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TitleSecondary structure transitions and dual PIP2 binding define cardiac KCNQ1-KCNE1 channel gating.
Journal, issue, pagesCell Res, Vol. 35, Issue 11, Page 887-899, Year 2025
Publish dateOct 2, 2025
AuthorsLing Zhong / Xiaoqing Lin / Xinyu Cheng / Shuangyan Wan / Yaoguang Hua / Weiwei Nan / Bin Hu / Xiangjun Peng / Zihan Zhou / Qiansen Zhang / Huaiyu Yang / Frank Noé / Zhenzhen Yan / Dexiang Jiang / Hangyu Zhang / Fengjiao Liu / Chenxin Xiao / Zhuo Zhou / Yimin Mou / Haijie Yu / Lijuan Ma / Chen Huang / Vincent Kam Wai Wong / Sookja Kim Chung / Bing Shen / Zhi-Hong Jiang / Erwin Neher / Wandi Zhu / Jin Zhang / Panpan Hou /
PubMed AbstractThe KCNQ1 + KCNE1 potassium channel complex produces the slow delayed rectifier current (I) critical for cardiac repolarization. Loss-of-function mutations in KCNQ1 and KCNE1 cause long QT ...The KCNQ1 + KCNE1 potassium channel complex produces the slow delayed rectifier current (I) critical for cardiac repolarization. Loss-of-function mutations in KCNQ1 and KCNE1 cause long QT syndrome (LQTS) types 1 and 5 (LQT1/LQT5), accounting for over one-third of clinical LQTS cases. Despite prior structural work on KCNQ1 and KCNQ1 + KCNE3, the structural basis of KCNQ1 + KCNE1 remains unresolved. Using cryo-electron microscopy and electrophysiology, we determined high-resolution (2.5-3.4 Å) structures of human KCNQ1, and KCNQ1 + KCNE1 in both closed and open states. KCNE1 occupies a pivotal position at the interface of three KCNQ1 subunits, inducing six helix-to-loop transitions in KCNQ1 transmembrane segments. Three of them occur at both ends of the S4-S5 linker, maintaining a loop conformation during I gating, while the other three, in S6 and helix A, undergo dynamic helix-loop transitions during I gating. These structural rearrangements: (1) stabilize the closed pore and the conformation of the intermediate state voltage-sensing domain, thereby determining channel gating, ion permeation, and single-channel conductance; (2) enable a dual-PIP2 modulation mechanism, where one PIP2 occupies the canonical site, while the second PIP2 bridges the S4-S5 linker, KCNE1, and the adjacent S6', stabilizing channel opening; (3) create a fenestration capable of binding compounds specific for KCNQ1 + KCNE1 (e.g., AC-1). Together, these findings reveal a previously unrecognized large-scale secondary structural transition during ion channel gating that fine-tunes I function and provides a foundation for developing targeted LQTS therapy.
External linksCell Res / PubMed:41034624 / PubMed Central
MethodsEM (single particle)
Resolution2.9 - 3.36 Å
Structure data

63935

9u7f

EMDB-63935, PDB-9u7f:
structure of human KCNQ1-KCNE1-CaM complex
Method: EM (single particle) / Resolution: 2.9 Å

64038

9uc8

EMDB-64038, PDB-9uc8:
structure of human KCNQ1-KCNE1-CaM complex with PIP2
Method: EM (single particle) / Resolution: 3.36 Å

Chemicals

ChemComp-PT5:
[(2R)-1-octadecanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phospho / phospholipid*YM

ChemComp-K:
Unknown entry

ChemComp-CA:
Unknown entry

ChemComp-PIO:
[(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / Ion channels

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