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磷酸化对人类免疫缺陷病毒Nef蛋白的调控

Regulation of human immunodeficiency virus Nef protein by phosphorylation.

作者信息

Bandres J C, Luria S, Ratner L

机构信息

Department of Medicine, Washington University School of Medicine, St. Louis, Missouri.

出版信息

Virology. 1994 May 15;201(1):157-61. doi: 10.1006/viro.1994.1278.

DOI:10.1006/viro.1994.1278
PMID:8178481
Abstract

Human immunodeficiency virus isolates express a Nef protein with either an alanine or a threonine at amino acid residue 15. The threonine residue is a site for phosphorylation by protein kinase C. Jurkat T cells constitutively expressing the alanine variant of Nef exhibit the ability to downregulate the induction of transcription factors NF-kB and AP-1. In contrast, Jurkat cells with the threonine variant of Nef are at least partially restored in their ability to recruit NF-kB and AP-1.

摘要

人类免疫缺陷病毒分离株表达的Nef蛋白在氨基酸残基15处为丙氨酸或苏氨酸。苏氨酸残基是蛋白激酶C磷酸化的位点。组成型表达Nef丙氨酸变体的Jurkat T细胞具有下调转录因子NF-κB和AP-1诱导的能力。相比之下,带有Nef苏氨酸变体的Jurkat细胞在募集NF-κB和AP-1的能力上至少部分得到恢复。

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