A New Highly Efficient Substrate-trapping Mutant of Protein Tyrosine Phosphatase 1B (PTP1B) Reveals Full Autoactivation of the Insulin Receptor Precursor-Reference-Cited by-同舟云学术

A New Highly Efficient Substrate-trapping Mutant of Protein Tyrosine Phosphatase 1B (PTP1B) Reveals Full Autoactivation of the Insulin Receptor Precursor

Published:2011-06 Issue:22 Volume:286 Page:19373-19380
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Boubekeur Samira,Boute Nicolas,Pagesy Patrick,Zilberfarb Vladimir,Christeff Névéna,Issad Tarik

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference53 articles.

1. Protein–protein interaction in insulin signaling and the molecular mechanisms of insulin resistance

2. Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose

3. A cascade of tyrosine autophosphorylation in the beta-subunit activates the phosphotransferase of the insulin receptor.

4. Isoproterenol Inhibits Insulin-Stimulated Tyrosine Phosphorylation of the Insulin Receptor Without Increasing its Serine/Threonine Phosphorylation

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