Heat shock protein 27 phosphorylation state is associated with cancer progression.
Heat shock protein 27 phosphorylation state is associated with cancer progression.
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DOI：
10.3389/fgene.2014.00346
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发表时间：
2014
影响因子：
3.7
通讯作者：
Rocchi P
中科院分区：
文献类型：
--
作者：
Katsogiannou M;Andrieu C;Rocchi P
了解控制应激诱导的存活的机制对于解释肿瘤如何经常抵抗治疗和改善当前的抗癌疗法至关重要。癌细胞能够通过调节热休克蛋白（Hsps）的表达和功能来科普应激和逃避药物毒性。Hsp27（HSPB1）是Hsp小家族成员之一，在肿瘤发生、治疗抵抗和细胞凋亡抑制等诸多信号通路中起着重要作用。Hsp27在许多类型的癌症中过表达，其功能受翻译后修饰如磷酸化调节。蛋白质磷酸化是真核细胞中最普遍的信号传导机制，它参与了所有基本的细胞过程。Hsp27的异常磷酸化与癌症有关，但其参与癌症发展和进展的分子机制仍不明确。本文综述了磷酸化对Hsp27在肿瘤细胞中的作用及其作为肿瘤治疗靶点的潜在价值。
Understanding the mechanisms that control stress-induced survival is critical to explain how tumors frequently resist to treatment and to improve current anti-cancer therapies. Cancer cells are able to cope with stress and escape drug toxicity by regulating heat shock proteins (Hsps) expression and function. Hsp27 (HSPB1), a member of the small Hsp family, represents one of the key players of many signaling pathways contributing to tumorigenicity, treatment resistance, and apoptosis inhibition. Hsp27 is overexpressed in many types of cancer and its functions are regulated by post-translational modifications, such as phosphorylation. Protein phosphorylation is the most widespread signaling mechanism in eukaryotic cells, and it is involved in all fundamental cellular processes. Aberrant phosphorylation of Hsp27 has been associated with cancer but the molecular mechanisms by which it is implicated in cancer development and progression remain undefined. This mini-review focuses on the role of phosphorylation in Hsp27 functions in cancer cells and its potential usefulness as therapeutic target in cancer.