Targeting of MIST to Src-family kinases via SKAP55-SLAP-130 adaptor complex in mast cells

被引:20
作者
Fujii, Y
Wakahara, S
Nakao, T
Hara, T
Ohtake, H
Komurasaki, T
Kitamura, K
Tatsuno, A
Fujiwara, N
Hozumi, N
Ra, C
Kitamura, D
Goitsuka, R
机构
[1] Sci Univ Tokyo, Res Inst Biol Sci, Noda, Chiba 2780022, Japan
[2] Taisho Pharmaceut Co Ltd, Dept Mol Biol Lab, Med Res Labs, Omiya, Saitama 3308530, Japan
[3] Taisho Pharmaceut Co Ltd, Eth Business Strategy Div, Med Res Labs, Omiya, Saitama 3308530, Japan
[4] Nihon Univ, Sch Med, Dept Mol Cell Immunol & Allergol, Adv Med Res Ctr, Tokyo, Japan
[5] Sci Univ Tokyo, Genome & Drug Res Ctr, Noda, Chiba 2780022, Japan
关键词
signal transduction; protein tyrosine kinase; mast cell; IgE receptor; adaptor;
D O I
10.1016/S0014-5793(03)00234-5
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
MIST (mast cell immunoreceptor signal transducer; also termed Clnk) is an adaptor protein structurally related to SLP-76-family hematopoietic cell-specific adaptor proteins. We demonstrate here that two major MIST-associated phosphoproteins expressed in mast cell lines are SLAP-130 and SKAP55, adaptors known to interact with the Src-homology (SH) 2 domain of Src-family protein tyrosine kinases (PTKs). MIST directly associated with SLAP-130 via its SH2 domain, and collaboration of SLAP-130 with SKAP55 was required for the recruitment of MIST to Lyn. Furthermore, MIST was preferentially recruited to Fyn rather than Lyn, which is regulated by higher affinity binding of SLAP-130 and SKAP55 with the Fyn-SH2 domain than the Lyn-SH2 domain. Our results suggest that the MIST-SLAP-130-SKAP55 adaptor complex functions downstream of high-affinity IgE receptor-associated Src-PTKs in mast cells. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码:111 / 116
页数:6
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