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TitleStructural and functional basis of mechanosensitive TMEM63 channelopathies.
Journal, issue, pagesNeuron, Year 2025
Publish dateJun 2, 2025
AuthorsWang Zheng / Augustus J Lowry / Harper E Smith / Jiale Xie / Shaun Rawson / Chen Wang / Jin Ou / Marcos Sotomayor / Tian-Min Fu / Huanghe Yang / Jeffrey R Holt /
PubMed AbstractTMEM63A, -B, and -C constitute a mammalian family of mechanosensitive ion channels that are mutated in neurodevelopmental disorders. The molecular mechanisms underlying TMEM63 activation by force and ...TMEM63A, -B, and -C constitute a mammalian family of mechanosensitive ion channels that are mutated in neurodevelopmental disorders. The molecular mechanisms underlying TMEM63 activation by force and the impact of disease-associated mutations have not been clarified. Here, we elucidate the structural and functional bases of a prevalent TMEM63B mutation p.V44M. We first found that TMEM63B p.V44M and the homologous TMEM63A p.V53M are gain-of-function mutations that do not enhance channel activity but instead evoke constitutive lipid scramblase activity. We then solved TMEM63A p.V53M mutant structures in both closed and lipid-open states, which revealed major rearrangements of pore-lining helices, creating a lateral cleft across the membrane. Simulation studies revealed lipid scrambling through this cleft. The structural rearrangements were triggered by disruption of a surface-proximal hydrophobic latch, a putative force-sensing module that includes a cluster of disease mutation sites. Our findings provide mechanistic insight into TMEM63 channelopathies and suggest a possible force-sensing mechanism.
External linksNeuron / PubMed:40480214
MethodsEM (single particle)
Resolution2.95 - 3.65 Å
Structure data

49158

9n93

EMDB-49158, PDB-9n93:
Human TMEM63A mutant V53M lipid-open state
Method: EM (single particle) / Resolution: 2.95 Å

49160

9n95

EMDB-49160, PDB-9n95:
Human TMEM63A mutant V53M closed state
Method: EM (single particle) / Resolution: 3.65 Å

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / Ion channel / Mechanosensitive / lipid scramblase

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