Source:http://linkedlifedata.com/resource/pubmed/id/10527873
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1999-11-12
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pubmed:databankReference | |
pubmed:abstractText |
We have recently isolated a novel proline-rich synapse-associated protein-1 (ProSAP1) that is highly enriched in postsynaptic density (PSD). A closely related multidomain protein, ProSAP2, shares a highly conserved PDZ (PSD-95/discs-large/ZO-1) domain (80% identity), a ppI domain that mediates the interaction with cortactin, and a C-terminal SAM (sterile alpha-motif) domain. In addition, ProSAP2 codes for five ankyrin repeats and a SH3 (Src homology 3) domain. Transcripts for both proteins are coexpressed in many regions of rat brain, but show a distinct expression pattern in the cerebellum. Using the PDZ domains of ProSAP1 and 2 as bait in the yeast two-hybrid system, we isolated several clones of the SAPAP/GKAP (SAP90/PSD-95-associated protein/guanylate kinase-associated protein) family. The association of the proteins was verified by coimmunoprecipitation and cotransfection in HEK cells. Therefore, proteins of the ProSAP family represent a novel link between SAP90/PSD-95 bound membrane receptors and the cytoskeleton at glutamatergic synapses of the central nervous system.
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pubmed:grant | |
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 |
0006-291X
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 1999 Academic Press.
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pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
264
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
247-52
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:10527873-Amino Acid Sequence,
pubmed-meshheading:10527873-Animals,
pubmed-meshheading:10527873-Brain,
pubmed-meshheading:10527873-Carrier Proteins,
pubmed-meshheading:10527873-Cytoskeleton,
pubmed-meshheading:10527873-Molecular Sequence Data,
pubmed-meshheading:10527873-Nerve Tissue Proteins,
pubmed-meshheading:10527873-Rats,
pubmed-meshheading:10527873-Sequence Homology, Amino Acid,
pubmed-meshheading:10527873-Synaptic Membranes
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pubmed:year |
1999
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pubmed:articleTitle |
Proline-rich synapse-associated proteins ProSAP1 and ProSAP2 interact with synaptic proteins of the SAPAP/GKAP family.
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pubmed:affiliation |
Department of Neurochemistry and Molecular Biology, Leibniz Institute for Neurobiology, Magdeburg, 39118, Germany. bockers@uni-muenster.de
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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