| pubmed-article:18649184 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18649184 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:18649184 | lifeskim:mentions | umls-concept:C1418264 | lld:lifeskim |
| pubmed-article:18649184 | lifeskim:mentions | umls-concept:C0599896 | lld:lifeskim |
| pubmed-article:18649184 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:18649184 | pubmed:dateCreated | 2008-7-23 | lld:pubmed |
| pubmed-article:18649184 | pubmed:abstractText | Pannexins are mammalian orthologs of innexins and have a predicted topological folding pattern similar to that of connexins, except they are glycosylated. Rat pannexin 1 is glycosylated at N254 and this residue is important for plasma membrane targeting. Here we demonstrate that cell surface expression levels of the rat pannexin 1 N254Q mutant are rescued by coexpression with the wild-type protein. In paired Xenopus oocytes, the functional effect of this rescue is inconsequential; however, cell surface deglycosylation by PNGase F significantly enhanced functional gap junction formation. In mammalian cells, wild-type oligomers traffic at a slower rate than Myc-or tetracysteine domain-tagged versions, a behavior opposite to that of tagged connexins. The temporal differences of Panx1 trafficking correlate with spatial differences of intracellular localizations induced by Golgi blockage by Brefeldin-A or glycosylation prevention by tunicamycin. Therefore, Panx1 has kinetics and dynamics that make it unique to serve distinct functions separate from connexin-based channels. | lld:pubmed |
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| pubmed-article:18649184 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18649184 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18649184 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:18649184 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18649184 | pubmed:month | May | lld:pubmed |
| pubmed-article:18649184 | pubmed:issn | 1543-5180 | lld:pubmed |
| pubmed-article:18649184 | pubmed:author | pubmed-author:DahlGerhardG | lld:pubmed |
| pubmed-article:18649184 | pubmed:author | pubmed-author:QiuFengF | lld:pubmed |
| pubmed-article:18649184 | pubmed:author | pubmed-author:SosinskyGinaG | lld:pubmed |
| pubmed-article:18649184 | pubmed:author | pubmed-author:BoassaDaniela... | lld:pubmed |
| pubmed-article:18649184 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18649184 | pubmed:volume | 15 | lld:pubmed |
| pubmed-article:18649184 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18649184 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18649184 | pubmed:pagination | 119-32 | lld:pubmed |
| pubmed-article:18649184 | pubmed:dateRevised | 2010-12-17 | lld:pubmed |
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| pubmed-article:18649184 | pubmed:meshHeading | pubmed-meshheading:18649184... | lld:pubmed |
| pubmed-article:18649184 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18649184 | pubmed:articleTitle | Trafficking dynamics of glycosylated pannexin 1 proteins. | lld:pubmed |
| pubmed-article:18649184 | pubmed:affiliation | National Center for Microscopy and Imaging Research, Center for Research in Biological Systems, University of California, San Diego, La Jolla, California 92093-0608, USA. dboassa@gmail.com | lld:pubmed |
| pubmed-article:18649184 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18649184 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:18649184 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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