GLUCAGON AND P21 RAS ENHANCE THE PHOSPHORYLATION OF THE SAME 38-KILODALTON MEMBRANE-PROTEIN FROM RAT-LIVER CELLS

被引：15

作者：

HEGDE, AN ^{[1
]}

DAS, MR ^{[1
]}

机构：

[1] CTR CELLULAR & MOLEC BIOL,UPPAL RD,HYDERABAD 500007,INDIA

来源：

MOLECULAR AND CELLULAR BIOLOGY | 1990年 / 10卷 / 06期

关键词：

D O I：

10.1128/MCB.10.6.2468

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：

We had reported earlier the enhanced phosphorylation of a 38-kilodalton protein (p38) in rat liver plasma membrane by ras proteins. Now we show that glucagon increased the phosphorylation of the same protein. The nature and site(s) of phosphorylation were the same as those for the ras proteins. Both ATP and GTP could donate phosphate for the phosphorylation of p38. The stimulation of p38 phosphorylation by glucagon was guanine nucleotide dependent. This observation, together with our data on the stimulation of p38 phosphorylaton by AIF4-, suggest the involvement of G proteins in the reaction. We also showed that glucagon stimulates the phosphorylation of p38 in vivo.

引用

页码：2468 / 2474

页数：7

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