Multisite phosphorylation of the α subunit of transducin by the insulin receptor kinase and protein kinase C

Y. Zick, R. Sagi-Eisenberg, M. Pines, P. Gierschik, Allen M. Spiegel

Research output: Contribution to journalArticle

99 Citations (Scopus)

Abstract

The GDP-bound α subunit of transducin, but not the guanosine 5'-[γ-thio]triphosphate-bound one, undergoes phosphorylation on tyrosine residues by the insulin receptor kinase and on serine residues by protein kinase C. Holotransducin is poorly phosphorylated by the insulin receptor kinase and is not phosphorylated by protein kinase C. Neither holotransducin nor any of its subunits were phosphorylated by the cAMP-dependent protein kinase. That a given subunit of transducin undergoes multisite phosphorylation depending on the type of nucleotide bound to it or the nature of the kinase suggests that hormone-dependent phosphorylation could provide a versatile mode for regulation of guanine nucleotide-binding protein (G protein) function. In particular, the findings that certain G proteins serve as substrates for both the insulin receptor kinase and protein kinase C implicate G proteins in playing a key role in mediating the action of insulin and ligands that act to activate protein kinase C.

Original languageEnglish (US)
Pages (from-to)9294-9297
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Volume83
Issue number24
StatePublished - 1986
Externally publishedYes

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Transducin
Insulin Receptor
GTP-Binding Proteins
Protein Kinase C
Phosphorylation
Phosphotransferases
Guanine Nucleotides
Guanosine
Cyclic AMP-Dependent Protein Kinases
Tyrosine
Carrier Proteins
Nucleotides
Hormones
Insulin
Ligands
protein kinase C kinase

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

Multisite phosphorylation of the α subunit of transducin by the insulin receptor kinase and protein kinase C. / Zick, Y.; Sagi-Eisenberg, R.; Pines, M.; Gierschik, P.; Spiegel, Allen M.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 83, No. 24, 1986, p. 9294-9297.

Research output: Contribution to journalArticle

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