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TitleStructural insights into AQP3 channel closure upon pH and redox changes reveal an autoregulatory molecular mechanism.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 10997, Year 2025
Publish dateDec 22, 2025
AuthorsPeng Huang / Raminta Venskutonytė / Carter J Wilson / Sara Bsharat / Rashmi B Prasad / Pontus Gourdon / Isabella Artner / Bert L de Groot / Karin Lindkvist-Petersson /
PubMed AbstractRegulation of intracellular levels of reactive oxygen species (ROS) remains poorly understood. Aquaporin 3 (AQP3) facilitates the membrane transport of hydrogen peroxide (HO), a key ROS signaling ...Regulation of intracellular levels of reactive oxygen species (ROS) remains poorly understood. Aquaporin 3 (AQP3) facilitates the membrane transport of hydrogen peroxide (HO), a key ROS signaling molecule. Here we elucidate the molecular mechanism of AQP3 and show that its regulatory properties are both pH dependent and autoregulated by HO. Using single particle cryo-electron microscopy, we present open and closed conformations of human AQP3. At pH 8.0, the channel adopts an open state, while acidic pH or exposure to HO promotes closure via a large conformational rearrangement of extracellular loop E. These findings reveal a mechanism for autoregulation of HO transport and establish AQP3 as a key modulator of redox homeostasis in human pancreatic β-cells.
External linksNat Commun / PubMed:41429774 / PubMed Central
MethodsEM (single particle)
Resolution3.0 - 3.2 Å
Structure data

53343

9qsx

EMDB-53343, PDB-9qsx:
Cryo-EM structure of aquaporin 3 at pH 8.0
Method: EM (single particle) / Resolution: 3.2 Å

53344

9qsy

EMDB-53344, PDB-9qsy:
Cryo-EM structure of aquaporin 3 at pH 5.5
Method: EM (single particle) / Resolution: 3.2 Å

53345

9qsz

EMDB-53345, PDB-9qsz:
Cryo-EM structure of aquaporin 3 at pH 8.0 with hydrogen peroxide
Method: EM (single particle) / Resolution: 3.0 Å

Chemicals

ChemComp-GOL:
GLYCEROL

PDB-1h8k:
A-SPECTRIN SH3 DOMAIN A11V, V23L, M25V, V53I, V58L MUTANT

ChemComp-HOH:
WATER

ChemComp-PEO:
HYDROGEN PEROXIDE

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / glycerol channel / hydrogen peroxide transport / tetramer

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