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TitleA Na pump with reduced stoichiometry is up-regulated by brine shrimp in extreme salinities.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 120, Issue 52, Page e2313999120, Year 2023
Publish dateDec 26, 2023
AuthorsPablo Artigas / Dylan J Meyer / Victoria C Young / Kerri Spontarelli / Jessica Eastman / Evan Strandquist / Huan Rui / Benoît Roux / Matthew A Birk / Hanayo Nakanishi / Kazuhiro Abe / Craig Gatto /
PubMed AbstractBrine shrimp () are the only animals to thrive at sodium concentrations above 4 M. Salt excretion is powered by the Na,K-ATPase (NKA), a heterodimeric (αβ) pump that usually exports 3Na in exchange ...Brine shrimp () are the only animals to thrive at sodium concentrations above 4 M. Salt excretion is powered by the Na,K-ATPase (NKA), a heterodimeric (αβ) pump that usually exports 3Na in exchange for 2 K per hydrolyzed ATP. express several NKA catalytic α-subunit subtypes. High-salinity adaptation increases abundance of α2, an isoform that contains two lysines (Lys308 and Lys758 in transmembrane segments TM4 and TM5, respectively) at positions where canonical NKAs have asparagines ( α1's Asn333 and Asn785). Using de novo transcriptome assembly and qPCR, we found that express two salinity-independent canonical α subunits (α1 and α3), as well as two β variants, in addition to the salinity-controlled α2. These β subunits permitted heterologous expression of the α2 pump and determination of its CryoEM structure in a closed, ion-free conformation, showing Lys758 residing within the ion-binding cavity. We used electrophysiology to characterize the function of α2 pumps and compared it to that of α1 (and its α2-mimicking single- and double-lysine substitutions). The double substitution N333K/N785K confers α2-like characteristics to α1, and mutant cycle analysis reveals energetic coupling between these two residues, illustrating how α2's Lys308 helps to maintain high affinity for external K when Lys758 occupies an ion-binding site. By measuring uptake under voltage clamp of the K-congener Rb, we prove that double-lysine-substituted pumps transport 2Na and 1 K per catalytic cycle. Our results show how the two lysines contribute to generate a pump with reduced stoichiometry allowing to maintain steeper Na gradients in hypersaline environments.
External linksProc Natl Acad Sci U S A / PubMed:38079564 / PubMed Central
MethodsEM (single particle)
Resolution3.44 Å
Structure data

36794

8k1l

EMDB-36794, PDB-8k1l:
Cryo-EM structure of Na+,K+-ATPase alpha2 from Artemia salina in cation-free E2P form
Method: EM (single particle) / Resolution: 3.44 Å

Chemicals

ChemComp-ALF:
TETRAFLUOROALUMINATE ION

Source
  • artemia salina (crustacean)
KeywordsTRANSPORT PROTEIN / P-type ATPase / sodium pump / membrane protein / transporter

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