Table 1. KCNMA1 mutation effects on BK channel function
MutationBK current propertiesMechanism
D434GIncreased currentG-V shift to hyperpolarized potentials, increased open probability, faster activation, slower deactivation, increased Ca2+ sensitivity (Du et al., 2005; Díez-Sampedro et al., 2006; Wang et al., 2009; Yang et al., 2010; Plante et al., 2019)
N995/999/1053SIncreased currentG-V shift to hyperpolarized potentials, increased open probability, faster activation, slower deactivation, Ca2+-independent mechanism (Li et al., 2018; Plante et al., 2019)
S351Y, G356R, G375R, N449fs*, I663VNo currentNot determined (Liang et al., 2019)
C413Y, P805LReduced currentG-V shift to depolarized potentials, decreased expression (P805L; Liang et al., 2019)
D984NReduced currentNot determined (Liang et al., 2019)
G354SReduced currentSlower activation (Carvalho-de-Souza et al., 2016)
R458Ter, Y676Lfs*7Not determinedPutative truncations (Tabarki et al., 2016; Yeşil et al., 2018)
K518N, E656A, N1195SNo current differenceLi et al., 2018
E884KNot determinedZhang et al., 2015

Dark gray, GOF mutations; light gray, LOF mutations; no shading, VUS. Full descriptions of experimental investigations for mutant channel properties are contained in Supplemental text. The N995S/N999S/N1053S mutation is reported in the literature using three different reference sequence numbering schemes but constitutes the same residue substitution (Figure 1). In this review, this mutation will be referred to by the numbering scheme in the original publication for the data being discussed.