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Primary structure and mRNA localization of protein F1, a growth‐related protein kinase C substrate associated with synaptic plasticity.
Author(s) -
Rosenthal A.,
Chan S. Y.,
Henzel W.,
Haskell C.,
Kuang W. J.,
Chen E.,
Wilcox J. N.,
Ullrich A.,
Goeddel D. V.,
Routtenberg A.
Publication year - 1987
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1987.tb02696.x
Subject(s) - biology , library science , computer science
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.