Biophysics

Microtubules under mechanical pressure can breach dense actin networks

1. Matthieu Gélin
2. Alexandre Schaeffer
3. Jérémie Gaillard
4. Christophe Guérin
5. Benoit Vianay
6. Magali Orhant-Prioux
7. Marcus Braun
8. Christophe Leterrier
9. Laurent Blanchoin
10. Manuel Théry

Reviewed by Review Commons

Diffusive mediator feedback explains the health-to-disease transition of skin inflammation

1. Maki Sudo
2. Koichi Fujimoto

Reviewed by Review Commons

Constitutive activity of ionotropic glutamate receptors via hydrophobic substitutions in the ligand-binding domain

1. Sandra Seljeset
2. Oksana Sintsova
3. Yuhong Wang
4. Hassan Y. Harb
5. Timothy Lynagh

• Curated by Biophysics Colab

  Evaluation statement (8 March 2024)

  Seljeset et al. investigate the mechanism by which NMDA receptors are activated by co-agonists glutamate and glycine. By mutating residue Asp732 in the glycine-binding site, they generate receptors activated by glutamate, and not glycine, but inhibited by glycine antagonists. Conventional and unnatural amino acid mutagenesis reveals that Asp732 interacts with nearby residues to influence channel gating as well as ligand binding. Furthermore, a homomeric receptor from Trichoplax adhaerens, which has a tyrosine in the homologous position, displays constitutive activity that becomes glycine-dependent when the tyrosine is mutated to aspartate. The study is valuable because it reveals the importance of position 732 for controlling ligand potency and channel activity in glutamate receptors, which should lead to a better understanding of how these receptors are primed for channel opening.

  Biophysics Colab recommends this study to scientists interested in the structure and function of glutamate receptors

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

  • Rigorous methodology
  • Transparent reporting
  • Appropriate interpretation

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

Reviewed by Biophysics Colab

Cryo-EM structure of Slo1 with the auxiliary γ1 subunit suggests mechanism of depolarization-independent activation

1. Milena Redhardt
2. Stefan Raunser
3. Tobias Raisch

Reviewed by Review Commons