Linked Life Data

21223469

Source:http://linkedlifedata.com/resource/pubmed/id/21223469

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2011-3-25
pubmed:abstractText
The cystic fibrosis transmembrane conductance regulator (CFTR) interacts with multiple N-ethylmaleimide sensitive factor attachment protein (SNARE) molecules largely via its N-terminal cytoplasmic domain. The earliest known among these SNAREs are the cognate Q-SNARE pair of Syntaxin 1A (STX1A) and SNAP23 on the plasma membrane. These SNAREs affect CFTR chloride channel gating. CFTR exocytosis/recycling in intestinal epithelial cells is dependent on another SNARE located in the apical plasma membrane, STX3. Members of the STX8/STX7/vesicle transport through interaction with t-SNAREs homolog 1b/VAMP8 SNARE complex, which function in early to late endosome/lysosome traffic, are all known to interact with CFTR. Two SNAREs, STX6 and STX16 that function at the trans-Golgi network (TGN), have now been revealed as members of the CFTR SNARE interactome. We summarize here the SNAREs that interact with CFTR and discuss the roles of these SNAREs in the intracellular trafficking of CFTR and CFTR-associated pathophysiology.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1600-0854
pubmed:author
pubmed:copyrightInfo
© 2011 John Wiley & Sons A/S.
pubmed:issnType
Electronic
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
364-71
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
The cystic fibrosis transmembrane conductance regulator's expanding SNARE interactome.
pubmed:affiliation
Department of Biochemistry, Yong Loo Lin School of Medicine, National University Health System, National University of Singapore, 8 Medical Drive, Singapore 117597, Singapore. bor_luen_tang@nuhs.edu.sg
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't