| pubmed-article:11294894 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11294894 | lifeskim:mentions | umls-concept:C0243982 | lld:lifeskim |
| pubmed-article:11294894 | lifeskim:mentions | umls-concept:C0021699 | lld:lifeskim |
| pubmed-article:11294894 | lifeskim:mentions | umls-concept:C1825794 | lld:lifeskim |
| pubmed-article:11294894 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:11294894 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:11294894 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:11294894 | pubmed:dateCreated | 2001-4-11 | lld:pubmed |
| pubmed-article:11294894 | pubmed:abstractText | The actin cytoskeleton plays a significant role in changes of cell shape and motility, and interactions between the actin filaments and the cell membrane are crucial for a variety of cellular processes. Several adaptor proteins, including talin, maintain the cytoskeleton-membrane linkage by binding to integral membrane proteins and to the cytoskeleton. Layilin, a recently characterized transmembrane protein with homology to C-type lectins, is a membrane-binding site for talin in peripheral ruffles of spreading cells. To facilitate studies of layilin's function, we have generated a layilin-Fc fusion protein comprising the extracellular part of layilin joined to human immunoglobulin G heavy chain and used this chimera to identify layilin ligands. Here, we demonstrate that layilin-Fc fusion protein binds to hyaluronan immobilized to Sepharose. Microtiter plate-binding assays, coprecipitation experiments, and staining of sections predigested with different glycosaminoglycan-degrading enzymes and cell adhesion assays all revealed that layilin binds specifically to hyaluronan but not to other tested glycosaminoglycans. Layilin's ability to bind hyaluronan, a ubiquitous extracellular matrix component, reveals an interesting parallel between layilin and CD44, because both can bind to cytoskeleton-membrane linker proteins through their cytoplasmic domains and to hyaluronan through their extracellular domains. This parallelism suggests a role for layilin in cell adhesion and motility. | lld:pubmed |
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| pubmed-article:11294894 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11294894 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11294894 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11294894 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11294894 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11294894 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:11294894 | pubmed:issn | 1059-1524 | lld:pubmed |
| pubmed-article:11294894 | pubmed:author | pubmed-author:BoniVV | lld:pubmed |
| pubmed-article:11294894 | pubmed:author | pubmed-author:HynesR ORO | lld:pubmed |
| pubmed-article:11294894 | pubmed:author | pubmed-author:RubioJJ | lld:pubmed |
| pubmed-article:11294894 | pubmed:author | pubmed-author:HigginsJ MJM | lld:pubmed |
| pubmed-article:11294894 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11294894 | pubmed:volume | 12 | lld:pubmed |
| pubmed-article:11294894 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11294894 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11294894 | pubmed:pagination | 891-900 | lld:pubmed |
| pubmed-article:11294894 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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