CIITA的磷酸化引导其寡聚化、积累并增强其在MHCII启动子上的活性。
Phosphorylation of CIITA directs its oligomerization, accumulation and increased activity on MHCII promoters.
作者信息
Tosi Giovanna, Jabrane-Ferrat Nabila, Peterlin B Matija
机构信息
Department of Medicine, Microbiology and Immunology, Rosalind Russell Medical Research Center, University of California, San Francisco, CA 94115-0703, USA.
出版信息
EMBO J. 2002 Oct 15;21(20):5467-76. doi: 10.1093/emboj/cdf557.
Abstract
The class II transactivator (CIITA) is the master regulator of major histocompatibility complex class II (MHCII) transcription. Its activity is regulated at the post-transcriptional level by phosphorylation and oligomerization. This aggregation mapped to and depended on the phosphorylation of residues between positions 253 and 321 in CIITA, which resulted in a dramatic accumulation of the protein and increased expression of MHCII genes in human promonocytic U937 cells, which represent immature antigen-presenting cells. Thus, the post-transcriptional modification of CIITA plays an important role in the immune response.
摘要
II类反式激活因子（CIITA）是主要组织相容性复合体II类（MHCII）转录的主要调节因子。其活性在转录后水平通过磷酸化和寡聚化进行调节。这种聚集定位于CIITA中253位至321位之间残基的磷酸化，并依赖于此，这导致该蛋白大量积累，并增加了人类原单核细胞U937细胞（代表未成熟抗原呈递细胞）中MHCII基因的表达。因此，CIITA的转录后修饰在免疫反应中起重要作用。
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