A Single Substitution of the Insulin Receptor Kinase Inhibits Serine Autophosphorylation in Vitro:  Evidence for an Interaction between the C-Terminus and the Activation Loop†

Biochemistry ◽  
2000 ◽  
Vol 39 (24) ◽  
pp. 7170-7177 ◽  
Author(s):  
Volker Noelle ◽  
Norbert Tennagels ◽  
Helmut W. Klein
Keyword(s):  
Insulin Receptor ◽  
Activation Loop ◽  
Receptor Kinase ◽  
C Terminus ◽  
Insulin Receptor Kinase ◽  
Single Substitution

Interaction of the insulin receptor kinase with serine/threonine kinases in vitro

1985 ◽  
Vol 28 (2) ◽  
pp. 171-182 ◽  
Author(s):  
Hans U. Haring ◽  
Morris F. White ◽  
C. Ronald Kahn ◽  
Zafeer Ahmad ◽  
Anna A. DePaoli-Roach ◽  
...  
Keyword(s):  
Insulin Receptor ◽  
Receptor Kinase ◽  
Threonine Kinases ◽  
Insulin Receptor Kinase

scholarly journals Tyrosine phosphorylation of two cytosolic proteins of 50 kDa and 35 kDa in rat liver by insulin-receptor kinase in vitro

1987 ◽  
Vol 248 (1) ◽  
pp. 27-33 ◽  
Author(s):  
Y C Kwok ◽  
C C Yip
Keyword(s):  
Insulin Receptor ◽  
Rat Liver ◽  
Growth Factor Receptor ◽  
Insulin Receptors ◽  
Artificial Substrates ◽  
Receptor Kinase ◽  
Insulin Receptor Tyrosine Kinase ◽  
Cytosolic Proteins ◽  
Insulin Receptor Kinase

Insulin-receptor tyrosine kinase can phosphorylate a variety of artificial substrates in vitro. Its physiological substrate(s), however, remains unknown. In the present study, we show that immobilized insulin receptors phosphorylate tyrosine residues of two cytosolic proteins of 50 kDa and 35 kDa in rat liver. Phosphorylation of these two proteins required Mn2+- or Mg2+-ATP as the phosphate donor. Phosphorylation was time- and temperature-dependent. Furthermore, the rate of phosphorylation of the two proteins was related to the autophosphorylated state of the insulin receptor. The pI of the phosphorylated 50 kDa and 35 kDa proteins was 5.4 and 5.6 respectively. These proteins were present in low abundance. They were not related to each other, nor to the insulin receptor, as demonstrated by in-gel proteolytic digestion and by immunoprecipitation using antibodies produced against them. They were specific substrates for the insulin receptor kinase, since they were not phosphorylated by epidermal-growth-factor-receptor kinase. These observations suggest that the 50 kDa and 35 kDa cytosolic proteins may be endogenous substrates for the insulin-receptor kinase.

scholarly journals APS, an adapter protein with a PH and SH2 domain, is a substrate for the insulin receptor kinase

1999 ◽  
Vol 341 (3) ◽  
pp. 665-668 ◽  
Author(s):  
Zamal AHMED ◽  
Beverley J. SMITH ◽  
Kei KOTANI ◽  
Peter WILDEN ◽  
Tahir S. PILLAY
Keyword(s):  
Insulin Receptor ◽  
Sh2 Domain ◽  
Activation Loop ◽  
Adapter Proteins ◽  
Adapter Protein ◽  
Receptor Kinase ◽  
Kinase Activation ◽  
Tyrosine Residues ◽  
Insulin Receptor Kinase ◽  
Receptor Binding Protein

APS (adapter protein with a PH and SH2 domain) is the newest member of a family of tyrosine kinase adapter proteins including SH2-B and Lnk. We previously identified SH2-B as an insulin-receptor-binding protein and substrate [Kotani, Wilden and Pillay (1998) Biochem J. 335, 103-109]. Here we show that APS interacts with the insulin receptor kinase activation loop through its SH2 domain and insulin stimulates the tyrosine-phosphorylation of APS. Furthermore, the phosphorylation of activation-loop tyrosine residues 1158 and 1162 are required for this interaction.

Tissue Specific Differences in the Insulin Receptor Kinase Activated in Vitro and in Vivo*

Endocrinology ◽  
1988 ◽  
Vol 122 (2) ◽  
pp. 427-437 ◽  
Author(s):  
CHARLES F. BURANT ◽  
MARY K. TREUTELAAR ◽  
MARIA G. BUSE
Keyword(s):  
Insulin Receptor ◽  
Receptor Kinase ◽  
Tissue Specific ◽  
Insulin Receptor Kinase
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