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A list by Biophysics Colab

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  4. Membrane curvature sensing and symmetry breaking of the M2 proton channel from Influenza A

    1. James Lincoff
    2. Cole VM Helsell
    3. Frank V Marcoline
    4. Andrew M Natale
    5. Michael Grabe

    • Curated by eLife

      Evaluation Summary:

      The authors combined atomistic simulations and continuum mechanics models to probe how structural features of the M2 channel impact the local membrane properties and stability of the channel in membranes of different curvatures. The insights gained in this work can potentially lead to novel strategies that screen for drug molecules that stabilize fission-incompetent conformations of the M2 channel. The multi-scale computational approach will find utility to many problems in membrane reshaping.

      (This preprint has been reviewed by eLife. We include the public reviews from the reviewers here; the authors also receive private feedback with suggested changes to the manuscript. Reviewer #2 and Reviewer #3 agreed to share their name with the authors.)

    Reviewed by eLife

    5 evaluationsAppears in 2 listsLatest version Latest activity

  9. Activation-pathway transitions in human voltage-gated proton channels revealed by a non-canonical fluorescent amino acid

    1. Esteban Suárez-Delgado
    2. Maru Orozco-Contreras
    3. Gisela E Rangel-Yescas
    4. Leon D Islas

    • Curated by Biophysics Colab

      Endorsement statement (22 December 2022)

      The preprint by Suarez-Delgado et al. explores the mechanisms by which the Hv1 voltage-activated proton channel is dependent upon transmembrane voltage and pH by incorporating the small fluorescent non-canonical amino acid Anap into the S4 helix and monitoring its fluorescence. Anap spectra suggest the fluorophore resides in an aqueous environment and moves relative to a quenching aromatic residue (F150) in the S2 helix upon depolarization. Two kinetically distinct components of fluorescence change support the presence of at least three conformational states in the activation pathway of Hv1. Measurements using different pH gradients suggest that S4 movement and channel opening are similarly affected by pH gradients. This is the first study to incorporate Anap into Hv1, and provide a rigorous and thorough characterization of how the fluorophore can be used to explore mechanisms of gating and regulation, paving the way for future studies. The work will be of interest to physiologists and biophysicists investigating membrane protein mechanisms using non-canonical fluorescent amino acids.

      (This endorsement by Biophysics Colab refers to version 2 of this preprint, which has been revised in response to peer review of version 1.)

    Reviewed by Biophysics Colab

    3 evaluationsAppears in 4 listsLatest version Latest activity

  14. PIEZO1 discriminates mechanical stimuli

    1. Alper D. Ozkan
    2. Tharaka D. Wijerathne
    3. Tina Gettas
    4. Jérôme J. Lacroix
    Appears in 1 listLatest version

  18. Inhibited KdpFABC transitions into an E1 off-cycle state

    1. Jakob M Silberberg
    2. Charlott Stock
    3. Lisa Hielkema
    4. Robin A Corey
    5. Jan Rheinberger
    6. Dorith Wunnicke
    7. Victor RA Dubach
    8. Phillip J Stansfeld
    9. Inga Hänelt
    10. Cristina Paulino

    • Curated by eLife

      Evaluation Summary:

      KdpFABC is a bacterial potassium uptake transporter made up of a channel-like subunit (KdpA) and a P-type ATPase (KdpB). When potassium levels are low (< 2 mM), the transporter actively and selectively uptakes potassium, but must be switched off again to prevent excessive K+ accumulation. Although structures of KdpFABC have been determined before, the structural basis for inhibition by phosphorylation is unknown. Here, the authors have determined the structure of KdpABC in an arrested (off-state) that is in a distinct conformation from previously determined P-type ATPase structures. More detailed structural comparisons are needed to more convincingly show this, however, and the protein required to inhibit KdpABC by phosphorylation remains unknown. This paper will be of interest to researchers in the microbiology and transporter communities.

      (This preprint has been reviewed by eLife. We include the public reviews from the reviewers here; the authors also receive private feedback with suggested changes to the manuscript. Reviewer #1 agreed to share their name with the authors.)

    Reviewed by eLife

    5 evaluationsAppears in 2 listsLatest version Latest activity
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