Nuclear and Cytoplasmic Glycosylation

作者: Doris M. Snow , Gerald W. Hart

DOI: 10.1016/S0074-7696(08)60416-7

关键词:

摘要: abstract O-GlcNAcylation is a form of cytoplasmic and nuclear glycosylation that found on many diverse proteins the cell including RNA polymerase II its associated transcription factors, cytoskeletal proteins, nucleoporins, viral heat shock tumor suppressors, oncogenes. It involves attachment single, unmodified N -acetylglucosaminyl residue O-glycosidically linked to hydroxyl groups serine threonine moieties proteins. highly abundant dynamic posttranslational modification appears modulate function in manner similar phosphorylation. All O -GlcNAc-containing are phosphoproteins involved formation multimeric complexes, suggesting -GlcNAc may play role mediating protein-protein interactions. sites resemble phosphorylation cases two modifications mutually exclusive; therefore, act as an antagonist help mediate essential functions cell.

参考文章(147)
Jay S. Skyler, Diabetic complications: The importance of glucose control Endocrinology and Metabolism Clinics of North America. ,vol. 25, pp. 243- 254 ,(1996) , 10.1016/S0889-8529(05)70323-6
Denise Auger, Pam Bounelis, Richard B. Marchase, Phosphoglucomutase is a Cytoplasmic Glycoprotein Implicated in the Regulated Secretory Pathway Springer, Berlin, Heidelberg. pp. 289- 292 ,(1993) , 10.1007/978-3-662-02928-2_52
B Gonzalez-Yanes, J.M. Cicero, R D Brown, C.M. West, Characterization of a cytosolic fucosylation pathway in Dictyostelium. Journal of Biological Chemistry. ,vol. 267, pp. 9595- 9605 ,(1992) , 10.1016/S0021-9258(19)50132-6
M Ishihara, N S Fedarko, H E Conrad, Transport of heparan sulfate into the nuclei of hepatocytes. Journal of Biological Chemistry. ,vol. 261, pp. 13575- 13580 ,(1986) , 10.1016/S0021-9258(18)67058-9
Robert Barker, Kenneth W. Olsen, Joel H. Shaper, Robert L. Hill, Agarose Derivatives of Uridine Diphosphate and N-Acetylglucosamine for the Purification of a Galactosyltransferase Journal of Biological Chemistry. ,vol. 247, pp. 7135- 7147 ,(1972) , 10.1016/S0021-9258(19)44605-X