Premium
Comparative proteomic analysis of the ATP ‐sensitive K + channel complex in different tissue types
Author(s) -
Kefaloyianni Eirini,
Lyssand John S.,
Moreno Cesar,
Delaroche Diane,
Hong Miyoun,
Fenyö David,
Mobbs Charles V.,
Neubert Thomas A.,
Coetzee William A.
Publication year - 2013
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201200324
Subject(s) - sulfonylurea receptor , inward rectifier potassium ion channel , microbiology and biotechnology , potassium channel , biology , cytoskeleton , cytoplasm , proteomics , endocytic cycle , biochemistry , subcellular localization , protein subunit , chemistry , cell , receptor , ion channel , biophysics , gene , endocytosis
ATP ‐sensitive K + ( K ATP ) channels are expressed ubiquitously, but have diverse roles in various organs and cells. Their diversity can partly be explained by distinct tissue‐specific compositions of four copies of the pore‐forming inward rectifier potassium channel subunits ( K ir6.1 and/or K ir6.2) and four regulatory sulfonylurea receptor subunits ( SUR 1 and/or SUR 2). Channel function and/or subcellular localization also can be modified by the proteins with which they transiently or permanently interact to generate even more diversity. We performed a quantitative proteomic analysis of K ATP channel complexes in the heart, endothelium, insulin‐secreting min6 cells (pancreatic β‐cell like), and the hypothalamus to identify proteins with which they interact in different tissues. Glycolysis is an overrepresented pathway in identified proteins of the heart, min6 cells, and the endothelium. Proteins with other energy metabolic functions were identified in the hypothalamic samples. These data suggest that the metabolo‐electrical coupling conferred by K ATP channels is conferred partly by proteins with which they interact. A large number of identified cytoskeletal and trafficking proteins suggests endocytic recycling may help control K ATP channel surface density and/or subcellular localization. Overall, our data demonstrate that K ATP channels in different tissues may assemble with proteins having common functions, but that tissue‐specific complex organization also occurs.