ABCC8 p.Met1Ala
Predicted by SNAP2: | A: N (72%), C: N (87%), D: D (53%), E: N (53%), F: N (78%), G: N (61%), H: N (66%), I: N (97%), K: N (61%), L: N (97%), N: N (66%), P: N (57%), Q: N (78%), R: N (61%), S: N (78%), T: N (78%), V: N (97%), W: N (61%), Y: N (72%), |
Predicted by PROVEAN: | A: N, C: N, D: N, E: N, F: N, G: N, H: N, I: N, K: N, L: N, N: N, P: N, Q: N, R: N, S: N, T: N, V: N, W: N, Y: N, |
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[hide] Domain organization of the ATP-sensitive potassium... J Biol Chem. 2013 Feb 8;288(6):4378-88. doi: 10.1074/jbc.M112.388629. Epub 2012 Dec 6. Wang S, Makhina EN, Masia R, Hyrc KL, Formanack ML, Nichols CG
Domain organization of the ATP-sensitive potassium channel complex examined by fluorescence resonance energy transfer.
J Biol Chem. 2013 Feb 8;288(6):4378-88. doi: 10.1074/jbc.M112.388629. Epub 2012 Dec 6., [PMID:23223337]
Abstract [show]
K(ATP) channels link cell metabolism to excitability in many cells. They are formed as tetramers of Kir6.2 subunits, each associated with a SUR1 subunit. We used mutant GFP-based FRET to assess domain organization in channel complexes. Full-length Kir6.2 subunits were linked to YFP or cyan fluorescent protein (CFP) at N or C termini, and all such constructs, including double-tagged YFP-Kir6.2-CFP (Y6.2C), formed functional K(ATP) channels. In intact COSm6 cells, background emission of YFP excited by 430-nm light was approximately 6%, but the Y6.2C construct expressed alone exhibited an apparent FRET efficiency of approximately 25%, confirmed by trypsin digestion, with or without SUR1 co-expression. Similar FRET efficiency was detected in mixtures of CFP- and YFP-tagged full-length Kir6.2 subunits and transmembrane domain only constructs, when tagged at the C termini but not at the N termini. The FRET-reported Kir6.2 tetramer domain organization was qualitatively consistent with Kir channel crystal structures: C termini and M2 domains are centrally located relative to N termini and M1 domains, respectively. Additional FRET analyses were performed on cells in which tagged full-length Kir6.2 and tagged SUR1 constructs were co-expressed. These analyses further revealed that 1) NBD1 of SUR1 is closer to the C terminus of Kir6.2 than to the N terminus; 2) the Kir6.2 cytoplasmic domain is not essential for complexation with SUR1; and 3) the N-terminal half of SUR1 can complex with itself in the absence of either the C-terminal half or Kir6.2.
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No. Sentence Comment
43 nSUR1 includes TMD0-L0-TMD1-NBD1 (residues Met-1 to Ala-1000), and cSUR1 includes TMD2-NBD2 (residues Cys-1001 to Lys-1580).
X
ABCC8 p.Met1Ala 23223337:43:43
status: NEW