Show simple item record

dc.contributor.author Lengyel Miklós
dc.contributor.author Czirják Gábor
dc.contributor.author Enyedi Péter
dc.date.accessioned 2017-01-19T12:34:41Z
dc.date.available 2017-01-19T12:34:41Z
dc.date.issued 2016
dc.identifier.citation pagination=13649-13661; journalVolume=291; journalIssueNumber=26; journalTitle=JOURNAL OF BIOLOGICAL CHEMISTRY;
dc.identifier.uri http://repo.lib.semmelweis.hu//handle/123456789/3412
dc.identifier.uri doi:10.1074/jbc.M116.719039
dc.description.abstract Two-pore domain (K2P) potassium channels are the major molecular correlates of the background (leak) K+ current in a wide variety of cell types. They generally play a key role in setting the resting membrane potential and regulate the response of excitable cells to various stimuli. K2P channels usually function as homodimers and only a few examples of heteromerization have been previously reported. Expression of the TREK (TWIK-related K+ channel) subfamily members of K2P channels often overlaps in neurons and in other excitable cells. Here we demonstrate that heterologous coexpression of TREK-1 and TREK-2 subunits results in the formation of functional heterodimers. Taking advantage of a tandem construct (in which the two different subunits were linked together to enforce heterodimerization) we characterized the biophysical and pharmacological properties of the TREK-1/TREK-2 current. The heteromer was inhibited by extracellular acidification and by spadin similarly to TREK-1, while its ruthenium red sensitivity was intermediate between TREK-1 and TREK-2 homodimers. The heterodimer has also been distinguished from the homodimers by its unique single channel conductance. Assembly of the two different subunits was confirmed by coimmunoprecipitation of epitope tagged TREK-1 and TREK-2 subunits, coexpressed in Xenopus oocytes. Formation of TREK-1/TREK-2 channels was also demonstrated in native dorsal root ganglion neurons indicating that heterodimerization may provide greater diversity of leak K+ conductances also in native tissues.
dc.relation.ispartof urn:issn:0021-9258
dc.title Formation of Functional Heterodimers by TREK-1 and TREK-2 Two-pore Domain Potassium Channel Subunits.
dc.type Journal Article
dc.date.updated 2016-05-30T08:07:57Z
dc.language.rfc3066 en
dc.identifier.mtmt 3071322
dc.identifier.pubmed 27129242
dc.contributor.department SE/AOK/I/Élettani Intézet
dc.contributor.institution Semmelweis Egyetem


Files in this item

This file is available only from Semmelweis network

View/Open

This item appears in the following Collection(s)

Show simple item record

Search DSpace


Advanced Search

Browse

My Account