O-Linked β-N-Acetylglucosaminyltransferase Substrate Specificity Is Regulated by Myosin Phosphatase Targeting and Other Interacting Proteins
O-Linked β-N-Acetylglucosaminyltransferase Substrate Specificity Is Regulated by Myosin Phosphatase Targeting and Other Interacting Proteins
复制标题
DOI：
10.1074/jbc.m806199200
复制
发表时间：
2008-12-05
影响因子：
4.8
通讯作者：
Hart, Gerald W.
中科院分区：
文献类型：
--
作者：
Cheung, Win D.;Sakabe, Kaoru;Hart, Gerald W.
o - glcnac转移酶（OGT）底物特异性受瞬时相互作用蛋白调控。为了进一步研究OGT的调控，我们通过酵母双杂交筛选鉴定了27个假定的OGT相互作用蛋白。其中两种蛋白Trak1 （OIP106）和O-GlcNA case先前已被证明与OGT相互作用并调节OGT。我们在这里证明了MYPT1和CARM1也与OGT相互作用并靶向OGT。在体内和体外，MYPT1和CARM1是OGT的底物。MYPT1和CARM1也能在体外改变OGT底物特异性。此外，在基础条件下，神经母细胞瘤细胞中MYPT1的缺失会改变几种蛋白的GlcNA循环，这表明MYPT1在体内调节OGT底物特异性。
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.