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.
AUTOR(ES)
Stumpo, D J
RESUMO
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 (Mr, 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 most highly expressed in brain, spinal cord, spleen, and lung, in parallel with the distribution of immuno-reactive 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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=287378Documentos Relacionados
- Nucleotide sequence of a cDNA for the bovine myristoylated alanine-rich C kinase substrate (MARCKS).
- Expression of the major protein kinase C substrate, the acidic 80-kilodalton myristoylated alanine-rich C kinase substrate, increases sharply when Swiss 3T3 cells move out of cycle and enter G0.
- Sequence of a cDNA encoding a small polymorphic histidine- and alanine-rich protein from Plasmodium falciparum.
- Widespread occurrence of "87 kDa," a major specific substrate for protein kinase C.
- Effect of reduced myristoylated alanine-rich C kinase substrate expression on hippocampal mossy fiber development and spatial learning in mutant mice: Transgenic rescue and interactions with gene background