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A list by Biophysics Colab

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  8. Allosteric modulation of dimeric GPR3 by ligands in the dimerization interface

    1. Zeming Qiu
    2. Wei Wang
    3. Yingying Nie
    4. Junxiang Lin
    5. Beimeng Zhang
    6. Haonan Xing
    7. Sanduo Zheng

    • Curated by eLife

      eLife Assessment

      Qiu et al. present multiple dimeric structures of GPR3, which reveal the binding mode of the inverse agonist AF64394. The findings provide important insights into the regulation of GPCR3 and potentially other related orphan GPCRs. The authors present convincing evidence of their claims through thoughtful analysis of their cryo-EM structures, mutagenesis, and cell-based assays. This work will be of interest to GPCR investigators, especially those studying the signaling of orphan receptors.

    Reviewed by eLife

    4 evaluationsAppears in 2 listsLatest version Latest activity

  11. β-Arrestin Condensates Regulate G Protein-Coupled Receptor Function

    1. Preston J. Anderson
    2. Peng Xiao
    3. Yani Zhong
    4. Adam Kaakati
    5. Juliana Alfonso-DeSouza
    6. Tianyao Zhang
    7. Chao Zhang
    8. Kevin Yu
    9. Lei Qi
    10. Wei Ding
    11. Samuel Liu
    12. Biswaranjan Pani
    13. Athmika Krishnan
    14. Oscar Chen
    15. Chanpreet Jassal
    16. Joseph Strawn
    17. Jin-Peng Sun
    18. Sudarshan Rajagopal
    Appears in 1 listLatest version

  15. Functionally-Coupled Ion Channels Begin Co-assembling at the Start of Their Synthesis

    1. Roya Pournejati
    2. Jessica M Huang
    3. Michael Ma
    4. Claudia M Moreno
    5. Oscar Vivas

    • Curated by eLife

      eLife Assessment

      This valuable manuscript provides convincing evidence that BK and CaV1.3 channels can co-localize as ensembles early in the biosynthetic pathway, including in the ER and Golgi. The findings, supported by a range of imaging and proximity assays, offer insights into channel organization in both heterologous and endogenous systems. However, mechanistic questions remain unresolved, particularly regarding the specificity of mRNA co-localization, the dynamics of ensemble trafficking, and the functional significance of pre-assembly at the plasma membrane. While the data broadly support the central claims, certain conclusions would benefit from more restrained interpretation and additional clarification to enhance the manuscript's impact and rigor.

    Reviewed by eLife

    3 evaluationsAppears in 2 listsLatest version Latest activity

  16. General Trends in the Calnexin-Dependent Expression and Pharmacological Rescue of Clinical CFTR Variants

    1. Austin Tedman
    2. John A Olson
    3. Minsoo Kim
    4. Catherine Foye
    5. JaNise J Jackson
    6. Eli F McDonald
    7. Andrew G McKee
    8. Karen Noguera
    9. Charles P Kuntz
    10. Jens Meiler
    11. Kathryn Oliver
    12. Lars Plate
    13. Jonathan P Schlebach

    • Curated by eLife

      eLife Assessment

      This important study systematically investigates the effects of calnexin, an endoplasmic reticulum chaperone, on the drug response of approximately 230 disease-causing variants of the cystic fibrosis transmembrane conductance regulator (CFTR) protein. Through deep mutational scanning, interactome profiling, and functional assays, the findings provide convincing evidence that calnexin significantly influences both CFTR expression and the efficacy of corrector drugs in a variant-specific manner. These insights advance our understanding of how cellular quality control machinery shapes the pharmacological responsiveness of CFTR variants, which are broadly relevant for researchers in protein folding and genetic disease therapeutics.

    Reviewed by eLife

    3 evaluationsAppears in 2 listsLatest version Latest activity

  18. Domain coupling in allosteric regulation of SthK measured using time-resolved transition metal ion FRET

    1. Pierce Eggan
    2. Sharona E Gordon
    3. William N Zagotta

    • Curated by eLife

      eLife Assessment

      This valuable study employs transition-metal FRET (tmFRET) and time-correlated single-photon counting to investigate allosteric conformational changes in both isolated cyclic nucleotide-binding domains (CNBDs) and full-length bacterial CNG channels, demonstrating that transmembrane domains stabilize CNBDs in their active state. By comparing isolated CNBD constructs with full-length channels, the authors reveal how allosteric networks couple domain movements to gating energetics, providing insights into ion channel regulation mechanisms. The rigorous methodology and compelling quantitative analysis establish a framework for applying tmFRET to study conformational dynamics in diverse protein systems.

    Reviewed by eLife

    9 evaluationsAppears in 2 listsLatest version Latest activity
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