Novel Chemical Tools to Study Ion Channel Biology (Advances in Experimental Medicine and Biology)

(sharon) #1

74 M. Priest and F. Bezanilla


Osteen JD, Barro-Soria R, Robey S, Sampson KJ, Kass RS, Larsson HP (2012) Allosteric gating
mechanism underlies the flexible gating of KCNQ1 potassium channels. Proc Natl Acad Sci
U S A 109:7103–7108
Pantazis A, Olcese R (2012) Relative transmembrane segment rearrangements during BK chan-
nel activation resolved by structurally assigned fluorophore–quencher pairing. J Gen Physiol
140:207–218
Pantazis A, Gudzenko V, Savalli N, Sigg D, Olcese R (2010) Operation of the voltage sensor of
a human voltage- and Ca2+-activated K+ channel. Proc Natl Acad Sci U S A 107:4459–4464
Passero CJ, Okumura S, Carattino MD (2009) Conformational changes associated with proton-
dependent gating of ASIC1a. J Biol Chem 284:36473–36481
Pathak M, Kurtz L, Tombola F, Isacoff E (2005) The cooperative voltage sensor motion that gates
a potassium channel. J Gen Physiol 125:57–69
Pathak MM, Yarov-Yarovoy V, Agarwal G, Roux B, Barth P, Kohout S, Tombola F, Isacoff EY
(2007) Closing In on the resting state of the Shaker K+ channel. Neuron 56:124–140
Peters CJ, Vaid M, Horne AJ, Fedida D, Accili EA (2009) The molecular basis for the actions of
KVβ1.2 on the opening and closing of the KV1.2 delayed rectifier channel. Channels 3:314–
322
Pless SA, Lynch JW (2009a) Ligand-specific conformational changes in the α1 glycine receptor
ligand-binding domain. J Biol Chem 284:15847–15856
Pless SA, Lynch JW (2009b) Magnitude of a conformational change in the glycine receptor β1–β 2
loop is correlated with agonist efficacy. J Biol Chem 284:27370–27376
Pless SA, Lynch JW (2009c) Distinct conformational changes in activated agonist-bound and
agonist-free glycine receptor subunits. J Neurochem 108:1585–1594
Pless SA, Dibas MI, Lester HA, Lynch JW (2007) Conformational variability of the glycine recep-
tor M2 domain in response to activation by different agonists. J Biol Chem 282:36057–36067
Posson DJ, Ge P, Miller C, Bezanilla F, Selvin PR (2005) Small vertical movement of a K+ chan-
nel voltage sensor measured with luminescence energy transfer. Nature 436:848–851
Puljung MC, Zagotta WN (2011) Labeling of Specific cysteines in proteins using reversible metal
protection. Biophys J 100:2513–2521
Qiu F, Rebolledo S, Gonzalez C, Larsson HP (2013) Subunit interactions during cooperative open-
ing of voltage-gated proton channels. Neuron 77:288–298
Raghuraman H, Islam SM, Mukherjee S, Roux B, Perozo E (2014) Dynamics transitions at
the outer vestibule of the KcsA potassium channel during gating. Proc Natl Acad Sci U S A
111:1831–1836
Richards R, Dempski RE (2011) Examining the conformational dynamics of membrane proteins in
situ with site-directed fluorescence labeling. J Vis Exp 51:2627. doi:10.3791/2627
Rudokas MW, Varga Z, Schubert AR, Asaro AB, Silva JR (2014) The Xenopus oocyte cut-open
vaseline gap voltage-clamp technique with fluorometry. J Vis Exp 85. doi:10.3791/51040
Ruscic KJ, Miceli F, Villalba-Galea CA, Dai H, Mishina Y, Bezanilla F, Goldstein SAN (2013) IKs
channels open slowly because KCNE1 accessory subunits slow the movement of S4 voltage
sensors in KCNQ1 pore-forming subunits. Proc Natl Acad Sci U S A 110:E559–E566
Savalli N, Kondratiev A, Toro L, Olcese R (2006) Voltage-dependent conformational changes in
human Ca2+- and voltage-activated K+ channel, revealed by voltage-clamp fluorometry. Proc
Natl Acad Sci U S A 103:12619–12624
Savalli N, Kondratiev A, Quintana SB de, Toro L, Olcese R (2007) Modes of operation of the
BKCa channel β2 subunit. J Gen Physiol 130:117–131
Savalli N, Pantazis A, Yusifov T, Sigg D, Olcese R (2012) The contribution of RCK domains to
human BK channel allosteric activation. J Biol Chem 287:21741–21750
Schönherr R, Mannuzzu LM, Isacoff EY, Heinemann SH (2002) Conformational switch between
slow and fast gating modes: allosteric regulation of voltage sensor mobility in the EAG K+
channel. Neuron 35:935–949
Semenova NP, Abarca-Heidemann K, Loranc E, Rothberg BS (2009) Bimane fluorescence
scanning suggests secondary structure near the S3-S4 linker of BK channels. J Biol Chem
284:10684–10693

Free download pdf