| pubmed-article:16492705 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16492705 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:16492705 | lifeskim:mentions | umls-concept:C2703161 | lld:lifeskim |
| pubmed-article:16492705 | lifeskim:mentions | umls-concept:C0597298 | lld:lifeskim |
| pubmed-article:16492705 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:16492705 | lifeskim:mentions | umls-concept:C1416800 | lld:lifeskim |
| pubmed-article:16492705 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:16492705 | pubmed:issue | Pt 6 | lld:pubmed |
| pubmed-article:16492705 | pubmed:dateCreated | 2006-3-9 | lld:pubmed |
| pubmed-article:16492705 | pubmed:abstractText | Palladin is a recently described phosphoprotein with an important role in cytoskeletal organization. The major palladin isoform (90-92 kDa) binds to three actin-associated proteins (ezrin, VASP and alpha-actinin), suggesting that palladin functions as a cytoskeletal scaffold. Here, we describe the organization of the palladin gene, which encodes multiple isoforms, including one (140 kDa) with a similar localization pattern to 90 kDa palladin. Overexpression of the 90 kDa or 140 kDa isoforms in COS-7 cells results in rearrangements of the actin cytoskeleton into super-robust bundles and star-like arrays, respectively. Sequence analysis of 140 kDa palladin revealed a conserved binding site for SH3 domains, suggesting that it binds directly to the SH3-domain protein Lasp-1. Binding of 140 kDa palladin, but not 90 kDa palladin, to Lasp-1 was confirmed by yeast two-hybrid and GST-pull-down assays. Isoform-specific siRNA experiments suggested that 140 kDa palladin plays a role in recruiting Lasp-1 to stress fibers. These results add Lasp-1, an actin-binding protein with a crucial role in cell motility, to the growing list of palladin's binding partners, and suggest that 140 kDa palladin has a specialized function in organizing the actin arrays that participate in cell migration and/or cellular contractility. | lld:pubmed |
| pubmed-article:16492705 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16492705 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16492705 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16492705 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16492705 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16492705 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16492705 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16492705 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16492705 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16492705 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:16492705 | pubmed:issn | 0021-9533 | lld:pubmed |
| pubmed-article:16492705 | pubmed:author | pubmed-author:OteyCarol ACA | lld:pubmed |
| pubmed-article:16492705 | pubmed:author | pubmed-author:RachlinAndrew... | lld:pubmed |
| pubmed-article:16492705 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16492705 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:16492705 | pubmed:volume | 119 | lld:pubmed |
| pubmed-article:16492705 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16492705 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16492705 | pubmed:pagination | 995-1004 | lld:pubmed |
| pubmed-article:16492705 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:16492705 | pubmed:meshHeading | pubmed-meshheading:16492705... | lld:pubmed |
| pubmed-article:16492705 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16492705 | pubmed:articleTitle | Identification of palladin isoforms and characterization of an isoform-specific interaction between Lasp-1 and palladin. | lld:pubmed |
| pubmed-article:16492705 | pubmed:affiliation | Department of Cell and Molecular Physiology, University of North Carolina School of Medicine, Chapel Hill, NC 27599-7545, USA. | lld:pubmed |
| pubmed-article:16492705 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16492705 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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