Downregulation of protein kinase C-γ is independent of a functional kinase domain

Ina Freisewinkel, Dieter Riethmacher, Silvia Stabel

Research output: Contribution to journalArticle

26 Citations (Scopus)

Abstract

Prolonged activation of protein kinase C (PKC) types α and β by tumor-promoting phorbol esters leads to desensitization of the phorbol ester response, downregulation of protein kinase C activity and depletion of the protein kinase C polypeptide. When the γ isoenzyme of PKC is transiently expressed in COS-1 cells and exposed to phorbol esters, PKC-γ is downregulated in COS cells although these cells do not normally express this subtype. A point mutation in the purative ATP-binding site (Lys-380→Met-380) of the protein kinase C γ isoenzyme which results in a kinase-deficient enzyme does not interfere with this downregulation. Our results suggest that autophosphorylation or constitutive signalling through the protein kinase C-γ kinase domain is not a prerequisite for downregulation of PKC activity.

Original languageEnglish
Pages (from-to)262-266
Number of pages5
JournalFEBS Letters
Volume280
Issue number2
DOIs
Publication statusPublished - Mar 25 1991
Externally publishedYes

Fingerprint

Protein Kinase C
Phosphotransferases
Down-Regulation
Phorbol Esters
COS Cells
Isoenzymes
Point Mutation
Tumors
Adenosine Triphosphate
Chemical activation
Binding Sites
Peptides
Enzymes
Neoplasms

Keywords

  • Baculovirus expression
  • Downregulation
  • Kinase-deficient mutant
  • Phorbol ester
  • Protein kinase C

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Downregulation of protein kinase C-γ is independent of a functional kinase domain. / Freisewinkel, Ina; Riethmacher, Dieter; Stabel, Silvia.

In: FEBS Letters, Vol. 280, No. 2, 25.03.1991, p. 262-266.

Research output: Contribution to journalArticle

Freisewinkel, Ina ; Riethmacher, Dieter ; Stabel, Silvia. / Downregulation of protein kinase C-γ is independent of a functional kinase domain. In: FEBS Letters. 1991 ; Vol. 280, No. 2. pp. 262-266.
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