Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 1
pubmed:dateCreated
2001-1-26
pubmed:abstractText
Cells maintain a negative resting membrane potential through the constitutive activity of background K+ channels. A novel multigene family of such K+ channels has recently been identified. A unique characteristic of these K+ channels is the presence of two homologous, subunit-like domains, each containing a pore-forming region. Sequence co-variations in the GYGD signature motifs of the two pore regions suggested an interaction between neighbouring pore domains. Mutations of the GYGD motif in the rat drk1 (Kv2.1) K+ channel showed that the tyrosine (Y) position was important for K+ selectivity and single channel conductance, whereas the aspartate (D) position was a critical determinant of open state stability. Tandem constructs engineered to mimic the GYGx-GxGD pattern seen in two-domain K+ channels delineated a co-operative intersubunit interaction between the Y and D positions, which determined ion selectivity, conductance and gating. In the bacterial KcsA K+ channel crystal structure, the equivalent aspartate residue (D80) does not directly interact with permeating K+ ions. However, the data presented here show that the D position is able to fine-tune ion selectivity through a functional interaction with the Y position in the neighbouring subunit. These data indicate a physiological basis for the extensive sequence variation seen in the GYGD motifs of two-domain K+ channels. It is suggested that a cell can precisely regulate its resting membrane potential by selectively expressing a complement of two-domain K+ channels.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-10367883, http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-10390363, http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-1279807, http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-1899917, http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-2000494, http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-2000495, http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-2206531, http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-2340178, http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-2388258, http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-2770868, http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-4700900, http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-6259331, http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-6309555, http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-68708, http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-7512171, http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-7546728, http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-7761417, http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-8038378, http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-8605869, http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-8658170, http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-8785286, http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-8789947, http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-8917578, http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-8938713, http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-8994597, http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-9003761, http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-9017198, http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-9037094, http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-9080186, http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-9312005, http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-9462864, http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-9506712, http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-9525859, http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-9579518, http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-9628484, http://linkedlifedata.com/resource/pubmed/commentcorrection/11136855-9851919
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0022-3751
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
530
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
21-33
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:11136855-Amino Acid Motifs, pubmed-meshheading:11136855-Amino Acid Sequence, pubmed-meshheading:11136855-Animals, pubmed-meshheading:11136855-Cell Membrane Permeability, pubmed-meshheading:11136855-Delayed Rectifier Potassium Channels, pubmed-meshheading:11136855-Genetic Engineering, pubmed-meshheading:11136855-Ion Channel Gating, pubmed-meshheading:11136855-Membrane Potentials, pubmed-meshheading:11136855-Molecular Sequence Data, pubmed-meshheading:11136855-Oligopeptides, pubmed-meshheading:11136855-Potassium Channels, pubmed-meshheading:11136855-Potassium Channels, Voltage-Gated, pubmed-meshheading:11136855-RNA, pubmed-meshheading:11136855-Rats, pubmed-meshheading:11136855-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:11136855-Shab Potassium Channels, pubmed-meshheading:11136855-Tyrosine
pubmed:year
2001
pubmed:articleTitle
GYGD pore motifs in neighbouring potassium channel subunits interact to determine ion selectivity.
pubmed:affiliation
Department of Pharmacology and Cancer Biology, Duke University Medical Center, PO Box 3813, Durham, NC 27708, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.