INTERACTION OF THE UNIQUE N-TERMINAL REGION OF TYROSINE KINASE P56LCK WITH CYTOPLASMIC DOMAINS OF CD4 AND CD8 IS MEDIATED BY CYSTEINE MOTIFS
INTERACTION OF THE UNIQUE N-TERMINAL REGION OF TYROSINE KINASE P56LCK WITH CYTOPLASMIC DOMAINS OF CD4 AND CD8 IS MEDIATED BY CYSTEINE MOTIFS
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DOI：
10.1016/0092-8674(90)90090-2
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发表时间：
1990-03-09
期刊：
影响因子：
64.5
通讯作者：
LITTMAN, DR
中科院分区：
文献类型：
--
作者：
TURNER, JM;BRODSKY, MH;LITTMAN, DR
P56lck是细胞质蛋白酪氨酸激酶src家族中淋巴细胞特异的成员，它与细胞表面糖蛋白CD4和CD8非共价相关，这两种糖蛋白表达在功能不同的T细胞亚群上。用瞬时共表达p56lck与CD4或CD8α共表达。在COS-7细胞中，我们发现p56lck的独特的N末端区域与CD8α的膜近端10和28细胞质残基结合。和CD4。需要在CD4、CD8α和p56lck的每个关键序列中有两个半胱氨酸残基才能结合。我们的结果提示了半胱氨酸介导的无关蛋白之间的相互作用的一个新的作用，并为其他SCR样胞浆激活酶与跨膜蛋白的关联提供了一个模型。
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 scr-like cytoplasmic kinases with transmembrane proteins.