Linked Life Data

21594802

Source:http://linkedlifedata.com/resource/pubmed/id/21594802

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2011-5-19
pubmed:abstractText
The cystic fibrosis transmembrane conductance regulator (CFTR) is the gene product mutated in cystic fibrosis, a common lethal genetic disease characterized by abnormal electrolyte transport across epithelia. CFTR functions as an ATP-gated, phosphorylation-regulated Cl- channel that mediates agonist-stimulated apical membrane epithelial Cl- and bicarbonate secretion and also regulates a variety of other transport proteins and cellular processes. CFTR belongs to the ATP-binding cassette (ABC) transporter superfamily. Its presumed architecture consists of two transmembrane domain regions that form the channel pore, two nucleotide-binding domains that bind and hydrolyze ATP, and a unique regulatory (R) domain that contains numerous protein kinase A (PKA) and protein kinase C (PKC) phosphorylation sites. Other kinases have also been shown more recently to phosphorylate and regulate CFTR activity. This chapter describes strategies and methods for studying the phosphorylation of CFTR both in vitro and whole-cell systems.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1940-6029
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
741
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
471-88
pubmed:dateRevised
2011-9-22
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
CFTR regulation by phosphorylation.
pubmed:affiliation
Renal-Electrolyte Division, School of Medicine, University of Pittsburgh, Pittsburgh, PA 15261, USA. rra11@pitt.edu
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural