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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Human immunodeficiency virus type 1 Nef and p56lck protein-tyrosine kinase interact with a common element in CD4 cytoplasmic tail.
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Human immunodeficiency virus type 1 Nef and p56lck protein-tyrosine kinase interact with a common element in CD4 cytoplasmic tail.

机译：1型人类免疫缺陷病毒Nef和p56lck蛋白-酪氨酸激酶与CD4细胞质尾巴中的一个共同元件相互作用。

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摘要

The human immunodeficiency virus type 1 nef gene induces endocytosis of CD4 antigen and disrupts the association between CD4 and p56lck protein-tyrosine kinase (EC 2.7.1.112). We demonstrate that in T cells these effects of the viral protein require a cluster of hydrophobic amino acids in a membrane-proximal region of the CD4 cytoplasmic tail; other amino acids in the C-terminal segment of CD4 cytoplasmic tail also contribute to the interaction. Mutations in CD4 that prevent down-modulation by Nef also decrease CD4 association with p56lck and prevent Nef-induced disruption of CD4-p56lck complexes. Together, the overlap in CD4 sequences required for interaction with Nef and p56lck and the tight correlation between Nef-induced CD4 down-modulation and disruption of CD4-p56lck association suggest that Nef, or cellular factors recruited by Nef, interact with this segment of CD4 to displace p56lck from the complex and induce CD4 endocytosis.
机译：人类免疫缺陷病毒1型nef基因诱导CD4抗原的内吞作用，并破坏CD4和p56lck蛋白-酪氨酸激酶之间的关联（EC 2.7.1.112）。我们证明，在T细胞中，病毒蛋白的这些作用在CD4胞质尾部的膜近端区域需要疏水性氨基酸簇。 CD4胞质尾部C末端片段中的其他氨基酸也有助于相互作用。阻止Nef下调的CD4突变也降低了CD4与p56lck的缔合，并阻止了Nef诱导的CD4-p56lck复合物的破坏。总之，与Nef和p56lck相互作用所需的CD4序列重叠以及Nef诱导的CD4下调与CD4-p56lck关联破坏之间的紧密相关性表明，Nef或Nef募集的细胞因子与CD4的这一部分相互作用从复合物中置换p56lck并诱导CD4内吞。

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