdn, Arthritis & Immunol Program, Oklahoma City, OK 73104 USA
[4] Duke Univ, Med Ctr, Dept Immunol, Durham, NC 27710 USA
关键词
NUCLEOTIDE EXCHANGE FACTOR; INOSITOL PHOSPHATASE SHIP; FC-GAMMA-RIIB; T-CELLS; TYROSINE PHOSPHORYLATION; DIFFERENTIAL REGULATION; SIGNALING PATHWAYS; SH2; DOMAIN; GTPASES; INTERNALIZATION;
D O I
10.1074/jbc.M109.040089
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The signal transduction events supporting B cell antigen receptor (BCR) endocytosis are not well understood. We have identified a pathway supporting BCR internalization that begins with tyrosine phosphorylation of the adapter protein LAB. Phosphorylated LAB recruits a complex of Grb2-dynamin and the guanine nucleotide exchange factor Vav. Vav is required for activation of the small GTPases Rac1 and Rac2. All these proteins contribute to (and dynamin, Vav, and Rac1/2 are required for) BCR endocytosis and presentation of antigen to T cells. This is the first description of a sequential signal transduction pathway from BCR to internalization and antigen presentation.
引用
收藏
页码:36202 / 36212
页数:11
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