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. 2024 Jul 1;156(7):e202413612.
doi: 10.1085/jgp.202413612. Epub 2024 Jun 11.

The S1 helix is a VIP in VSP

Affiliations

The S1 helix is a VIP in VSP

Ben Short. J Gen Physiol. .

Abstract

JGP study (Rayaprolu et al. https://doi.org/10.1085/jgp.202313467) shows that hydrophobic residues in the S1 transmembrane domain modulate the voltage sensor movements and enzymatic activity of voltage-sensing phosphatase.

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Figures

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Vamseedhar Rayaprolu and Susy Kohout.
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The VSD of voltage-sensing phosphatase can dimerize with the S1 (orange) and S4 (green) helices facing each other at the subunit interface. Rayaprolu et al. (2) reveal that hydrophobic resides (blue) in the S1 helix modulate both the voltage-sensitive movement of the S4 helix and the enzyme’s catalytic activity, suggesting that they play a key role in mediating communication between the protein’s voltage-sensing and phosphatase domains.

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  • doi: 10.1085/jgp.202313467

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References

    1. Islas, L.D. 2016. Channels. 10.1080/19336950.2016.1141842 - DOI
    1. Rayaprolu V., et al. . 2024. J. Gen. Physiol. 10.1085/jgp.202313467 - DOI
    1. Li, Q., et al. . 2014. Nat. Struct. Mol. Biol. 10.1038/nsmb.2768 - DOI - PMC - PubMed
    1. Rayaprolu, V., et al. . 2018. J. Gen. Physiol. 10.1085/jgp.201812064 - DOI - PMC - PubMed

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