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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
52
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pubmed:dateCreated |
2005-12-26
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pubmed:abstractText |
The syndecans are known to form homologous oligomers that may be important for their functions. We have therefore determined the role of oligomerization of syndecan-2 and syndecan-4. A series of glutathione S-transferase-syndecan-2 and syndecan-4 chimeric proteins showed that all syndecan constructs containing the transmembrane domain formed SDS-resistant dimers, but not those lacking it. SDS-resistant dimer formation was hardly seen in the syndecan chimeras where each transmembrane domain was substituted with that of platelet-derived growth factor receptor (PDGFR). Increased MAPK activity was detected in HEK293T cells transfected with syndecan/PDGFR chimeras in a syndecan transmembrane domain-dependent fashion. The chimera-induced MAPK activation was independent of both ligand and extracellular domain, implying that the transmembrane domain is sufficient to induce dimerization/oligomerization in vivo. Furthermore, the syndecan chimeras were defective in syndecan-4-mediated focal adhesion formation and protein kinase Calpha activation or in syndecan-2-mediated cell migration. Taken together, these data suggest that the transmembrane domains are sufficient for inducing dimerization and that transmembrane domain-induced oligomerization is crucial for syndecan-2 and syndecan-4 functions.
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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/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C-alpha,
http://linkedlifedata.com/resource/pubmed/chemical/Proteoglycans,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Platelet-Derived Growth...,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SDC2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/SDC4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Syndecan-2,
http://linkedlifedata.com/resource/pubmed/chemical/Syndecan-4
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
280
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
42573-9
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:16253987-Amino Acid Sequence,
pubmed-meshheading:16253987-Cell Adhesion,
pubmed-meshheading:16253987-Cell Line,
pubmed-meshheading:16253987-Cell Movement,
pubmed-meshheading:16253987-DNA Primers,
pubmed-meshheading:16253987-Dimerization,
pubmed-meshheading:16253987-Enzyme Activation,
pubmed-meshheading:16253987-Genetic Vectors,
pubmed-meshheading:16253987-Glutathione Transferase,
pubmed-meshheading:16253987-Humans,
pubmed-meshheading:16253987-Immunoblotting,
pubmed-meshheading:16253987-Ligands,
pubmed-meshheading:16253987-MAP Kinase Signaling System,
pubmed-meshheading:16253987-Membrane Glycoproteins,
pubmed-meshheading:16253987-Molecular Sequence Data,
pubmed-meshheading:16253987-Mutation,
pubmed-meshheading:16253987-Protein Binding,
pubmed-meshheading:16253987-Protein Kinase C-alpha,
pubmed-meshheading:16253987-Protein Structure, Tertiary,
pubmed-meshheading:16253987-Proteoglycans,
pubmed-meshheading:16253987-Receptors, Platelet-Derived Growth Factor,
pubmed-meshheading:16253987-Recombinant Fusion Proteins,
pubmed-meshheading:16253987-Syndecan-2,
pubmed-meshheading:16253987-Syndecan-4,
pubmed-meshheading:16253987-Transfection
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pubmed:year |
2005
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pubmed:articleTitle |
Transmembrane domain-induced oligomerization is crucial for the functions of syndecan-2 and syndecan-4.
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pubmed:affiliation |
Department of Life Sciences, Division of Molecular Life Sciences and Center for Cell Signaling Research, Ewha Womans University, Seoul 120-750, Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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