After insulin binds Journal Article


Author: Rosen, O. M.
Article Title: After insulin binds
Abstract: Three recent advances pertinent to the mechanism of insulin action include (i) the discovery that the insulin receptor is an insulin-dependent protein tyrosine kinase, functionally related to certain growth actor receptors and oncogene-encoded proteins, (ii) the molecular cloning of the insulin proreceptor complementary DNA, and (iii) evidence that the protein tyrosine kinase activity of the receptor is essential for insulin action. Efforts are now focusing on the physiological substrates for the receptor kinase. Experience to date suggests that they will be rare proteins whose phosphorylation in intact cells may be transient. The advantages of attempting to dissect the initial biochemical pathway of insulin action include the wealth of information about the metabolic consequences of insulin action and the potential for genetic analysis in Drosophila and in man.
Keywords: review; drosophila; receptor, epidermal growth factor; tyrosine; phosphorylation; oncogenes; dna; substrate specificity; insulin; molecular weight; phosphothreonine; phosphoserine; receptors, cell surface; phosphotyrosine; insulin receptor; protein-tyrosine kinase; human; priority journal; support, non-u.s. gov't; support, u.s. gov't, p.h.s.; receptor, insulin
Journal Title: Science
Volume: 237
Issue: 4821
ISSN: 0036-8075
Publisher: American Association for the Advancement of Science  
Date Published: 1987-09-18
Start Page: 1452
End Page: 1458
Language: English
DOI: 10.1126/science.2442814
PUBMED: 2442814
PROVIDER: scopus
DOI/URL:
Notes: Article -- Export Date: 5 February 2021 -- Source: Scopus
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  1. Ora Mendelsohn Rosen
    58 Rosen