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TitleStructure and electromechanical coupling of a voltage-gated Na/H exchanger.
Journal, issue, pagesNature, Vol. 623, Issue 7985, Page 193-201, Year 2023
Publish dateOct 25, 2023
AuthorsHyunku Yeo / Ved Mehta / Ashutosh Gulati / David Drew /
PubMed AbstractVoltage-sensing domains control the activation of voltage-gated ion channels, with a few exceptions. One such exception is the sperm-specific Na/H exchanger SLC9C1, which is the only known ...Voltage-sensing domains control the activation of voltage-gated ion channels, with a few exceptions. One such exception is the sperm-specific Na/H exchanger SLC9C1, which is the only known transporter to be regulated by voltage-sensing domains. After hyperpolarization of sperm flagella, SLC9C1 becomes active, causing pH alkalinization and CatSper Ca channel activation, which drives chemotaxis. SLC9C1 activation is further regulated by cAMP, which is produced by soluble adenyl cyclase (sAC). SLC9C1 is therefore an essential component of the pH-sAC-cAMP signalling pathway in metazoa, required for sperm motility and fertilization. Despite its importance, the molecular basis of SLC9C1 voltage activation is unclear. Here we report cryo-electron microscopy (cryo-EM) structures of sea urchin SLC9C1 in detergent and nanodiscs. We show that the voltage-sensing domains are positioned in an unusual configuration, sandwiching each side of the SLC9C1 homodimer. The S4 segment is very long, 90 Å in length, and connects the voltage-sensing domains to the cytoplasmic cyclic-nucleotide-binding domains. The S4 segment is in the up configuration-the inactive state of SLC9C1. Consistently, although a negatively charged cavity is accessible for Na to bind to the ion-transporting domains of SLC9C1, an intracellular helix connected to S4 restricts their movement. On the basis of the differences in the cryo-EM structure of SLC9C1 in the presence of cAMP, we propose that, upon hyperpolarization, the S4 segment moves down, removing this constriction and enabling Na/H exchange.
External linksNature / PubMed:37880360 / PubMed Central
MethodsEM (single particle)
Resolution3.08 - 3.68 Å
Structure data

17182

8otq

EMDB-17182, PDB-8otq:
Cryo-EM structure of Strongylocentrotus purpuratus sperm-specific Na+/H+ exchanger SLC9C1 in GDN
Method: EM (single particle) / Resolution: 3.22 Å

17185

8otw

EMDB-17185, PDB-8otw:
Cryo-EM structure of Strongylocentrotus purpuratus SLC9C1 in presence of cAMP
Method: EM (single particle) / Resolution: 3.68 Å

17186

8otx

EMDB-17186, PDB-8otx:
Cryo-EM structure of Strongylocentrotus purpuratus sperm-specific Na+/H+ exchanger SLC9C1 in nanodisc
Method: EM (single particle) / Resolution: 3.08 Å

Chemicals

ChemComp-CPL:
1-PALMITOYL-2-LINOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE / phospholipid*YM

ChemComp-PLM:
PALMITIC ACID

ChemComp-3PH:
1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE

ChemComp-HOH:
WATER

Source
  • strongylocentrotus purpuratus (purple sea urchin)
KeywordsTRANSPORT PROTEIN / VSD / CNBD / Transporter / Voltage sensor / exchanger / sperm motility / cAMP binding

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