Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2003-1-22
pubmed:abstractText
Phosphoinositides are critical regulators of ion channel and transporter activity. Defects in interactions of inwardly rectifying potassium (Kir) channels with phosphoinositides lead to disease. ATP-sensitive K(+) channels (K(ATP)) are unique among Kir channels in that they serve as metabolic sensors, inhibited by ATP while stimulated by long-chain (LC) acyl-CoA. Here we show that K(ATP) are the least specific Kir channels in their activation by phosphoinositides and we demonstrate that LC acyl-CoA activation of these channels depends on their low phosphoinositide specificity. We provide a systematic characterization of phosphoinositide specificity of the entire Kir channel family expressed in Xenopus oocytes and identify molecular determinants of such specificity. We show that mutations in the Kir2.1 channel decreasing phosphoinositide specificity allow activation by LC acyl-CoA. Our data demonstrate that differences in phosphoinositide specificity determine the modulation of Kir channel activity by distinct regulatory lipids.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/12525701-10197533, http://linkedlifedata.com/resource/pubmed/commentcorrection/12525701-10491749, http://linkedlifedata.com/resource/pubmed/commentcorrection/12525701-10527927, http://linkedlifedata.com/resource/pubmed/commentcorrection/12525701-10545132, http://linkedlifedata.com/resource/pubmed/commentcorrection/12525701-10559906, http://linkedlifedata.com/resource/pubmed/commentcorrection/12525701-10593888, http://linkedlifedata.com/resource/pubmed/commentcorrection/12525701-10966860, http://linkedlifedata.com/resource/pubmed/commentcorrection/12525701-11055989, http://linkedlifedata.com/resource/pubmed/commentcorrection/12525701-11306691, http://linkedlifedata.com/resource/pubmed/commentcorrection/12525701-11349001, http://linkedlifedata.com/resource/pubmed/commentcorrection/12525701-11665643, http://linkedlifedata.com/resource/pubmed/commentcorrection/12525701-11734659, http://linkedlifedata.com/resource/pubmed/commentcorrection/12525701-12086641, http://linkedlifedata.com/resource/pubmed/commentcorrection/12525701-12198096, http://linkedlifedata.com/resource/pubmed/commentcorrection/12525701-12408817, http://linkedlifedata.com/resource/pubmed/commentcorrection/12525701-1419000, http://linkedlifedata.com/resource/pubmed/commentcorrection/12525701-1438581, http://linkedlifedata.com/resource/pubmed/commentcorrection/12525701-8631866, http://linkedlifedata.com/resource/pubmed/commentcorrection/12525701-8688080, http://linkedlifedata.com/resource/pubmed/commentcorrection/12525701-8868049, http://linkedlifedata.com/resource/pubmed/commentcorrection/12525701-9038137, http://linkedlifedata.com/resource/pubmed/commentcorrection/12525701-9074760, http://linkedlifedata.com/resource/pubmed/commentcorrection/12525701-9144288, http://linkedlifedata.com/resource/pubmed/commentcorrection/12525701-9395492, http://linkedlifedata.com/resource/pubmed/commentcorrection/12525701-9448327, http://linkedlifedata.com/resource/pubmed/commentcorrection/12525701-9486652, http://linkedlifedata.com/resource/pubmed/commentcorrection/12525701-9558481, http://linkedlifedata.com/resource/pubmed/commentcorrection/12525701-9756869, http://linkedlifedata.com/resource/pubmed/commentcorrection/12525701-9759495, http://linkedlifedata.com/resource/pubmed/commentcorrection/12525701-9804554
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
100
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
745-50
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Specificity of activation by phosphoinositides determines lipid regulation of Kir channels.
pubmed:affiliation
Department of Physiology and Biophysics, Mount Sinai School of Medicine of New York University, New York, NY 10029, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't