Source:http://linkedlifedata.com/resource/pubmed/id/18621433
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
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pubmed:dateCreated |
2008-9-15
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pubmed:abstractText |
Syndecan-4, a cell surface heparan sulfate proteoglycan, is known to regulate the organization of the cytoskeleton, and oligomerization is crucial for syndecan-4 function. We therefore explored a possible regulatory effect of syndecan-4 oligomerization on the cytoskeleton. Glutathione-S-transferase-syndecan-4 proteins were used to show that syndecan-4 interacted specifically with alpha-actinin, but not paxillin, talin, and vinculin. Interestingly, only dimeric, and not monomeric, recombinant syndecan-4 interacted with alpha-actinin in the presence of phosphatidylinositol 4,5-bisphosphate (PIP2), and PIP2 potentiated the interaction of both the cytoplasmic domain syndecan-4 peptide and recombinant syndecan-4 proteins with alpha-actinin, implying that oligomerization of syndecan-4 was important for this interaction. Consistent with this notion, alpha-actinin interaction was largely absent in syndecan-4 mutants defective in transmembrane domain-induced oligomerization, and alpha-actinin-associated focal adhesions were decreased in rat embryo fibroblasts expressing mutant syndecan-4. Besides, this interaction was consistently lower with the phosphorylation-mimicking syndecan-4 mutant S183E which is known to destabilize the oligomerization of the syndecan-4 cytoplasmic domain. Taken together, the data suggest that the oligomeric status of syndecan-4 plays a crucial role in regulating the interaction of syndecan-4 with alpha-actinin.
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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 |
Oct
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pubmed:issn |
0171-9335
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
87
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
807-15
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pubmed:meshHeading |
pubmed-meshheading:18621433-Actinin,
pubmed-meshheading:18621433-Amino Acid Sequence,
pubmed-meshheading:18621433-Animals,
pubmed-meshheading:18621433-Cell Membrane,
pubmed-meshheading:18621433-Cells, Cultured,
pubmed-meshheading:18621433-Cytoplasm,
pubmed-meshheading:18621433-Cytoskeleton,
pubmed-meshheading:18621433-Focal Adhesions,
pubmed-meshheading:18621433-Membrane Glycoproteins,
pubmed-meshheading:18621433-Molecular Sequence Data,
pubmed-meshheading:18621433-Phosphatidylinositol 4,5-Diphosphate,
pubmed-meshheading:18621433-Phosphorylation,
pubmed-meshheading:18621433-Protein Structure, Tertiary,
pubmed-meshheading:18621433-Rats,
pubmed-meshheading:18621433-Syndecan-4
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pubmed:year |
2008
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pubmed:articleTitle |
The oligomeric status of syndecan-4 regulates syndecan-4 interaction with alpha-actinin.
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pubmed:affiliation |
Department of Life Sciences, Ewha Womans University, Daehyun-dong, Seodaemoon-Gu, Seoul 120-750, Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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