Protein kinase C alters the responsiveness of adenylyl cyclases to G protein α and βγ subunits

Gregor Zimmermann, Ronald Taussig

Research output: Contribution to journalArticle

114 Citations (Scopus)

Abstract

The ability of protein kinase C (PKC) to regulate the responsiveness of adenylyl cyclase to different activators was assessed. Membranes prepared from Sf9 cells infected with recombinant baculoviruses encoding either type II or IV adenylyl cyclase were incubated with recombinant PKCα (purified from Sf9 cells), and the effects on adenylyl cyclase activity were measured after reconstitution with G(sα), Gβγ, or forskolin. PKCα treatment of type II adenylyl cyclase leads to increases in basal, forskolin-stimulated, and βγ-stimulated activities and greater sensitivity to stimulation by G(sα). Paradoxically, most of the βγ potentiation of G(sα)-stimulated activity is eliminated by pretreatment with PKCα. By contrast, treatment of type IV adenylyl cyclase with PKCα has little effect on the basal, forskolin-stimulated, or βγ-stimulated activities but markedly reduces the G(sα)stimulated and βγ-potentiated activity of this isoform. These studies demonstrate that protein kinases can alter both the activity of adenylyl cyclase isoforms and their responsiveness to G protein regulation, thereby altering the ability of adenylyl cyclases to integrate signals derived from multiple hormonal inputs.

Original languageEnglish (US)
Pages (from-to)27161-27166
Number of pages6
JournalJournal of Biological Chemistry
Volume271
Issue number43
DOIs
StatePublished - 1996

Fingerprint

Protein Subunits
GTP-Binding Proteins
Adenylyl Cyclases
Protein Kinase C
Colforsin
Sf9 Cells
Protein Isoforms
Baculoviridae
Recombinant Proteins
Protein Kinases
Membranes
adenylyl cyclase 4

ASJC Scopus subject areas

  • Biochemistry

Cite this

Protein kinase C alters the responsiveness of adenylyl cyclases to G protein α and βγ subunits. / Zimmermann, Gregor; Taussig, Ronald.

In: Journal of Biological Chemistry, Vol. 271, No. 43, 1996, p. 27161-27166.

Research output: Contribution to journalArticle

@article{a6ce5de831fc4ef5a283393b27a7cb1a,
title = "Protein kinase C alters the responsiveness of adenylyl cyclases to G protein α and βγ subunits",
abstract = "The ability of protein kinase C (PKC) to regulate the responsiveness of adenylyl cyclase to different activators was assessed. Membranes prepared from Sf9 cells infected with recombinant baculoviruses encoding either type II or IV adenylyl cyclase were incubated with recombinant PKCα (purified from Sf9 cells), and the effects on adenylyl cyclase activity were measured after reconstitution with G(sα), Gβγ, or forskolin. PKCα treatment of type II adenylyl cyclase leads to increases in basal, forskolin-stimulated, and βγ-stimulated activities and greater sensitivity to stimulation by G(sα). Paradoxically, most of the βγ potentiation of G(sα)-stimulated activity is eliminated by pretreatment with PKCα. By contrast, treatment of type IV adenylyl cyclase with PKCα has little effect on the basal, forskolin-stimulated, or βγ-stimulated activities but markedly reduces the G(sα)stimulated and βγ-potentiated activity of this isoform. These studies demonstrate that protein kinases can alter both the activity of adenylyl cyclase isoforms and their responsiveness to G protein regulation, thereby altering the ability of adenylyl cyclases to integrate signals derived from multiple hormonal inputs.",
author = "Gregor Zimmermann and Ronald Taussig",
year = "1996",
doi = "10.1074/jbc.271.43.27161",
language = "English (US)",
volume = "271",
pages = "27161--27166",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "43",

}

TY - JOUR

T1 - Protein kinase C alters the responsiveness of adenylyl cyclases to G protein α and βγ subunits

AU - Zimmermann, Gregor

AU - Taussig, Ronald

PY - 1996

Y1 - 1996

N2 - The ability of protein kinase C (PKC) to regulate the responsiveness of adenylyl cyclase to different activators was assessed. Membranes prepared from Sf9 cells infected with recombinant baculoviruses encoding either type II or IV adenylyl cyclase were incubated with recombinant PKCα (purified from Sf9 cells), and the effects on adenylyl cyclase activity were measured after reconstitution with G(sα), Gβγ, or forskolin. PKCα treatment of type II adenylyl cyclase leads to increases in basal, forskolin-stimulated, and βγ-stimulated activities and greater sensitivity to stimulation by G(sα). Paradoxically, most of the βγ potentiation of G(sα)-stimulated activity is eliminated by pretreatment with PKCα. By contrast, treatment of type IV adenylyl cyclase with PKCα has little effect on the basal, forskolin-stimulated, or βγ-stimulated activities but markedly reduces the G(sα)stimulated and βγ-potentiated activity of this isoform. These studies demonstrate that protein kinases can alter both the activity of adenylyl cyclase isoforms and their responsiveness to G protein regulation, thereby altering the ability of adenylyl cyclases to integrate signals derived from multiple hormonal inputs.

AB - The ability of protein kinase C (PKC) to regulate the responsiveness of adenylyl cyclase to different activators was assessed. Membranes prepared from Sf9 cells infected with recombinant baculoviruses encoding either type II or IV adenylyl cyclase were incubated with recombinant PKCα (purified from Sf9 cells), and the effects on adenylyl cyclase activity were measured after reconstitution with G(sα), Gβγ, or forskolin. PKCα treatment of type II adenylyl cyclase leads to increases in basal, forskolin-stimulated, and βγ-stimulated activities and greater sensitivity to stimulation by G(sα). Paradoxically, most of the βγ potentiation of G(sα)-stimulated activity is eliminated by pretreatment with PKCα. By contrast, treatment of type IV adenylyl cyclase with PKCα has little effect on the basal, forskolin-stimulated, or βγ-stimulated activities but markedly reduces the G(sα)stimulated and βγ-potentiated activity of this isoform. These studies demonstrate that protein kinases can alter both the activity of adenylyl cyclase isoforms and their responsiveness to G protein regulation, thereby altering the ability of adenylyl cyclases to integrate signals derived from multiple hormonal inputs.

UR - http://www.scopus.com/inward/record.url?scp=0029998598&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0029998598&partnerID=8YFLogxK

U2 - 10.1074/jbc.271.43.27161

DO - 10.1074/jbc.271.43.27161

M3 - Article

C2 - 8900209

AN - SCOPUS:0029998598

VL - 271

SP - 27161

EP - 27166

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 43

ER -