Linked Life Data

8504798

Source:http://linkedlifedata.com/resource/pubmed/id/8504798

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1993-7-8
pubmed:abstractText
The cytoskeletal component vinculin has been demonstrated by hydrophobic photoradiolabelling, to insert into bilayers containing acidic phospholipids and trace amounts of a photoactivatable analogue of lecithin. It is shown in this study that the higher-molecular-mass variant metavinculin and alpha-actinin, also share this property. alpha-Actinin and vinculin were also shown to associate with phosphatidylserine liposomes by chromatography of protein/lipid mixtures on a Bio-Gel A-5m column. Furthermore, interesting differences in the behaviour of binary mixtures of these proteins, in the presence of phosphatidylserine liposomes, are shown. Thus, incubation of alpha-actinin with vinculin or metavinculin, prior to the addition of liposomes, strongly inhibited the photoradiolabelling of alpha-actinin under conditions in which the liposome surface was non-limiting, but enhanced the labelling of vinculin. In contrast, vinculin and metavinculin did not mutually influence their labelling. Using gel-filtration chromatography, it was shown that alpha-actinin still bound to the vinculin-liposome complex, under conditions similar to those used for hydrophobic photolabelling with a non-limiting lipid surface. In the presence of limiting amounts of liposomes, the alpha-actinin/vinculin ratio was markedly decreased in the liposome fractions. Our results suggest the formation of a ternary complex consisting of vinculin, alpha-actinin and phospholipids. In this complex, both proteins interact at the bilayer, resulting in an altered conformation of the two proteins and, as a consequence, in modified bilayer interactions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
213
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1009-15
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Evidence for a ternary interaction between alpha-actinin, (meta)vinculin and acidic-phospholipid bilayers.
pubmed:affiliation
Department of Pathology, University of Bern, Switzerland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't