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CD2和CD4 T细胞表面抗原胞质结构域的自主作用。

Autonomous roles for the cytoplasmic domains of the CD2 and CD4 T cell surface antigens.

作者信息

Beyers A D, Davis S J, Cantrell D A, Izquierdo M, Williams A F

机构信息

MRC Cellular Immunology Unit, Sir William Dunn School of Pathology, University of Oxford, UK.

出版信息

EMBO J. 1991 Feb;10(2):377-85. doi: 10.1002/j.1460-2075.1991.tb07959.x.

Abstract

CD2 and CD4 are single chain transmembrane T cell surface molecules that are involved in signal transduction. Chimaeric constructs from rat CD2 and CD4 antigens were expressed in the Jurkat human T cell line to examine the role of extracellular, transmembrane and cytoplasmic domains in mediating functions controlled by CD2 and CD4. The results show that the large rise in concentration of cytoplasmic free Ca2+ mediated via CD2 crosslinking is controlled by the cytoplasmic domain and does not require the CD2 transmembrane and extracellular domains. Similarly the CD4 cytoplasmic domain alone was shown to encode the specificity for binding to the p56lck tyrosine kinase and to control down-modulation of CD4 after treatment with phorbol ester. Evidence was obtained that down-modulation of CD4 occurs when p56lck dissociates from the cytoplasmic domain due to phosphorylation of Ser 405.

摘要

CD2和CD4是参与信号转导的单链跨膜T细胞表面分子。将大鼠CD2和CD4抗原的嵌合构建体在Jurkat人T细胞系中表达,以研究细胞外、跨膜和细胞质结构域在介导由CD2和CD4控制的功能中的作用。结果表明,通过CD2交联介导的细胞质游离Ca2+浓度的大幅升高由细胞质结构域控制,不需要CD2跨膜和细胞外结构域。同样,单独的CD4细胞质结构域被证明编码与p56lck酪氨酸激酶结合的特异性,并在佛波酯处理后控制CD4的下调。有证据表明,当p56lck由于Ser 405的磷酸化而从细胞质结构域解离时,CD4会发生下调。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a0df/452657/3873fdab0e09/emboj00100-0138-a.jpg

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