1. Structure of an open KATP channel reveals tandem PIP2 binding sites mediating the Kir6.2 and SUR1 regulatory interface

    This article has 5 authors:
    1. Camden M. Driggers
    2. Yi-Ying Kuo
    3. Phillip Zhu
    4. Assmaa ElSheikh
    5. Show-Ling Shyng
    This article has been curated by 1 group:
    • Curated by Biophysics Colab

      Evaluation statement (10 January 2024)

      Driggers et al. is an elegant study that reports the structure of an open KATP channel complex formed from the Q52R diabetes mutation of the pore-forming subunit Kir 6.2, the sulfonylurea receptor (SUR1), and long-chain phosphatidylinositol 4,5-bisphosphate (PIP2) – a key lipid that stabilizes the open state of the channel and regulates inhibition by intracellular ATP. The structure reveals one PIP2 site related to that seen in other Kir channels as well as a second unanticipated one where the lipid snuggles into the interface between Kir6.2 and a region of SUR1 previously implicated in promoting the open state of KATP. This important finding helps to explain how PIP2 exerts such a profound regulatory influence on KATP.

      Biophysics Colab considers this to be a convincing study and recommends it to scientists working on KATP and other membrane proteins regulated by PIP2.

      (This evaluation 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

    This article has 3 evaluationsAppears in 3 listsLatest version Latest activity
  2. Acyl-CoA thioesterase-2 facilitates β-oxidation in glycolytic skeletal muscle in a lipid supply dependent manner

    This article has 13 authors:
    1. Carmen Bekeova
    2. Ji In Han
    3. Heli Xu
    4. Evan Kerr
    5. Brittney Blackburne
    6. Shannon C. Lynch
    7. Clementina Mesaros
    8. Marta Murgia
    9. Rajanikanth Vadigepalli
    10. Joris Beld
    11. Roberta Leonardi
    12. Nathaniel W. Snyder
    13. Erin L. Seifert
    This article has been curated by 1 group:
    • Curated by eLife

      eLife assessment

      This study presents new data highlighting the importance of appropriate coenzyme A handling in the mitochondria for maintaining appropriate energy production capacity. Several findings regarding the role of a key metabolic enzyme in how skeletal muscle cells use different substrates for energy production are valuable and supported by solid evidence, but there are concerns whether the data support the conclusion that ACOT2 regulates mitochondrial matrix acyl-CoA levels in white skeletal muscle to facilitate fatty acid oxidation β-oxidation.

    Reviewed by eLife

    This article has 4 evaluationsAppears in 1 listLatest version Latest activity
  3. A bioactive peptide from the pearl has dual roles in resisting SARS-CoV-2 infection and its complications

    This article has 9 authors:
    1. Xiaojun Liu
    2. Yayu Wang
    3. Zehui Yin
    4. Qin Wang
    5. Xinjiani Chen
    6. Bailei Li
    7. Liping Yao
    8. Zhen Zhang
    9. Rongqing Zhang

    Reviewed by PREreview

    This article has 1 evaluationAppears in 1 listLatest version Latest activity
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