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双蛋白赖氨酸和蛋白N端甲基转移酶METTL13的结构、活性与功能

Structure, Activity and Function of the Dual Protein Lysine and Protein N-Terminal Methyltransferase METTL13.

作者信息

Jakobsson Magnus E

机构信息

Department of Immunotechnology, Lund University, Medicon Village, 22100 Lund, Sweden.

出版信息

Life (Basel). 2021 Oct 21;11(11):1121. doi: 10.3390/life11111121.

Abstract

METTL13 (also known as eEF1A-KNMT and FEAT) is a dual methyltransferase reported to target the N-terminus and Lys55 in the eukaryotic translation elongation factor 1 alpha (eEF1A). METTL13-mediated methylation of eEF1A has functional consequences related to translation dynamics and include altered rate of global protein synthesis and translation of specific codons. Aberrant regulation of METTL13 has been linked to several types of cancer but the precise mechanisms are not yet fully understood. In this article, the current literature related to the structure, activity, and function of METTL13 is systematically reviewed and put into context. The links between METTL13 and diseases, mainly different types of cancer, are also summarized. Finally, key challenges and opportunities for METTL13 research are pinpointed in a prospective outlook.

摘要

METTL13(也称为eEF1A-KNMT和FEAT)是一种双甲基转移酶,据报道它作用于真核翻译延伸因子1α(eEF1A)的N端和赖氨酸55位点。METTL13介导的eEF1A甲基化具有与翻译动力学相关的功能后果,包括整体蛋白质合成速率的改变以及特定密码子的翻译。METTL13的异常调控与多种癌症相关,但具体机制尚未完全明确。在本文中,系统回顾了与METTL13的结构、活性和功能相关的现有文献,并进行了背景阐述。还总结了METTL13与疾病(主要是不同类型癌症)之间的联系。最后,在前瞻性展望中明确了METTL13研究的关键挑战和机遇。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3551/8624817/9df0b2ff85ce/life-11-01121-g002.jpg

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