O-GlcNAcylation of co-activator-associated arginine methyltransferase 1 regulates its protein substrate specificity

Author:

Charoensuksai Purin1,Kuhn Peter12,Wang Lu1,Sherer Nathan1,Xu Wei1

Affiliation:

1. McArdle Laboratory for Cancer Research, University of Wisconsin School of Medicine and Public Health, Madison, WI 53705, U.S.A.

2. Biological Sciences Department, Edgewood College, Madison, WI 53711, U.S.A.

Abstract

O-GlcNAcylation (O-linked-β-N-acetylglucosaminidation) sites of CARM1 (co-activator-associated arginine methyltransferase 1) have been mapped to four possible sites. O-GlcNAc (O-linked-β-N-acetylglucosamine)-depleted CARM1 generated by three different methods displays different substrate specificity from that of wild-type CARM1, suggesting that O-GlcNAcylation of CARM1 is an important determinant for CARM1 substrate specificity.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

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