Primary Structure and MRNA Localization of Protein F1, a Growth-related Protein Kinase C Substrate Associated with Synaptic Plasticity

Overview

Journal EMBO J

Specialties Biotechnology
Molecular Biology

Date 1987 Dec 1

PMID 3428269

Citations 24

Authors

A Rosenthal

S Y Chan

W Henzel

C Haskell

W J Kuang

E Chen

J N Wilcox

A Ullrich

D V Goeddel

A Routtenberg

Affiliations

Soon will be listed here.

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.

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