CK2-mediated phosphorylation of SUZ12 promotes PRC2 function by stabilizing enzyme active site

Lihu Gong; Xiuli Liu; Lianying Jiao; Xin Yang; Andrew Lemoff; Xin Liu

doi:10.1038/s41467-022-34431-1

Nature Communications (Nov 2022)

CK2-mediated phosphorylation of SUZ12 promotes PRC2 function by stabilizing enzyme active site

Lihu Gong,
Xiuli Liu,
Lianying Jiao,
Xin Yang,
Andrew Lemoff,
Xin Liu

Affiliations

Lihu Gong: Cecil H. and Ida Green Center for Reproductive Biology Sciences, University of Texas Southwestern Medical Center
Xiuli Liu: Cecil H. and Ida Green Center for Reproductive Biology Sciences, University of Texas Southwestern Medical Center
Lianying Jiao: Cecil H. and Ida Green Center for Reproductive Biology Sciences, University of Texas Southwestern Medical Center
Xin Yang: Cecil H. and Ida Green Center for Reproductive Biology Sciences, University of Texas Southwestern Medical Center
Andrew Lemoff: Department of Biochemistry, University of Texas Southwestern Medical Center
Xin Liu: Cecil H. and Ida Green Center for Reproductive Biology Sciences, University of Texas Southwestern Medical Center

DOI: https://doi.org/10.1038/s41467-022-34431-1
Journal volume & issue: Vol. 13, no. 1
pp. 1 – 15

Abstract

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Here the authors identify SUZ12 as a cellular substate of casein kinase 2 (CK2), and show this phosphorylation changes the active site structure of Polycomb repressive complex 2 (PRC2) and promotes PRC2 function in cell identity maintenance during stem cell differentiation.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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