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Regulation of recombinant PKC alpha activity by protein phosphatase 1 and protein phosphatase 2A.
Journal article

Regulation of recombinant PKC alpha activity by protein phosphatase 1 and protein phosphatase 2A.

  • Ricciarelli R Institut für Biochemie und Molekularbiologie, Universität Bern, Bühlstrasse 28, Bern, 3012, Switzerland.
  • Azzi A
  • 1998-07-24
Published in:
  • Archives of biochemistry and biophysics. - 1998
Adenosine Triphosphate
Enzyme Activation
Isoenzymes
Membrane Proteins
Phosphoprotein Phosphatases
Phosphorylation
Protein Kinase C
Protein Kinase C-alpha
Protein Phosphatase 1
Protein Phosphatase 2
Recombinant Proteins
English The sensitivity of PKC alpha to two protein phosphatases (PP1 and PP2A) has been studied. The results show that both phosphatases reversibly inhibit PKC alpha activity suggesting an effect at PKC autophosphorylation sites and not at transphosphorylation sites. Moreover, PP1 has been found at low concentration to activate PKC alpha implying the existence of an inhibitory phosphorylation site. Further, PKC alpha has been shown to phosphorylate PP2A at its regulatory subunit B.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://sonar.ch/global/documents/70770
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