Cell Reports : 余巍/刘辰莹合作组揭示衰老基因SIRT2 调控丝氨酸合成途径参与肿瘤形成的机制

2020-08-13 BioArt

代谢重编程为细胞的快速增殖与生长提供原料,肿瘤细胞的标志之一。与正常细胞的氧化磷酸化不同,肿瘤细胞即使在氧气充足的情况下,也会选择大量摄取葡萄糖通过有氧糖酵解生成乳酸与ATP,称为瓦伯格效应。

代谢重编程为细胞的快速增殖与生长提供原料,肿瘤细胞的标志之一。与正常细胞的氧化磷酸化不同,肿瘤细胞即使在氧气充足的情况下,也会选择大量摄取葡萄糖通过有氧糖酵解(aerobic glycolysis)生成乳酸与ATP,称为瓦伯格效应(Warburg effect)。这些代谢通路的转变,通常伴随着细胞的恶性转化,而背后的机制至今尚未完全阐明。复旦大学余巍课题组长期从事衰老相关基因SIRT家族调控肿瘤等衰老疾病的研究。此前,该课题组就揭示了SIRT1响应氧化应激调控酪氨酸tRNA合成酶的工作(PNAS 2017),线粒体中SIRT3调控一碳单位代谢酶参与结直肠肿瘤发生的分子机制(Nature Communications 2018;Cell Death & Disease 2020)。

2020年8月11日,复旦大学余巍课题组在Cell Reports在线发表文章Acetylation stabilizes Phosphoglycerate dehydrogenase by disrupting the interaction of E3 ligase RNF5 to promote breast tumorigenesis,发现SIRT2可以调控丝氨酸合成通路中的限速酶PHGDH阻止其E3泛素连接酶RNF5泛素化修饰并降解。

SIRT2和Tip60调节PHGDH的可逆乙酰化修饰对葡萄糖进行响应,PHGDH在K58的乙酰化破坏了泛素连接酶RNF5与PHGDH的结合从而阻止了PHGDH的降解PHGDH是丝氨酸合成途径中的限速酶,它的高表达与多种肿瘤有关。在约40%的黑色素瘤和6%的乳腺癌中存在PHGDH基因的拷贝数增加。然而,最近有研究表明,在没有拷贝数增加的情况下,PHGDH仍然高表达并促进了乳腺癌的发生。这表明在细胞中,除了基因拷贝数增加外,还存在某种机制,可以调节PHGDH的表达。余巍课题组研究发现,E3泛素连接酶RNF5可以通过泛素化促进PHGDH蛋白的降解,并降低细胞内的丝氨酸/甘氨酸水平。丝氨酸/甘氨酸的缺乏抑制了肿瘤细胞的抗氧化和增殖能力。SIRT2和Tip60调节PHGDH的可逆乙酰化修饰对葡萄糖进行响应,PHGDH的乙酰化修饰作为调节信号,抑制PHGDH-RNF5的相互作用,从而促进了肿瘤细胞中PHGDH蛋白的累积,为肿瘤细胞中PHGDH的高表达提供了新的解释。此研究揭示了SIRT2-PHGDH调控轴在肿瘤形成中的作用,为开发靶向SIRT2-PHGDH调控轴治疗肿瘤的小分子药物提供理论基础。

复旦大学博士生王超为本文第一作者,复旦大学余巍研究员和上海交通大学医学院附属新华医院刘辰莹副研究员为共同通讯作者,浙江省肿瘤医院凌志强教授对本研究提供大量帮助。

复旦大学余巍团队长期致力于去乙酰化酶HDAC家族调控衰老疾病的机制研究。

原始出处:

Chao Wang, Xingyou Wan, Tong Yu, et al.Acetylation Stabilizes Phosphoglycerate Dehydrogenase by Disrupting the Interaction of E3 Ligase RNF5 to Promote Breast Tumorigenesis.Cell Rep. 2020 Aug 11;32(6):108021. doi: 10.1016/j.celrep.2020.108021.

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    2021-02-21 爆笑小医
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    2020-08-13 肿肿

    机制研究离临床仍然有距离,不过与临床结合思考,仍然有帮助的,不能仅仅是纯临床思维,转化思维同样重要

    0

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