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  1. ATP-release pannexin channels are gated by lysophospholipids

    This article has 12 authors:
    1. Erik Henze
    2. Russell N Burkhardt
    3. Bennett William Fox
    4. Tyler J Schwertfeger
    5. Eric Gelsleichter
    6. Kevin Michalski
    7. Lydia Kramer
    8. Margret Lenfest
    9. Jordyn M Boesch
    10. Hening Lin
    11. Frank C Schroeder
    12. Toshimitsu Kawate
    This article has been curated by 2 groups:
    • Curated by eLife

      eLife Assessment

      Pannexin (Panx) channels are a family of poorly understood large-pore channels that mediate the release of substrates like ATP from cells, yet the physiological stimuli that activate these channels remain poorly understood. The study by Henze et al. describes an elegant approach wherein activity-guided fractionation of mouse liver led to the discovery that lysophospholipids (LPCs) activate Panx1 and Panx2 channels expressed in cells or reconstituted into liposomes. The authors provide compelling evidence that LPC-mediated activation of Panx1 is involved in joint pain and that Panx1 channels are required for the established effects of LPC on inflammasome activation in monocytes, suggesting that Panx channels play a role in inflammatory pathways. Overall, this important study reports a previously unanticipated mechanism wherein LPCs directly activate Panx channels. The work will be of interest to scientists investigating phospholipids, Panx channels, purinergic signalling and inflammation.

      [Editors' note: this paper was reviewed and curated by Biophysics Colab]

    • Curated by Biophysics Colab

      Evaluation Statement (30 January 2025)

      Kay and Aminzare discuss a claim made in a prior publication that macromolecular condensation acts as a water buffering mechanism in cells to compensate for the effects of osmotic shock. The authors argue that, although such a buffer could temporarily maintain a transmembrane osmolality differential, this differential would drive water across the membrane to reach a steady-state in which osmolality within the cell equals osmolality outside the cell. Using the well-established pump-leak model for osmotic water transport, they further show that the timescale at which a water buffer could maintain a modest 10% osmolality differential across the membrane is at most one minute for a typical animal cell.

      Biophysics Colab recommends this study to researchers working on membrane transport, intracellular water buffering, and condensate biology.

      Biophysics Colab has evaluated this study as one that meets the following criteria:

      • Rigorous methodology
      • Transparent reporting
      • Appropriate interpretation

      (This evaluation refers to version 3 of this preprint, which has been revised in response to peer review of versions 1 and 2.)

    Reviewed by eLife, Biophysics Colab

    This article has 12 evaluationsAppears in 4 listsLatest version Latest activity