Source:http://linkedlifedata.com/resource/pubmed/id/17990980
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
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| pubmed:dateCreated |
2008-2-7
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| pubmed:abstractText |
The membrane-bound mucins have a heavily O-glycosylated extracellular domain, a single-pass membrane domain and a short cytoplasmic tail. Three of the membrane-bound mucins,MUC3, MUC12 and MUC17, are clustered on chromosome 7 and found in the gastrointestinal tract. These mucins have C-terminal sequences typical of PDZ-domain-binding proteins. To identify PDZ proteins that are able to interact with the mucins,we screened PDZ domain arrays using YFP (yellow fluorescent protein)-tagged proteins. MUC17 exhibited a strong binding to PDZK1 (PDZ domain containing 1), whereas the binding toNHERF1 (Na+/H+-exchanger regulatory factor 1) was weak.Furthermore, we showed weak binding of MUC12 to PDZK1, NHERF1 and NHERF2. GST (glutathione transferase) pull-down experiments confirmed that the C-terminal tail of MUC17 coprecipitates with the scaffold protein PDZK1 as identified byMS. This was mediated through the C-terminal PDZ-interaction site in MUC17, which was capable of binding to three of the four PDZ domains in PDZK1. Immunostaining of wild-type or Pdzk1-/- mouse jejunum with an antiserum against Muc3(17),the mouse orthologue of human MUC17, revealed strong brushborder membrane staining in the wild-type mice compared with an intracellular Muc3(17) staining in the Pdzk1-/- mice. This suggests that Pdzk1 plays a specific role in stabilizing Muc3(17)in the apical membrane of small intestinal enterocytes.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/MUC17 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Mucins,
http://linkedlifedata.com/resource/pubmed/chemical/PDZK1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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| pubmed:status |
MEDLINE
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| pubmed:month |
Mar
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| pubmed:issn |
1470-8728
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| pubmed:author | |
| pubmed:issnType |
Electronic
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| pubmed:day |
1
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| pubmed:volume |
410
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
283-9
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| pubmed:meshHeading |
pubmed-meshheading:17990980-Adenocarcinoma,
pubmed-meshheading:17990980-Animals,
pubmed-meshheading:17990980-Base Sequence,
pubmed-meshheading:17990980-Binding Sites,
pubmed-meshheading:17990980-Carrier Proteins,
pubmed-meshheading:17990980-Cell Line,
pubmed-meshheading:17990980-Cell Line, Tumor,
pubmed-meshheading:17990980-Cell Membrane,
pubmed-meshheading:17990980-Cloning, Molecular,
pubmed-meshheading:17990980-Colonic Neoplasms,
pubmed-meshheading:17990980-Cricetinae,
pubmed-meshheading:17990980-Cytoplasm,
pubmed-meshheading:17990980-DNA Primers,
pubmed-meshheading:17990980-Humans,
pubmed-meshheading:17990980-Intestinal Mucosa,
pubmed-meshheading:17990980-Intestine, Small,
pubmed-meshheading:17990980-Kidney,
pubmed-meshheading:17990980-Mesocricetus,
pubmed-meshheading:17990980-Microvilli,
pubmed-meshheading:17990980-Molecular Sequence Data,
pubmed-meshheading:17990980-Mucins,
pubmed-meshheading:17990980-Recombinant Proteins
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| pubmed:year |
2008
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| pubmed:articleTitle |
The C-terminus of the transmembrane mucin MUC17 binds to the scaffold protein PDZK1 that stably localizes it to the enterocyte apical membrane in the small intestine.
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| pubmed:affiliation |
Department of Medical Biochemistry and Cell Biology, Göteborg University, 413 90 Gothenburg, Sweden.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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