CD8α链的胞质结构域是其与p56lck相互作用所必需的。

The cytoplasmic domain of the CD8 alpha-chain is required for its interaction with p56lck.

作者信息

Yao L, Nakauchi H, Honjo T, Kawakami T

机构信息

Department of medical Chemistry, Kyoto University School of Medicine, Japan.

出版信息

Immunol Lett. 1990 Jul;24(4):267-71. doi: 10.1016/0165-2478(90)90011-e.

DOI:10.1016/0165-2478(90)90011-e

PMID:2118122

Abstract

The CD8 glycoprotein expressed on the surface of CTLs is a heterodimer composed of alpha (Lyt-2) and beta (Lyt-3) chains. Recent studies have shown that CD4 and CD8 are physically associated with a T cell-specific protein-tyrosine kinase p56lck. Our previous experiments have suggested strongly that p56lck interacts directly with CD4 and CD8 molecules. The present report using cytoplasmic deletion mutants of the CD8 alpha-chain gene has extended our observations to demonstrate unequivocally that the cytoplasmic domain of the CD8 alpha chain is responsible for interaction with p56lck. The data has also confirmed the importance of the conserved twelve amino acid sequence motif of the CD8 alpha cytoplasmic domain in complex formation with p56lck.

摘要

细胞毒性T淋巴细胞（CTL）表面表达的CD8糖蛋白是一种由α链（Lyt-2）和β链（Lyt-3）组成的异二聚体。最近的研究表明，CD4和CD8与一种T细胞特异性蛋白酪氨酸激酶p56lck在物理上相关联。我们之前的实验有力地表明，p56lck直接与CD4和CD8分子相互作用。本报告利用CD8α链基因的胞质缺失突变体扩展了我们的观察结果，明确证明CD8α链的胞质结构域负责与p56lck相互作用。数据还证实了CD8α胞质结构域中保守的12个氨基酸序列基序在与p56lck形成复合物中的重要性。