Linked Life Data

21439353

Source:http://linkedlifedata.com/resource/pubmed/id/21439353

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2011-5-23
pubmed:abstractText
In the present study, we characterized a STAS-domain amino acid mutation of SLC26A9 having a significant impact on ion transport. We focused on the sole conserved L- leucine residue of the STAS domain identified among SLC26 members. We therefore characterized the L683P mutation of SLC26A9 in Xenopus oocytes by monitoring the protein functional expression (two-electrode technique for voltage-clamp analysis) and its presence at the cell membrane (surface protein biotinylation technique). This mutation was found to reduce Cl(-) transport through SLC26A9 as well as the positive interaction exerted by SLC26A9 on CFTR ion transport activity. The origin of this effect is discussed in the light of the presence of the SLC26A9-L683P mutant at the plasma membrane.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-3002
pubmed:author
pubmed:copyrightInfo
Copyright © 2011 Elsevier B.V. All rights reserved.
pubmed:issnType
Print
pubmed:volume
1810
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
577-83
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Characterization of the L683P mutation of SLC26A9 in Xenopus oocytes.
pubmed:affiliation
Universite de Nice, Nice, Cedex 2, France.
pubmed:publicationType
Journal Article