Molecular cloning and expression of the major protein kinase C substrate of platelets View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1988-06

AUTHORS

Michael Tyers, Richard A. Rachubinski, Mary I. Stewart, Angela M. Varrichio, Robert G. L. Shorr, Richard J. Haslam, Calvin B. Harley

ABSTRACT

In platelets, agonists that stimulate phosphoinositide turnover cause the rapid phosphorylation of a protein of apparent relative molecular mass (Mr) 40–47,000, called P47, by protein kinase C (PKC)1–4. Diverse identities have been ascribed to P47 including lipocortin5, inositol 1,4,5-trisphosphate 5-phosphomonoesterase6, pyruvate dehydrogenase α subunit7 and an actin regulatory protein8. We have isolated human P47 clones by immunological screening of a λgtll complementary DNA library from HL-60 cells, a human promyelocytic leukaemia cell line9. P47 recom-binants thus identified hybridized to a 3.0 kilobase (kb) messenger RNA in mature white blood cell lines; the same mRNA was induced in HL-60 cells during differentiation. A 1,050 base pair (bp) open reading frame that could encode a protein of Mr 40,087 was confirmed by comparison with peptide sequences from platelet P47, and by expression of the putative recombinant P47 in E. coli and in vitro. The P47 sequence appears to have been conserved throughout vertebrate evolution, and is not similar to any other known sequence including human lipocortin and the α subunit of pyruvate dehydrogenase. The P47 protein contains a potential Ca2+-binding 'EF-hand' structure and a region that strongly resembles known PKC phosphorylation sites. More... »

PAGES

470-473

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/333470a0

DOI

http://dx.doi.org/10.1038/333470a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1022440822

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/2897630


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