酪氨酸激酶p56lck独特的N端区域与CD4和CD8胞质结构域的相互作用是由半胱氨酸基序介导的。

Interaction of the unique N-terminal region of tyrosine kinase p56lck with cytoplasmic domains of CD4 and CD8 is mediated by cysteine motifs.

作者信息

Turner J M, Brodsky M H, Irving B A, Levin S D, Perlmutter R M, Littman D R

机构信息

Department of Microbiology and Immunology, University of California, San Francisco 94143.

出版信息

Cell. 1990 Mar 9;60(5):755-65. doi: 10.1016/0092-8674(90)90090-2.

DOI:10.1016/0092-8674(90)90090-2

PMID:2107025

Abstract

p56lck, a lymphocyte-specific member of the src family of cytoplasmic protein-tyrosine kinases, is associated noncovalently with the cell surface glycoproteins CD4 and CD8, which are expressed on functionally distinct subpopulations of T cells. Using transient coexpression of p56lck with CD4 or CD8 alpha in COS-7 cells, we show that the unique N-terminal region of p56lck binds to the membrane-proximal 10 and 28 cytoplasmic residues of CD8 alpha and CD4, respectively. Two cysteine residues in each of the critical sequences in CD4, CD8 alpha, and p56lck are required for association. Our results suggest a novel role for cysteine-mediated interactions between unrelated proteins and provide a model for the association of other src-like cytoplasmic kinases with transmembrane proteins.

摘要

p56lck是细胞质蛋白酪氨酸激酶src家族的淋巴细胞特异性成员，它与细胞表面糖蛋白CD4和CD8非共价结合，CD4和CD8在功能不同的T细胞亚群上表达。通过在COS-7细胞中瞬时共表达p56lck与CD4或CD8α，我们发现p56lck独特的N端区域分别与CD8α和CD4的膜近端10个和28个细胞质残基结合。CD4、CD8α和p56lck中每个关键序列的两个半胱氨酸残基对于这种结合是必需的。我们的结果提示了半胱氨酸介导的不相关蛋白之间相互作用的新作用，并为其他src样细胞质激酶与跨膜蛋白的结合提供了一个模型。