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丙酮酸激酶 M2 在癌症中的调控和功能。

Regulation and function of pyruvate kinase M2 in cancer.

机构信息

Brain Tumor Center and Department of Neuro-Oncology, The University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA.

出版信息

Cancer Lett. 2013 Oct 10;339(2):153-8. doi: 10.1016/j.canlet.2013.06.008. Epub 2013 Jun 18.

DOI:10.1016/j.canlet.2013.06.008
PMID:23791887
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3950276/
Abstract

Altered metabolism is fundamental to the growth and survival of cancer cells. Pyruvate kinase M2 (PKM2), a key enzyme in cancer metabolism, has been demonstrated to play a central role not only in metabolic reprogramming but also in direct regulation of gene expression and subsequent cell cycle progression. This review outlines the current understanding of PKM2 protein kinase activity and regulatory mechanisms underlying PKM2 expression, enzymatic activity, and nuclear localization, thus highlighting PKM2 as a potential therapeutic target.

摘要

代谢改变是癌细胞生长和存活的基础。丙酮酸激酶 M2(PKM2)是癌症代谢中的关键酶,已被证明不仅在代谢重编程中发挥核心作用,而且在直接调节基因表达和随后的细胞周期进程中也发挥核心作用。本文概述了目前对 PKM2 蛋白激酶活性和调节机制的理解,包括 PKM2 表达、酶活性和核定位的调节机制,从而突出了 PKM2 作为潜在治疗靶点的潜力。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f95c/3950276/5a3978325d10/nihms505854f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f95c/3950276/72ab780e88c4/nihms505854f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f95c/3950276/05cbcae14ad7/nihms505854f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f95c/3950276/5a3978325d10/nihms505854f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f95c/3950276/72ab780e88c4/nihms505854f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f95c/3950276/05cbcae14ad7/nihms505854f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f95c/3950276/5a3978325d10/nihms505854f3.jpg

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ERK1/2-dependent phosphorylation and nuclear translocation of PKM2 promotes the Warburg effect.ERK1/2 依赖性磷酸化和 PKM2 的核转位促进了瓦博格效应。
Nat Cell Biol. 2012 Dec;14(12):1295-304. doi: 10.1038/ncb2629. Epub 2012 Nov 25.
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EGFR-induced and PKCε monoubiquitylation-dependent NF-κB activation upregulates PKM2 expression and promotes tumorigenesis.
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Front Oncol. 2024 Apr 12;14:1392085. doi: 10.3389/fonc.2024.1392085. eCollection 2024.
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ULK1-dependent phosphorylation of PKM2 antagonizes O-GlcNAcylation and regulates the Warburg effect in breast cancer.ULK1 依赖性磷酸化 PKM2 拮抗 O-GlcNAc 化并调节乳腺癌中的瓦博格效应。
Oncogene. 2024 Jun;43(23):1769-1778. doi: 10.1038/s41388-024-03035-y. Epub 2024 Apr 17.
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