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首页> 外文期刊>Oncogene >Monomeric but not trimeric clathrin heavy chain regulates p53-mediated transcription
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Monomeric but not trimeric clathrin heavy chain regulates p53-mediated transcription

机译：单体而不是三聚体网格蛋白重链调节p53介导的转录

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摘要

Tumor suppressor p53 protein is the transcription factor responsible for various genes including DNA repair, growth arrest, apoptosis and antiangiogenesis. Recently, we showed that clathrin heavy chain (CHC), which was originally identified as a cytosolic protein regulating endocytosis, is present in nuclei and functions as a coactivator for p53. Here, we determined the detailed p53-binding site of CHC and a CHC deletion mutant containing this region (CHC833-1406) behaved as a monomer in cells. Monomeric CHC833-1406 still had a higher ability to transactivate p53 than wild-type CHC although this CHC mutant no longer had endocytic function. Moreover, similar to wild-type CHC, monomeric CHC enhances p53-mediated transcription through the recruitment of histone acetyltransferase p300. Immunofluorescent microscopic analysis exhibited that CHC833-1406 is predominantly localized in nuclei, suggesting that there may be a certain regulatory domain for nuclear export in the C-terminus of CHC. Thus, the trimerization domain of CHC is not necessary for the transactivation of p53 target genes and these data provide further evidence that nuclear CHC plays a role distinct from clathrin-mediated endocytosis.
机译：肿瘤抑制因子p53蛋白是负责各种基因的转录因子，包括DNA修复，生长停滞，凋亡和抗血管生成。最近，我们显示网格蛋白重链（CHC），最初被确定为调节胞吞作用的胞质蛋白，存在于细胞核中，并起p53的共激活子的作用。在这里，我们确定了CHC的详细p53结合位点和包含该区域的CHC缺失突变体（CHC833-1406）在细胞中起着单体的作用。尽管该CHC突变体不再具有内吞功能，但单体CHC833-1406仍具有比野生型CHC高的p53激活能力。此外，类似于野生型CHC，单体CHC通过募集组蛋白乙酰转移酶p300增强p53介导的转录。免疫荧光显微镜分析显示，CHC833-1406主要位于细胞核中，表明在CHC的C端可能存在一定的核出口调控域。因此，CHC的三聚化结构域对于p53靶基因的反式激活不是必需的，这些数据进一步证明了核CHC的作用不同于网格蛋白介导的内吞作用。

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