Linked Life Data

2557340

Source:http://linkedlifedata.com/resource/pubmed/id/2557340

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
36
pubmed:dateCreated
1990-2-1
pubmed:abstractText
We have evaluated the possibility that a major, abundant cellular substrate for protein kinase C might be a calmodulin-binding protein. We have recently labeled this protein, which migrates on sodium dodecyl sulfate-gel electrophoresis with an apparent Mr of 60,000 from chicken and 80,000-87,000 from bovine cells and tissues, the myristoylated alanine-rich C kinase substrate (MARCKS). The MARCKS proteins from both species could be cross-linked to 125I-calmodulin in a Ca2+-dependent manner. Phosphorylation of either protein by protein kinase C prevented 125I-calmodulin binding and cross-linking, suggesting that the calmodulin-binding domain might be located at or near the sites of protein kinase C phosphorylation. Both bovine and chicken MARCKS proteins contain an identical 25-amino acid domain that contains all 4 of the serine residues phosphorylated by protein kinase C in vitro. In addition, this domain is similar in sequence and structure to previously described calmodulin-binding domains. A synthetic peptide corresponding to this domain inhibited calmodulin binding to the MARCKS protein and also could be cross-linked to 125I-calmodulin in a calcium-dependent manner. In addition, protein kinase C-dependent phosphorylation of the synthetic peptide inhibited its binding and cross-linking to 125I-calmodulin. The peptide bound to fluorescently labeled 5-dimethylaminonaphthalene-1-sulfonyl-calmodulin with a dissociation constant of 2.8 nM, and inhibited the calmodulin-dependent activation of cyclic nucleotide phosphodiesterase with an IC50 of 4.8 nM. Thus, the peptide mimics the calmodulin-binding properties of the MARCKS protein and probably represents its calmodulin-binding domain. Phosphorylation of these abundant, high affinity calmodulin-binding proteins by protein kinase C in intact cells could cause displacement of bound calmodulin, perhaps leading to activation of Ca2+-calmodulin-dependent processes.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
264
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
21818-23
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:2557340-3',5'-Cyclic-GMP Phosphodiesterases, pubmed-meshheading:2557340-Amino Acid Sequence, pubmed-meshheading:2557340-Animals, pubmed-meshheading:2557340-Brain, pubmed-meshheading:2557340-Calmodulin, pubmed-meshheading:2557340-Cattle, pubmed-meshheading:2557340-Chickens, pubmed-meshheading:2557340-Cross-Linking Reagents, pubmed-meshheading:2557340-Intracellular Signaling Peptides and Proteins, pubmed-meshheading:2557340-Kinetics, pubmed-meshheading:2557340-Membrane Proteins, pubmed-meshheading:2557340-Molecular Sequence Data, pubmed-meshheading:2557340-Molecular Weight, pubmed-meshheading:2557340-Peptides, pubmed-meshheading:2557340-Phosphorylation, pubmed-meshheading:2557340-Protein Kinase C, pubmed-meshheading:2557340-Proteins, pubmed-meshheading:2557340-Rats, pubmed-meshheading:2557340-Substrate Specificity, pubmed-meshheading:2557340-Succinimides
pubmed:year
1989
pubmed:articleTitle
Phosphorylation-regulated calmodulin binding to a prominent cellular substrate for protein kinase C.
pubmed:affiliation
Howard Hughes Medical Institute Laboratories, Duke University Medical Center, Durham, North Carolina 27710.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't