Linked Life Data

9202139

Source:http://linkedlifedata.com/resource/pubmed/id/9202139

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1997-7-14
pubmed:databankReference
pubmed:abstractText
Inward rectifying potassium (K+(in)) channels play an important role in turgor regulation and ion uptake in higher plants. Here, we report a previously unrecognized feature of these proteins: K+(in) channel C-terminal polypeptides mediate channel protein interactions. Using a C-terminal fragment of potato guard cell K+(in) channel KST1 in a yeast two-hybrid screen two novel putative K+(in) channel proteins (SKT2 and SKT3) were identified by interaction of their C-termini which contained a conserved domain (K(HA)). Interactions were confirmed by Western blot-related assays utilizing K+(in) channel C-termini fused to green fluorescence protein. Although deletion of the K(HA)-domain abolished these interactions, K+(in) currents were still detectable by patch-clamp measurements of insect cells expressing these KST1 mutants, indicating that formation of a functional channel does not depend on this C-terminal domain.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
9
pubmed:volume
409
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
166-70
pubmed:dateRevised
2005-11-17
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Association of plant K+(in) channels is mediated by conserved C-termini and does not affect subunit assembly.
pubmed:affiliation
Max-Planck-Institut für Molekulare Pflanzenphysiologie (MPI-MOPP), Potsdam, Germany.
pubmed:publicationType
Journal Article