The mechanism underlying redundant functions of the YTHDF proteins

Genome Biology

Short Report

Xiaoming Zhou¹  Jiangbo Wei²  Zhongyu Zou²  Chuan He³  Caraline Sepich-Poore⁴ 

[1] Department of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, 75390, Dallas, TX, USA;Department of Chemistry, The University of Chicago, 60637, Chicago, IL, USA;Howard Hughes Medical Institute, The University of Chicago, 60637, Chicago, IL, USA;Department of Chemistry, The University of Chicago, 60637, Chicago, IL, USA;Howard Hughes Medical Institute, The University of Chicago, 60637, Chicago, IL, USA;Department of Biochemistry and Molecular Biology and Institute for Biophysical Dynamics, The University of Chicago, 60637, Chicago, IL, USA;Department of Chemistry, The University of Chicago, 60637, Chicago, IL, USA;Howard Hughes Medical Institute, The University of Chicago, 60637, Chicago, IL, USA;Department of Biochemistry and Molecular Biology and Institute for Biophysical Dynamics, The University of Chicago, 60637, Chicago, IL, USA;University of Chicago Medical Scientist Training Program, 60637, Chicago, IL, USA;

关键词: YTHDF1;    YTHDF2;    YTHDF3;    mA;    Translation control;    P-body;   

DOI  :  10.1186/s13059-023-02862-8

 received in 2022-04-28, accepted in 2023-01-19,  发布年份 2023

来源: Springer

【 摘 要 】

The YTH N6-methyladenosine RNA binding proteins (YTHDFs) mediate the functional effects of N6-methyladenosine (m6A) on RNA. Recently, a report proposed that all YTHDFs work redundantly to facilitate RNA decay, raising questions about the exact functions of individual YTHDFs, especially YTHDF1 and YTHDF2. We show that YTHDF1 and YTHDF2 differ in their low-complexity domains (LCDs) and exhibit different behaviors in condensate formation and subsequent physiological functions. Biologically, we also find that the global stabilization of RNA after depletion of all YTHDFs is driven by increased P-body formation and is not strictly m6A dependent.

【 授权许可】

CC BY   
© The Author(s) 2023

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