2017年10月11日 · It is widely recognised that the KCNQ1/KCNE1 (Q1/E1) channel requires phosphatidylinositol-4,5-bisphosphate (PIP2) binding for function. We previously identified a cluster of basic residues in the proximal C-terminus of KCNQ1 that form a …

2006年10月19日 · As illustrated in figure 4C, the WT VSV-tagged KCNE1-KCNQ1 fusion protein, but not the fusion-proteins containing Y111C, L114P and P117L mutations, was readily detected with extracellular anti-VSV antibody. These data demonstrate that the presence of KCNE1 is not sufficient to restore KCNQ1 trafficking to the cell surface.

To better discriminate differences in cellular localization of KCNQ1 between S and AS subjects, we transfected the iPSC-CMs with a plasmid over-expressing wild-type (WT) or mutant KCNQ1 proteins fused with a VSV tag located on the extracellular N-terminal domain. 11 VSV-positive staining of WT KCNQ1 was present in S-, AS-, and CTR-iPSC-CMs but ...

2021年7月20日 · Using recent structures of KCNQ1 and KCNE beta subunits in different states, we present a mechanism by which KCNE1 rotates the VSD relative to the PD and affects the VSD–PD coupling of KCNQ1...

2018年3月7日 · We investigated the impact of 51 KCNQ1 variants with mutations located within the voltage sensor domain (VSD), with an emphasis on elucidating effects on cell surface expression, protein folding, and structure.

2008年8月1日 · KCNQ1 (alias KvLQT1 or Kv7.1) and KCNE1 (alias IsK or minK) co-assemble to form the voltage-activated K + channel responsible for IKs —a major repolarizing current in the human heart—and their dysfunction promotes cardiac arrhythmias. The channel is a component of larger macromolecular complexes containing known and undefined regulatory proteins.

VSV-positive staining of WT KCNQ1 was present in S-, AS-, and CTR-iPSC-CMs but the signal intensity was lower in S-iPSC-CMs compared with AS-and CTR-iPSC-CMs ( Figure 3 A).

2020年2月25日 · KCNQ1 adopts the canonical structural organization of the K V superfamily in which the central homotetrameric pore domain is flanked by four VSDs, each with four transmembrane helical segments (S1-S4).

2020年5月1日 · KCNQ1 presents a unique functional feature when compared to other VGLs, where it can switch from the voltage dependent state to the constitutively active state. The voltage sensor domain (Q1-VSD) can lose its voltage dependence upon association with members of the KCNE family making it constitutively active [35].

2020年1月23日 · KCNQ1, also known as Kv7.1, is a voltage-dependent K + channel that regulates gastric acid secretion, salt and glucose homeostasis, and heart rhythm. Its functional properties are regulated in a tissue-specific manner through co …