Phosphorylation of G-protein alpha-subunits in intact adipose cells: evidence against a mediating role in insulin-dependent metabolic effects.
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Summary
Data argue against a mediating role of phosphorylated G-protein alpha-subunits in the action of insulin.
- Type
- article
- Published
- 1989-12-05
- Cited by
- 2
- References
- 34
- OpenAlex
- https://openalex.org/W2009751001
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:32213990
Keywords
Phosphoprotein, Immunoprecipitation, Antiserum, Phosphorylation, Protein subunit
References
- Kinetic parameters of transport of 3-O-methylglucose and glucose in adipocytes.
- Insulin exerts actions through a distinct species of guanine nucleotide regulatory protein: inhibition of adenylate cyclase.
- Identification of a cellular 110 000-Da protein substrate for the insulin-receptor kinase.
- Evidence that insulin activates fat-cell acetyl-CoA carboxylase by increased phosphorylation at a specific site.
- The glucose transporter in 3T3-L1 adipocytes is phosphorylated in response to phorbol ester but not in response to insulin.
- cAMP-dependent protein kinase and lipolysis in rat adipocytes. I. Cell preparation, manipulation, and predictability in behavior.
- Insulin-dependent phosphorylation of GTP-binding proteins in phospholipid vesicles.
- Regulation of insulin-stimulated glucose transport in the isolated rat adipocyte. cAMP-independent effects of lipolytic and antilipolytic agents.
- Activity and phosphorylation state of glucose transporters in plasma membranes from insulin-, isoproterenol-, and phorbol ester-treated rat adipose cells.
- An endogenous substrate for the insulin receptor-associated tyrosine kinase.
- Phosphorylation of hormone-sensitive lipase by cyclic AMP-dependent protein kinase.
- Insulin inhibits pertussis toxin-catalyzed ADP-ribosylation of G-proteins. Evidence for a novel interaction between insulin receptors and G-proteins.
- Insulin-stimulated glucose transport in rat adipose cells. Modulation of transporter intrinsic activity by isoproterenol and adenosine.
- The Metabolism of Isolated Fat Cells: I. Effects of Hormones on Glucose Metabolism and Lipolysis
- Insulin stimulates the phosphorylation of the 95,000-dalton subunit of its own receptor.
- Immunochemical detection of the alpha-subunit of the G-protein, GZ, in membranes and cytosols of mammalian cells.
- Adipocyte plasma membranes contain two Gi subtypes but are devoid of Go
- Insulin rapidly stimulates tyrosine phosphorylation of a Mr-185,000 protein in intact cells
- The insulin receptor tyrosyl kinase phosphorylates holomeric forms of the guanine nucleotide regulatory proteins Gi and Go
- Insulin-activated tyrosine phosphorylation of a 15-kilodalton protein in intact 3T3-L1 adipocytes.
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