Molecular cloning, characterization, and expression of a cDNA encoding the '80- to 87-kDa' myristoylated alanine-rich C kinase substrate: A major cellular substrate for protein kinase C

D. J. Stumpo, J. M. Graff, K. A. Albert, P. Greengard, P. J. Blackshear

Research output: Contribution to journalArticle

252 Citations (Scopus)

Abstract

We isolated and sequenced a cDNA clone encoding the bovine '80- to 87-kDa' protein, a major cellular substrate for protein kinase C. An open reading frame of 1005 base pairs predicted a protein of 335 amino acids (M(r), 31,949). Despite this predicted size, the protein migrated on SDS/polyacrylamide gels with an apparent molecular weight of 80-87,000 after expression of the cDNA in cells lacking the protein. It was highly enriched in alanine (28.4 mol %), contained an amino-terminal myristoylation consensus sequence, and included a 25-residue basic domain containing the known protein kinase C phosphorylation sites. Two mRNA species (2.6 and 4.4 kilobases) were mostly highly expressed in brain, spinal cord, spleen, and lung, in parallel with the distribution of immunoreactive protein. Genomic blot analysis indicated the likelihood of a single gene coding for this mRNA. We propose the name myristoylated alanine-rich C kinase substrate (MARCKS) for this protein.

Original languageEnglish (US)
Pages (from-to)4012-4016
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume86
Issue number11
StatePublished - 1989

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Molecular Cloning
Protein Kinase C
Complementary DNA
Proteins
Messenger RNA
Consensus Sequence
Base Pairing
Alanine
Open Reading Frames
Names
myristoylated alanine-rich C kinase substrate
Spinal Cord
Spleen
Clone Cells
Molecular Weight
Phosphorylation
Amino Acids
Lung
Brain
Genes

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

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title = "Molecular cloning, characterization, and expression of a cDNA encoding the '80- to 87-kDa' myristoylated alanine-rich C kinase substrate: A major cellular substrate for protein kinase C",
abstract = "We isolated and sequenced a cDNA clone encoding the bovine '80- to 87-kDa' protein, a major cellular substrate for protein kinase C. An open reading frame of 1005 base pairs predicted a protein of 335 amino acids (M(r), 31,949). Despite this predicted size, the protein migrated on SDS/polyacrylamide gels with an apparent molecular weight of 80-87,000 after expression of the cDNA in cells lacking the protein. It was highly enriched in alanine (28.4 mol {\%}), contained an amino-terminal myristoylation consensus sequence, and included a 25-residue basic domain containing the known protein kinase C phosphorylation sites. Two mRNA species (2.6 and 4.4 kilobases) were mostly highly expressed in brain, spinal cord, spleen, and lung, in parallel with the distribution of immunoreactive protein. Genomic blot analysis indicated the likelihood of a single gene coding for this mRNA. We propose the name myristoylated alanine-rich C kinase substrate (MARCKS) for this protein.",
author = "Stumpo, {D. J.} and Graff, {J. M.} and Albert, {K. A.} and P. Greengard and Blackshear, {P. J.}",
year = "1989",
language = "English (US)",
volume = "86",
pages = "4012--4016",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
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TY - JOUR

T1 - Molecular cloning, characterization, and expression of a cDNA encoding the '80- to 87-kDa' myristoylated alanine-rich C kinase substrate

T2 - A major cellular substrate for protein kinase C

AU - Stumpo, D. J.

AU - Graff, J. M.

AU - Albert, K. A.

AU - Greengard, P.

AU - Blackshear, P. J.

PY - 1989

Y1 - 1989

N2 - We isolated and sequenced a cDNA clone encoding the bovine '80- to 87-kDa' protein, a major cellular substrate for protein kinase C. An open reading frame of 1005 base pairs predicted a protein of 335 amino acids (M(r), 31,949). Despite this predicted size, the protein migrated on SDS/polyacrylamide gels with an apparent molecular weight of 80-87,000 after expression of the cDNA in cells lacking the protein. It was highly enriched in alanine (28.4 mol %), contained an amino-terminal myristoylation consensus sequence, and included a 25-residue basic domain containing the known protein kinase C phosphorylation sites. Two mRNA species (2.6 and 4.4 kilobases) were mostly highly expressed in brain, spinal cord, spleen, and lung, in parallel with the distribution of immunoreactive protein. Genomic blot analysis indicated the likelihood of a single gene coding for this mRNA. We propose the name myristoylated alanine-rich C kinase substrate (MARCKS) for this protein.

AB - We isolated and sequenced a cDNA clone encoding the bovine '80- to 87-kDa' protein, a major cellular substrate for protein kinase C. An open reading frame of 1005 base pairs predicted a protein of 335 amino acids (M(r), 31,949). Despite this predicted size, the protein migrated on SDS/polyacrylamide gels with an apparent molecular weight of 80-87,000 after expression of the cDNA in cells lacking the protein. It was highly enriched in alanine (28.4 mol %), contained an amino-terminal myristoylation consensus sequence, and included a 25-residue basic domain containing the known protein kinase C phosphorylation sites. Two mRNA species (2.6 and 4.4 kilobases) were mostly highly expressed in brain, spinal cord, spleen, and lung, in parallel with the distribution of immunoreactive protein. Genomic blot analysis indicated the likelihood of a single gene coding for this mRNA. We propose the name myristoylated alanine-rich C kinase substrate (MARCKS) for this protein.

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