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敲低热休克蛋白 27（HspB1）可诱导几种潜在的靶蛋白降解。

Knock down of heat shock protein 27 (HspB1) induces degradation of several putative client proteins.

机构信息

Centre de Génétique Moléculaire et Cellulaire, CNRS UMR5534, Université Lyon 1, Université de Lyon, Villeurbanne, France.

出版信息

PLoS One. 2012;7(1):e29719. doi: 10.1371/journal.pone.0029719. Epub 2012 Jan 4.

DOI:10.1371/journal.pone.0029719
PMID:22238643
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3251601/
Abstract

Hsp27 belongs to the heat shock protein family and displays chaperone properties in stress conditions by holding unfolded polypeptides, hence avoiding their inclination to aggregate. Hsp27 is often referenced as an anti-cancer therapeutic target, but apart from its well-described ability to interfere with different stresses and apoptotic processes, its role in non-stressed conditions is still not well defined. In the present study we report that three polypeptides (histone deacetylase HDAC6, transcription factor STAT2 and procaspase-3) were degraded in human cancerous cells displaying genetically decreased levels of Hsp27. In addition, these proteins interacted with Hsp27 complexes of different native size. Altogether, these findings suggest that HDAC6, STAT2 and procaspase-3 are client proteins of Hsp27. Hence, in non stressed cancerous cells, the structural organization of Hsp27 appears to be a key parameter in the regulation by this chaperone of the level of specific polypeptides through client-chaperone type of interactions.

摘要

热休克蛋白 27 属于热休克蛋白家族，在应激条件下具有伴侣蛋白特性，通过保持未折叠的多肽，从而避免它们倾向于聚集。热休克蛋白 27 通常被认为是一种抗癌治疗靶点，但除了其众所周知的能够干扰不同应激和细胞凋亡过程的能力外，其在非应激条件下的作用仍未得到很好的定义。在本研究中，我们报告说，三种多肽（组蛋白去乙酰化酶 HDAC6、转录因子 STAT2 和前胱冬酶-3）在显示遗传水平降低的热休克蛋白 27 的人类癌细胞中降解。此外，这些蛋白质与不同天然大小的 Hsp27 复合物相互作用。总之，这些发现表明 HDAC6、STAT2 和前胱冬酶-3 是 Hsp27 的客户蛋白。因此，在非应激的癌细胞中，Hsp27 的结构组织似乎是通过伴侣蛋白与客户蛋白相互作用来调节特定多肽水平的关键参数。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/190a/3251601/9327155a3a81/pone.0029719.g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/190a/3251601/31eb3a723e4f/pone.0029719.g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/190a/3251601/ea17606df6bc/pone.0029719.g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/190a/3251601/9dcb30d90606/pone.0029719.g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/190a/3251601/3c8bf0e01578/pone.0029719.g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/190a/3251601/11ab36eeeba4/pone.0029719.g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/190a/3251601/9327155a3a81/pone.0029719.g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/190a/3251601/31eb3a723e4f/pone.0029719.g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/190a/3251601/ea17606df6bc/pone.0029719.g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/190a/3251601/9dcb30d90606/pone.0029719.g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/190a/3251601/3c8bf0e01578/pone.0029719.g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/190a/3251601/11ab36eeeba4/pone.0029719.g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/190a/3251601/9327155a3a81/pone.0029719.g006.jpg

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