CONTROL OF GLYCOGEN-SYNTHASE BY HIERARCHICAL PROTEIN-PHOSPHORYLATION

被引:220
作者
ROACH, PJ
机构
[1] Dept of Biochem/Mol Biology, Indiana University, School of Medicine, Indianapolis
关键词
Glycogen metabolism; Isozyme; Mutagenesis; Phosphoprotein; Phosphorylation site; Protein kinase; Synthetic peptides;
D O I
10.1096/fasebj.4.12.2168324
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Protein phosphorylation is one of the most common mechanisms for controlling protein function. We now know that most phosphoproteins contain multiple phosphorylation sites and that these sites are often located in clusters. From the study of the enzyme glycogen synthase, one mechanism for the formation of phosphorylation clusters has been discovered that involves the concerted action of two or more protein kinases. One protein kinase, the primary kinase, introduces a phosphate group that is a requirement for the action of another, secondary, protein kinase. Thus the multiple phosphorylation occurs in a hierarchal fashion. This mechanism, which is critical for the phosphorylation of glycogen synthase, is likely to be a much more widespread phenomenon.
引用
收藏
页码:2961 / 2968
页数:8
相关论文
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