Primary structure and mRNA localization of protein F1, a growth-related protein kinase C substrate associated with synaptic plasticity.

A. Rosenthal*, S. Y. Chan, W. Henzel, C. Haskell, W. J. Kuang, E. Chen, J. N. Wilcox, A. Ullrich, D. V. Goeddel, A. Routtenberg

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

154 Scopus citations

Abstract

Protein F1 is a neuron-specific, synaptic-enriched, membrane-bound substrate of protein kinase C (PKC) whose phosphorylation is related to synaptic plasticity in the adult. The sequence of 26 N-terminal amino acids was determined from purified rat protein F1. A 78-mer synthetic oligonucleotide designed from the partial N-terminal sequence enabled identification of protein F1 cDNA clones in a rat brain library. F1 protein is a 226 amino acid protein encoded by a 1.5 kb brain-specific, developmentally-regulated mRNA. Transcripts for protein F1 can be detected at birth, and their level declines after maturation. A full-length cDNA clone was transcribed and translated in vitro. Translation products could be immunoprecipitated with anti-F1 antibodies. In situ hybridization analysis revealed protein F1 transcripts in hippocampal pyramidal cells, but not in granule cells. In cerebellum, granule cells contained protein F1 mRNA, while Purkinje cells did not. Co-localization of protein F1 with protein kinase C-II [PKC-II (beta)], rather than PKC-I (gamma) suggests that PKC-II may phosphorylate protein F1.

Original languageEnglish (US)
Pages (from-to)3641-3646
Number of pages6
JournalThe EMBO journal
Volume6
Issue number12
DOIs
StatePublished - Dec 1 1987

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

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