期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 283, 期 49, 页码 33935-33941出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M806199200
关键词
-
资金
- National Institutes of Health [R01 HD13563, R01 CA42486]
- National Science Foundation
O-GlcNAc-transferase (OGT) substrate specificity is regulated by transiently interacting proteins. To further examine the regulation of OGT, we have identified 27 putative OGT-interacting proteins through a yeast two-hybrid screen. Two of these proteins, Trak1 (OIP106) and O-GlcNA case, have been shown previously to interact with and regulate OGT. We demonstrate here that MYPT1 and CARM1 also interact with and target OGT. MYPT1 and CARM1 are substrates of OGT in vitro and in vivo. MYPT1 and CARM1 also function to alter OGT substrate specificity in vitro. Furthermore depletion of MYPT1 in Neuro-2a neuroblastoma cells alters GlcNA cylation of several proteins under basal conditions, suggesting that MYPT1 regulates OGT substrate specificity in vivo.
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