Source:http://linkedlifedata.com/resource/pubmed/id/11067857
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
2001-5-23
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pubmed:abstractText |
Annexin II heterotetramer (AIIt) is a multifunctional Ca(2+)-binding protein composed of two 11-kDa subunits and two annexin II subunits. The annexin II subunit contains the binding sites for anionic phospholipids, heparin, and F-actin, whereas the p11 subunit provides a regulatory function. The F-actin-binding site is presently unknown. In the present study we have utilized site-directed mutagenesis to create annexin II mutants with truncations in the C terminus of the molecule. Interestingly, a mutant annexin II lacking its C-terminal 16, 13, or 9 amino acids was unable to bind to F-actin but still retained its ability to interact with both anionic phospholipids and heparin. Recombinant AIIt, composed of wild-type p11 subunits and the mutant annexin II subunits, was also unable to bundle F-actin. This loss of F-actin bundling activity was directly attributable to the inability of mutant AIIt to bind F-actin. These results establish for the first time that the annexin II C-terminal amino acid residues, LLYLCGGDD, participate in F-actin binding.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
16
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5310-5
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11067857-Actins,
pubmed-meshheading:11067857-Amino Acid Motifs,
pubmed-meshheading:11067857-Animals,
pubmed-meshheading:11067857-Annexin A2,
pubmed-meshheading:11067857-Binding Sites,
pubmed-meshheading:11067857-Kinetics,
pubmed-meshheading:11067857-Mutagenesis, Site-Directed,
pubmed-meshheading:11067857-Mutation,
pubmed-meshheading:11067857-Phospholipids
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pubmed:year |
2001
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pubmed:articleTitle |
The C terminus of annexin II mediates binding to F-actin.
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pubmed:affiliation |
Cancer Biology Research Group, Department of Biochemistry, University of Calgary, Calgary, Alberta T2N 4N1, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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