Source:http://linkedlifedata.com/resource/pubmed/id/14596619
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
44
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| pubmed:dateCreated |
2003-11-4
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| pubmed:abstractText |
Polycystin-1, the protein product of the polycystic kidney disease-1 (PKD1) gene, was originally predicted to be an integral membrane glycoprotein with 11 transmembrane (TM) domains (TM 1-11). Subsequent comparative sequence analyses led to a revision of the original model, which retained the overall topology and 11 TM segments (TM I-XI) but dropped 3 of the original domains and introduced 3 new TM domains. The membrane-spanning potential and the orientation of each of the proposed TM domains following the extracellular REJ domain (TM I-XI and TM 11) have now been tested. Using a series of N-terminal polycystin TM-glycosylation reporter gene fusions expressed in vivo, we assayed N-linked glycosylation of the C-terminal glycosylation reporter as an indicator of TM domain presence and orientation. This approach has clearly demonstrated that 7 of the 12 TM domains tested function as membrane-spanning domains. In vitro analysis of the topogenic potential of the five remaining TM domains revealed that four of these also function as membrane-spanning domains, thus supporting an 11 TM structure for polycystin-1 comprised of TM domains I-XI. In addition, these studies suggest that the membrane insertion of TM domains I-IX occurs in a cotranslational and sequential manner, while multiple topogenic determinants appear to be required for the integration of the C-terminal-most TM segments of polycystin-1.
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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/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/TRPP Cation Channels,
http://linkedlifedata.com/resource/pubmed/chemical/polycystic kidney disease 1 protein
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| pubmed:status |
MEDLINE
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| pubmed:month |
Nov
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| pubmed:issn |
0006-2960
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
11
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| pubmed:volume |
42
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
13035-48
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| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:14596619-Animals,
pubmed-meshheading:14596619-Cell Line,
pubmed-meshheading:14596619-Clone Cells,
pubmed-meshheading:14596619-Gene Expression Regulation,
pubmed-meshheading:14596619-Genes, Reporter,
pubmed-meshheading:14596619-Genetic Vectors,
pubmed-meshheading:14596619-Glycosylation,
pubmed-meshheading:14596619-Humans,
pubmed-meshheading:14596619-Mice,
pubmed-meshheading:14596619-Models, Genetic,
pubmed-meshheading:14596619-Models, Molecular,
pubmed-meshheading:14596619-Peptide Fragments,
pubmed-meshheading:14596619-Polycystic Kidney, Autosomal Dominant,
pubmed-meshheading:14596619-Protein Biosynthesis,
pubmed-meshheading:14596619-Protein Structure, Tertiary,
pubmed-meshheading:14596619-Proteins,
pubmed-meshheading:14596619-Recombinant Fusion Proteins,
pubmed-meshheading:14596619-TRPP Cation Channels,
pubmed-meshheading:14596619-Transfection
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| pubmed:year |
2003
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| pubmed:articleTitle |
Transmembrane domain analysis of polycystin-1, the product of the polycystic kidney disease-1 (PKD1) gene: evidence for 11 membrane-spanning domains.
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| pubmed:affiliation |
Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, Kansas 66160-7421, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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