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TitleMechanisms of KCNQ1 gating modulation by KCNE1/3 for cell-specific function.
Journal, issue, pagesCell Res, Vol. 35, Issue 11, Page 876-886, Year 2025
Publish dateJul 31, 2025
AuthorsChenxi Cui / Lu Zhao / Ali A Kermani / Shuzong Du / Tanadet Pipatpolkai / Meiqin Jiang / Sagar Chittori / Yong Zi Tan / Jingyi Shi / Lucie Delemotte / Jianmin Cui / Ji Sun /
PubMed AbstractKCNQ1 potassium channels are essential for physiological processes such as cardiac rhythm and intestinal chloride secretion. KCNE family subunits (KCNE1-5) associate with KCNQ1, conferring distinct ...KCNQ1 potassium channels are essential for physiological processes such as cardiac rhythm and intestinal chloride secretion. KCNE family subunits (KCNE1-5) associate with KCNQ1, conferring distinct properties across various tissues. KCNQ1 activation requires membrane depolarization and phosphatidylinositol 4,5-bisphosphate (PIP2) whose cellular levels are controlled by Gαq-coupled GPCR activation. While modulation of KCNQ1's voltage-dependent activation by KCNE1/3 is well-characterized, their effects on PIP2-dependent gating of KCNQ1 via GPCR signaling remain less understood. Here we resolved structures of KCNQ1-KCNE1 and reassessed the reported KCNQ1-KCNE3 structures with and without PIP2. We revealed that KCNQ1-KCNE1/3 complexes feature two PIP2-binding sites, with KCNE1/3 contributing to a previously overlooked, uncharacterized site involving residues critical for coupling voltage sensor and pore domains. Via this site, KCNE1 and KCNE3 distinctly modulate the PIP2-dependent gating, in addition to the voltage sensitivity, of KCNQ1. Consequently, KCNE3 converts KCNQ1 into a voltage-insensitive PIP2-gated channel governed by GPCR signaling to maintain ion homeostasis in non-excitable cells. KCNE1, by significantly enhancing KCNQ1's PIP2 affinity and resistance to GPCR regulation, forms predominantly voltage-gated channels with KCNQ1 for conducting the slow-delayed rectifier current in excitable cardiac cells. Our study highlights how KCNE1/3 modulates KCNQ1 gating in different cellular contexts, providing insights into tissue-specifically targeting multi-functional channels.
External linksCell Res / PubMed:40745202 / PubMed Central
MethodsEM (single particle)
Resolution2.7 - 3.9 Å
Structure data

64997

9vec

EMDB-64997, PDB-9vec:
structure of human KCNQ1-KCNE1-CaM complex
Method: EM (single particle) / Resolution: 2.7 Å

65008

9vei

EMDB-65008, PDB-9vei:
structure of human KCNQ1-KCNE1-CaM complex with PIP2
Method: EM (single particle) / Resolution: 3.9 Å

65013

9ven

EMDB-65013, PDB-9ven:
structure of human KCNQ1-CaM-PIP2 complex with bent conformation
Method: EM (single particle) / Resolution: 3.8 Å

65014

9veo

EMDB-65014, PDB-9veo:
structure of human KCNQ1-CaM-PIP2 complex with straight conformation
Method: EM (single particle) / Resolution: 3.7 Å

PDB-9wd8:
structure of human KCNQ1-KCNE3-CaM complex with two PIP2
Method: ELECTRON MICROSCOPY / Resolution: 3.9 Å

Chemicals

ChemComp-CA:
Unknown entry

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

PDB-1bbg:
RAGWEED POLLEN ALLERGEN FROM AMBROSIA TRIFIDA V, NMR, MINIMIZED AVERAGE STRUCTURE

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / potassium channel complex

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