Reitz F B, Pagliaro L
Center for Bioengineering, University of Washington, Seattle 98195-7962, U.S.A.
Horm Metab Res. 1997 Jun;29(6):317-21. doi: 10.1055/s-2007-979043.
The enzyme glucokinase has recently been found to be largely responsible for glucose homeostatic responses of both the liver and pancreas. The mechanism(s) of these responses remains unknown but recent studies suggest that the intracellular localization of glucokinase, controlled by glucokinase regulatory protein, may be important. This protein is known to bind to and inhibit glucokinase in a phosphofructose-sensitive manner, and we present evidence for the interaction of these proteins with F-actin. Glucokinase regulatory protein gelled F-actin, and gelation was specifically inhibited by glucokinase and the regulatory protein effectors fructose-1-phosphate (F1P) and fructose-6-phosphate (F6P). These results suggest that glucokinase regulatory protein may play a role in metabolism-sensitive glucokinase localization in vivo.
最近发现，酶葡萄糖激酶在很大程度上负责肝脏和胰腺的葡萄糖稳态反应。这些反应的机制尚不清楚，但最近的研究表明，由葡萄糖激酶调节蛋白控制的葡萄糖激酶的细胞内定位可能很重要。已知该蛋白以对磷酸果糖敏感的方式结合并抑制葡萄糖激酶，并且我们提供了这些蛋白与F-肌动蛋白相互作用的证据。葡萄糖激酶调节蛋白使F-肌动蛋白凝胶化，并且凝胶化被葡萄糖激酶以及调节蛋白效应物果糖-1-磷酸（F1P）和果糖-6-磷酸（F6P）特异性抑制。这些结果表明，葡萄糖激酶调节蛋白可能在体内对代谢敏感的葡萄糖激酶定位中起作用。
