2010
DOI: 10.1073/pnas.1010124107
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Ion sensing in the RCK1 domain of BK channels

Abstract: BK-type K + channels are activated by voltage and intracellular Ca 2+ , which is important in modulating muscle contraction, neural transmission, and circadian pacemaker output. Previous studies suggest that the cytosolic domain of BK channels contains two different Ca 2+ binding sites, but the molecular composition of one of the sites is not completely known. Here we report, by systematic mutagenesis studies, the identification of E535 as part of this Ca 2+ binding site. This site is specific for binding to C… Show more

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Cited by 81 publications
(96 citation statements)
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“…These results suggest that changes in FRET signals might originate from Mg 2+ interacting with the gating ring at the high-affinity binding site in the RCK1 domain and/or the Ca 2+ bowl located in the RCK2 domain. To explore these possibilities, we first introduced mutations D362A and D367A, which are known to alter Ca 2+ binding to the RCK1 site (4,31). Because in our previous work we used another mutation for this purpose (M513I), we first verified that in our construct the D362A/D367A 2 E and F), which remained very similar to the unaltered BK667CY constructs ( Fig.…”
Section: +mentioning
confidence: 62%
See 1 more Smart Citation
“…These results suggest that changes in FRET signals might originate from Mg 2+ interacting with the gating ring at the high-affinity binding site in the RCK1 domain and/or the Ca 2+ bowl located in the RCK2 domain. To explore these possibilities, we first introduced mutations D362A and D367A, which are known to alter Ca 2+ binding to the RCK1 site (4,31). Because in our previous work we used another mutation for this purpose (M513I), we first verified that in our construct the D362A/D367A 2 E and F), which remained very similar to the unaltered BK667CY constructs ( Fig.…”
Section: +mentioning
confidence: 62%
“…1 A and B, red circles) (2). The first site identified, named the Ca 2+ bowl (28)(29)(30), is contained within the RCK2 domain (mainly D895 and D897 in the human BK channels), whereas another site was described in the RCK1 domain (including residues D362, D367, and E535) (2,4,31). Additionally, Mg 2+ ions bind specifically, but with low affinity, to a site formed by four amino acids: two from the transmembrane region (D99 and N172) and two located in the RCK1 (E374 and E399) (Fig.…”
Section: +mentioning
confidence: 99%
“…3G), including ∼10 nM at which the Ca 2+ sensors of Slo1 are unoccupied and also 100 μM at which the high-affinity Ca 2+ sensors should be largely saturated with Ca 2+ (20)(21)(22). However, the ΔV 0.5 induced by DHA at 100 μM Ca 2+ was smaller than that at 10 nM (P = 0.03), indicating a potential influence by Ca 2+ .…”
Section: Resultsmentioning
confidence: 93%
“…Subsequently, the side chain of Glu 535 (Fig. 1C, right) was reported to be a part of the RCK1 Ca 2ϩ coordination site together with Asp 367 (31). High-resolution crystal structures of the cytosolic domain have been obtained either with the RCK2 Ca 2ϩ -bowl occupied by Ca 2ϩ (PDB 3 code 3MT5) (32) or in the absence of Ca 2ϩ (PDB code 3NAF) (33).…”
mentioning
confidence: 99%