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TitleStructures of TASK-1 and TASK-3 K2P channels provide insight into their gating and dysfunction in disease.
Journal, issue, pagesStructure, Vol. 33, Issue 1, Page 115-122.e4, Year 2025
Publish dateJan 2, 2025
AuthorsPeter Rory Hall / Thibault Jouen-Tachoire / Marcus Schewe / Peter Proks / Thomas Baukrowitz / Elisabeth P Carpenter / Simon Newstead / Karin E J Rödström / Stephen J Tucker /
PubMed AbstractTASK-1 and TASK-3 are pH-sensitive two-pore domain (K2P/KCNK) K channels. Their functional roles make them promising targets for treatment of multiple disorders including sleep apnea, pain, and ...TASK-1 and TASK-3 are pH-sensitive two-pore domain (K2P/KCNK) K channels. Their functional roles make them promising targets for treatment of multiple disorders including sleep apnea, pain, and atrial fibrillation. Mutations in these channels are also associated with neurodevelopmental and hypertensive disorders. A previous crystal structure of TASK-1 revealed a lower "X-gate" as a hotspot for missense gain-of-function (GoF) mutations associated with DDSA (developmental delay with sleep apnea). However, the mechanisms of gating in TASK channels are still not fully understood. Here, we resolve structures for both human TASK-1 and TASK-3 by cryoelectron microscopy (cryo-EM), as well as a recurrent TASK-3 variant (G236R) associated with KCNK9 imprinting syndrome (KIS) (formerly known as Birk-Barel syndrome). Combined with functional studies of the X-gating mechanism, we provide evidence for how a highly conserved gating mechanism becomes defective in disease, and also provide further insight into the pathway of conformational changes that underlie the pH-dependent inhibition of TASK channel activity.
External linksStructure / PubMed:39637865
MethodsEM (single particle)
Resolution2.48 - 3.32 Å
Structure data

51158

9g9v

EMDB-51158, PDB-9g9v:
Structure of the human two pore domain potassium ion channel TASK-3 (K2P9.1)
Method: EM (single particle) / Resolution: 3.32 Å

51159

9g9w

EMDB-51159, PDB-9g9w:
Structure of the human two pore domain potassium ion channel TASK-3 (K2P9.1) G236R mutant
Method: EM (single particle) / Resolution: 2.48 Å

51160

9g9x

EMDB-51160, PDB-9g9x:
Structure of the human two pore domain potassium ion channel TASK-1 (K2P3.1)
Method: EM (single particle) / Resolution: 3.13 Å

Chemicals

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

ChemComp-K:
Unknown entry

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / K2P / potassium channel / ion channel

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