Linked Life Data

9665728

Source:http://linkedlifedata.com/resource/pubmed/id/9665728

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
28
pubmed:dateCreated
1998-8-12
pubmed:abstractText
The tail domain of vinculin (Vt) contains a salt-insensitive binding site for acidic phospholipids which is masked by the intramolecular head-tail interaction in native vinculin [Johnson, R. P., and Craig, S. W. (1995) Biochem. Biophys. Res. Commun. 210, 159-164]. To characterize further this phospholipid binding site, we have used hydrophobic photolabeling with a photoactivatable phosphatidylcholine analogue to detect insertion of protein into the lipid bilayer. We show here that, although the properties of binding to acidic phospholipid vesicles and spontaneous insertion into the bilayer are cryptic and inactive in vinculin at physiologic ionic strength, these activities of the purified tail domain can be activated by physical and chemical disruption of the intramolecular interaction between the head and tail domains. By analyzing the lipid binding and insertion activity of a series of GST-Vt fusion proteins, we defined 55 amino acids, comprising vinculin residues 916-970, that mimic the lipid-binding and insertion activity of Vt. Predictions of secondary structure suggest that these 55 amino acids form a basic, amphipathic helical hairpin. This prediction is supported by circular dichroism analysis, which indicates that at least 80% of the residues in residues 916-970 are in a helical conformation. This predicted helical hairpin motif, which is conserved in all vinculins and is present in an acidic phospholipid-binding region of alpha-catenin, is distinct from C2 and PH domains, and likely represents a third type of acidic phospholipid-binding structure.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
37
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10211-22
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:9665728-Amino Acid Sequence, pubmed-meshheading:9665728-Animals, pubmed-meshheading:9665728-Chickens, pubmed-meshheading:9665728-Circular Dichroism, pubmed-meshheading:9665728-Conserved Sequence, pubmed-meshheading:9665728-Freezing, pubmed-meshheading:9665728-Hydrogen-Ion Concentration, pubmed-meshheading:9665728-Lipid Bilayers, pubmed-meshheading:9665728-Liposomes, pubmed-meshheading:9665728-Macromolecular Substances, pubmed-meshheading:9665728-Molecular Sequence Data, pubmed-meshheading:9665728-Osmolar Concentration, pubmed-meshheading:9665728-Peptide Fragments, pubmed-meshheading:9665728-Phosphatidylinositols, pubmed-meshheading:9665728-Phosphatidylserines, pubmed-meshheading:9665728-Phospholipids, pubmed-meshheading:9665728-Photoaffinity Labels, pubmed-meshheading:9665728-Protein Binding, pubmed-meshheading:9665728-Protein Structure, Secondary, pubmed-meshheading:9665728-Protein Structure, Tertiary, pubmed-meshheading:9665728-Sensitivity and Specificity, pubmed-meshheading:9665728-Vinculin
pubmed:year
1998
pubmed:articleTitle
A conserved motif in the tail domain of vinculin mediates association with and insertion into acidic phospholipid bilayers.
pubmed:affiliation
Department of Biological Chemistry, Johns Hopkins School of Medicine, Baltimore, Maryland 21205, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't