Fyn binds to and phosphorylates T cell immunoglobulin and mucin domain-1 (Tim-1)

被引：17

作者：

Curtiss, Miranda L. ^{[1
,2
,3
]}

Hostager, Bruce S. ^{[1
]}

Stepniak, Elizabeth ^{[1
]}

Singh, Melody ^{[1
]}

Manhica, Natalie ^{[1
]}

Knisz, Judit ^{[1
]}

Traver, Geri ^{[1
]}

Rennert, Paul D. ^{[4
]}

Colgan, John D. ^{[1
]}

Rothman, Paul B. ^{[1
]}

机构：

[1] Univ Iowa, Dept Internal Med, Carver Coll Med, Iowa City, IA 52242 USA

[2] Univ Iowa, Med Scientist Training Program, Carver Coll Med, Iowa City, IA 52242 USA

[3] Univ Iowa, Interdisciplinary Grad Program Immunol, Carver Coll Med, Iowa City, IA 52242 USA

[4] Biogen Idec Inc, Cambridge, MA 01746 USA

来源：

MOLECULAR IMMUNOLOGY | 2011年 / 48卷 / 12-13期

关键词：

Tim-1; Havcr-1; B cell; Fyn; Signaling; MONKEY KIDNEY-CELLS; HEPATITIS-A VIRUS; IG-ALPHA; PHOSPHATIDYLSERINE RECEPTOR; HUMORAL IMMUNITY; APOPTOTIC CELLS; B-CELLS; ACTIVATION; FAMILY; IDENTIFICATION;

D O I：

10.1016/j.molimm.2011.03.023

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 gene encoding T cell immunoglobulin and mucin domain-1 (Tim-1) is linked to atopy and asthma susceptibility in mice and humans. Tim-1 is a transmembrane protein expressed on activated lymphocytes and appears to have a role as a co-stimulatory receptor in T cells. The protein has not been shown to have enzymatic activity but contains a site within its cytoplasmic tail predicted to be a target for tyrosine kinases. Here, we show that Tim-1 can associate with the kinase Fyn, a member of the Src family of tyrosine kinases. This association does not require Fyn's kinase activity and is independent of the phosphorylation of a conserved tyrosine present within the cytoplasmic tail of Tim-1. Fyn is necessary for phosphorylation of this tyrosine in Tim-1 and the phosphorylation of Tim-1 varies with the levels of Fyn present in cells. These data suggest a role for Fyn in the signaling downstream of Tim-1. (C) 2011 Elsevier Ltd. All rights reserved.

引用

页码：1424 / 1431

页数：8

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