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METTL3 acetylation sites recognition

ABSTRACT: We performed stable isotope labeling of amino acids in cell culture (SILAC) and mass spectrometry (MS) analysis to identify potential acetylation sites on METTL3 in response to ectopic p300 expression.

ORGANISM(S): Homo Sapiens

SUBMITTER: Han You

PROVIDER: PXD028177 | iProX | Sat Aug 28 00:00:00 BST 2021

REPOSITORIES: iProX

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METTL3 acetylation impedes cancer metastasis via fine-tuning its nuclear and cytosolic functions.

Li Yuanpei Y He Xiaoniu X Lu Xiao X Gong Zhicheng Z Li Qing Q Zhang Lei L Yang Ronghui R Wu Chengyi C Huang Jialiang J Ding Jiancheng J He Yaohui Y Liu Wen W Chen Ceshi C Cao Bin B Zhou Dawang D Shi Yufeng Y Chen Juxiang J Wang Chuangui C Zhang Shengping S Zhang Jian J Ye Jing J You Han H

Nature communications 20221026 1

The methyltransferase like 3 (METTL3) has been generally recognized as a nuclear protein bearing oncogenic properties. We find predominantly cytoplasmic METTL3 expression inversely correlates with node metastasis in human cancers. It remains unclear if nuclear METTL3 is functionally distinct from cytosolic METTL3 in driving tumorigenesis and, if any, how tumor cells sense oncogenic insults to coordinate METTL3 functions within these intracellular compartments. Here, we report an acetylation-depe ...[more]

PMID: 36289222

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