Protein kinase C phosphorylates a 47 Mr protein (F1) directly related to synaptic plasticity

Raymond F. Akers, Aryeh Routtenberg*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

148 Scopus citations

Abstract

Ca2+-phospholipid-dependent protein kinase C, and activators of protein kinase C (phosphatidylserine, phorbol esters) stimulate the in vitro phosphorylation of a 47 kdalton phosphoprotein (protein F1) previously shown (Routtenberg, Lovinger and Steward, Behav. neural Biol., 43 (1985) 3-11) to be directly related to the plasticity of long-term potentiation. These data indicate that protein F1 serves as a protein kinase C substrate, and suggest the hypothesis that protein kinase C is involved in processes of long-term potentiation.

Original languageEnglish (US)
Pages (from-to)147-151
Number of pages5
JournalBrain research
Volume334
Issue number1
DOIs
StatePublished - May 13 1985

Keywords

  • Ca
  • brain protein phosphorylation
  • long-term potentiation
  • phorbol esters
  • phospholipid
  • protein kinase C
  • synaptic plasticity

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Clinical Neurology
  • Developmental Biology

Fingerprint Dive into the research topics of 'Protein kinase C phosphorylates a 47 M<sub>r</sub> protein (F1) directly related to synaptic plasticity'. Together they form a unique fingerprint.

Cite this