Abstract：
:The insulin receptor appears as a tetrameric glycoprotein consisting of two Mr 130,000 subunits (alpha), and two Mr 95,000 subunits (beta) in a disulfide-linked complex. Insulin bound to its specific cell surface receptors in its target cells leads to a complex array of molecular events resulting in insulin effects. It is now generally believed that protein phosphorylation-dephosphorylation reactions represent an important mechanism by which a variety of extracellular stimuli regulate cellular functions. Insulin mediates such reactions, but it is not known whether these are the biochemical link between the binding of insulin to its receptor and its final cellular effects. In search of initial post-binding events which might play a role in insulin action, we looked for phosphorylation of insulin receptors. We show that the insulin receptor displays two functional domains, an insulin binding alpha-subunit, and an insulin responsive protein kinase contained in the beta-subunit. We envisage the insulin receptor as an integrated system for transmembrane signal transmission in which hormone binding to the alpha-subunit leads to activation of the beta-subunit via conformational changes.
journal_name
Biochimiejournal_title
Biochimieauthors
Van Obberghen E,Ballotti R,Gazzano H,Fehlmann M,Rossi B,Gammeltoft S,Debant A,Le Marchand-Brustel Y,Kowalski Adoi
10.1016/s0300-9084(85)80109-7subject
Has Abstractpub_date
1985-10-01 00:00:00pages
1119-24issue
10-11eissn
0300-9084issn
1638-6183pii
S0300-9084(85)80109-7journal_volume
67pub_type
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