Insulin receptor autophosphorylation. I. Autophosphorylation kinetics of the native receptor and its cytoplasmic kinase domain.
Insulin receptor autophosphorylation. I. Autophosphorylation kinetics of the native receptor and its cytoplasmic kinase domain.
复制标题
胰岛素受体自身磷酸化。
DOI：
10.1021/bi00073a007
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发表时间：
1993
期刊：
影响因子：
2.9
通讯作者：
Kohanski,RA
中科院分区：
文献类型：
--
作者：
Kohanski,RA
Revised Manuscript Received March 12, 1993 abstract: Kinetic analysis of autophosphorylation was done using a non-Michaelis-Menten kinetic model. This model describes autophosphorylation in terms of a fast reaction phase, a slow reaction phase, and a partition function for the two phases. Kinetic parameters determined by this new approach show that insulin stimulates autophosphorylation by promoting (1) a 10-fold increase in the rate constant for the fast phase of the reaction and (2) a 2-fold increase in the partition function favoring the fast phase. Insulin did not significantly affect the binding constant for ATP in this fast phase. Kinetic parameters obtained for the cytoplasmic kinase domain were similar to those obtained for the native insulin receptor in the absence of insulin. The insulin receptor has three subdomains encompassing its seven autophosphorylation sites. The juxtamembrane sites react primarily in the slow kinetic phase, favored by the absence of stimulation and low ATP concentrations. The carboxy-terminal and central autophosphorylation subdomains react primarily in the fast kinetic phase, favored by raising the ATP concentration and/or the presence of insulin. These observations demonstrate that (1) both ATP and insulin regulate reaction in each autophosphorylation subdomain,(2) insulinstimulation occurs predominantly in the central and carboxy-terminal regions, and (3) autophosphorylation observed with the cytoplasmic kinase domain was similar to native insulin receptor in the absence of insulin. These findings are consistent with conclusions based on the kinetic analysis of autophosphorylation.The native insulin receptor/protein (tyrosine) kinase contains two insulin binding-subunits and two/3-subunits that cross the plasma membrane and bear the protein kinase domain. Insulin stimulates autophosphorylation of the receptor within this intracellular domain, and this leads to activation of substrate phosphorylation [cf. reviews by Ellis et al.(1991) and Olefsky,(1990)]. There are three subdomains that
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位点特异性 β 亚基酪氨酸自磷酸化与胰岛素受体（酪氨酸）蛋白激酶活性的胰岛素激活的关系。
DOI：
--
发表时间：
1988
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Tornqvist,HE;Avruch,J
通讯作者：
Avruch,J
一种快速简便的无盐[γ-32P]ATP制备方法
DOI：
--
发表时间：
1981
期刊：
影响因子：
--
作者：
J. Palmer;J. Palmer;J. Avruch;J. Avruch
通讯作者：
J. Avruch
由胰岛素受体酪氨酸激酶催化的底物磷酸化。
DOI：
--
发表时间：
1989
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Flores-Riveros,JR;Sibley,E;Kastelic,T;Lane,MD
通讯作者：
Lane,MD
人胰岛素受体激酶结构域的另一个版本：表达、纯化和表征。
DOI：
10.1073/pnas.86.20.7848
发表时间：
1989
影响因子：
11.1
作者：
Villalba,M;Wente,SR;Russell,DS;Ahn,JC;Reichelderfer,CF;Rosen,OM
通讯作者：
Rosen,OM
胰岛素与人胎盘溶解胰岛素受体的结合。
DOI：
--
发表时间：
1983
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Kohanski,RA;Lane,MD
通讯作者：
Lane,MD