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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2005-12-21
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pubmed:abstractText |
Palladin is an actin-associated protein that has been suggested to play critical roles in establishing cell morphology and maintaining cytoskeletal organization in a wide variety of cell types. Palladin has been shown previously to bind directly to three different actin-binding proteins vasodilator-stimulated phosphoprotein (VASP), alpha-actinin and ezrin, suggesting that it functions as an organizing unit that recruits actin-regulatory proteins to specific subcellular sites. Palladin contains sequences resembling a motif known to bind profilin. Here, we demonstrate that palladin is a binding partner for profilin, interacting with profilin via a poly proline-containing sequence in the amino-terminal half of palladin. Double-label immunofluorescence staining shows that palladin and profilin partially colocalize in actin-rich structures in cultured astrocytes. Our results suggest that palladin may play an important role in recruiting profilin to sites of actin dynamics.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Profilins,
http://linkedlifedata.com/resource/pubmed/chemical/Proline,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/palladin protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/palladin protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/vasodilator-stimulated...
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1742-464X
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pubmed:author |
pubmed-author:BoukhelifaMalikaM,
pubmed-author:CarpenOlliO,
pubmed-author:HuttelmaierStefanS,
pubmed-author:JockuschBrigitte MBM,
pubmed-author:JohanssonThomasT,
pubmed-author:KarlssonRogerR,
pubmed-author:MozaMonicaM,
pubmed-author:OteyCarol ACA,
pubmed-author:ParastManaM,
pubmed-author:RachlinAndrewA,
pubmed-author:RoyParthaP
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pubmed:issnType |
Print
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pubmed:volume |
273
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
26-33
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:16367745-Amino Acid Sequence,
pubmed-meshheading:16367745-Animals,
pubmed-meshheading:16367745-Binding Sites,
pubmed-meshheading:16367745-COS Cells,
pubmed-meshheading:16367745-Cell Adhesion Molecules,
pubmed-meshheading:16367745-Cercopithecus aethiops,
pubmed-meshheading:16367745-Cytoskeletal Proteins,
pubmed-meshheading:16367745-Dose-Response Relationship, Drug,
pubmed-meshheading:16367745-Fluorescent Antibody Technique,
pubmed-meshheading:16367745-HeLa Cells,
pubmed-meshheading:16367745-Humans,
pubmed-meshheading:16367745-Mice,
pubmed-meshheading:16367745-Microfilament Proteins,
pubmed-meshheading:16367745-Models, Genetic,
pubmed-meshheading:16367745-Molecular Sequence Data,
pubmed-meshheading:16367745-Phosphoproteins,
pubmed-meshheading:16367745-Profilins,
pubmed-meshheading:16367745-Proline,
pubmed-meshheading:16367745-Recombinant Proteins,
pubmed-meshheading:16367745-Surface Plasmon Resonance,
pubmed-meshheading:16367745-Swiss 3T3 Cells,
pubmed-meshheading:16367745-Time Factors,
pubmed-meshheading:16367745-Transfection
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pubmed:year |
2006
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pubmed:articleTitle |
The proline-rich protein palladin is a binding partner for profilin.
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pubmed:affiliation |
Department of Cell and Molecular Physiology and Neuroscience Center, University of North Carolina at Chapel Hill, 27599-7545, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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