Source:http://linkedlifedata.com/resource/pubmed/id/10967549
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2000-11-9
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pubmed:abstractText |
A yeast two-hybrid screen was employed to identify ligands for the cytoplasmic domain of the NG2 chondroitin sulfate proteoglycan. Two overlapping cDNA clones selected in the screen are identical in sequence to a DNA segment coding for the most amino-terminal of the 13 PDZ domains found in the multi-PDZ-protein MUPP1. Antibodies made against recombinant polypeptides representing these two clones (NIP-2 and NIP-7) are reactive with the same 250-kDa molecule recognized by anti-MUPP1 antibodies, confirming the presence of the NIP-2 and NIP-7 sequences in the MUPP1 protein. NIP-2 and NIP-7 GST fusion proteins effectively recognize NG2 in pull-down assays, demonstrating the ability of these polypeptide segments to interact with the intact proteoglycan. The fusion proteins fail to bind NG2 missing the C-terminal half of the cytoplasmic domain, emphasizing the role of the NG2 C-terminus in the interaction with MUPP1. The existence of an NG2/MUPP1 interaction in situ is demonstrated by the ability of NG2 antibodies to co-immunoprecipitate both NG2 and MUPP1 from detergent extracts of cells expressing the two molecules. MUPP1 may serve as a multivalent scaffold that provides a means of linking NG2 with key structural and/or signaling components in the cytoplasm.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/MPDZ protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Proteoglycans,
http://linkedlifedata.com/resource/pubmed/chemical/chondroitin sulfate proteoglycan 4
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0730-2312
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 2000 Wiley-Liss, Inc.
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pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
79
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
213-24
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:10967549-Amino Acid Sequence,
pubmed-meshheading:10967549-Antigens,
pubmed-meshheading:10967549-Base Sequence,
pubmed-meshheading:10967549-Carrier Proteins,
pubmed-meshheading:10967549-Cell Membrane,
pubmed-meshheading:10967549-Cytoplasm,
pubmed-meshheading:10967549-DNA, Complementary,
pubmed-meshheading:10967549-Humans,
pubmed-meshheading:10967549-Ligands,
pubmed-meshheading:10967549-Molecular Sequence Data,
pubmed-meshheading:10967549-Precipitin Tests,
pubmed-meshheading:10967549-Proteoglycans,
pubmed-meshheading:10967549-Sequence Homology, Nucleic Acid,
pubmed-meshheading:10967549-Signal Transduction,
pubmed-meshheading:10967549-Tumor Cells, Cultured
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pubmed:year |
2000
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pubmed:articleTitle |
The multi-PDZ domain protein MUPP1 is a cytoplasmic ligand for the membrane-spanning proteoglycan NG2.
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pubmed:affiliation |
The Burnham Institute, Cancer Research Center, La Jolla, California 92037, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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