Biophysics

Membrane curvature governs the distribution of Piezo1 in live cells

1. Shilong Yang
2. Xinwen Miao
3. Steven Arnold
4. Boxuan Li
5. Alan T. Ly
6. Huan Wang
7. Matthew Wang
8. Xiangfu Guo
9. Medha M. Pathak
10. Wenting Zhao
11. Charles D. Cox
12. Zheng Shi

• Curated by Biophysics Colab

  Endorsement statement (6 December 2022)

  The preprint by Yang et al. asks how the shape of the membrane influences the localization of mechanosensitive Piezo channels. The authors use a creative approach involving methods that distort the plasma membrane by generating blebs and artificial filopodia. They convincingly show that curvature of the lipid environment influences Piezo1 localization, such that increased curvature causes channel depletion, and that application of the chemical modulator Yoda1 is sufficient to allow channels to enter filopodia. The study provides support for a provocative “flattening model” of Yoda1 action, and should inspire future studies by researchers interested in mechanosensitive channels and membrane curvature.

  (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

Architecture of the chikungunya virus replication organelle

1. Timothée Laurent
2. Pravin Kumar
3. Susanne Liese
4. Farnaz Zare
5. Mattias Jonasson
6. Andreas Carlson
7. Lars-Anders Carlson

Reviewed by Review Commons

Ranking Peptide Binders by Affinity with AlphaFold**

1. Liwei Chang
2. Alberto Perez

Reviewed by Arcadia Science

Versatile patterns in the actin cortex of motile cells: Self-organized pulses can coexist with macropinocytic ring-shaped waves

1. Arik Yochelis
2. Sven Flemming
3. Carsten Beta

• Curated by eLife

  Evaluation Summary:

  Individual cells may act in response to stimuli or in a self-organized fashion. The relative weight of these two modes determines in the end to which degree cells or rather organs/organisms carry function. This study reports an example of very complex self-organization of actin waves as the coexistence of slowly moving broad waves of high F-actin concentration and rapidly propagating planar F-actin pulses. The paper is interesting for everybody interested in conceptual questions like signalling versus self-organization, in cellular morpho-dynamics and theory of dynamic patterns.

  (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. The reviewers remained anonymous to the authors.)

Reviewed by eLife

Dilated cardiomyopathy mutation E525K in human beta-cardiac myosin stabilizes the interacting-heads motif and super-relaxed state of myosin

1. David V Rasicci
2. Prince Tiwari
3. Skylar ML Bodt
4. Rohini Desetty
5. Fredrik R Sadler
6. Sivaraj Sivaramakrishnan
7. Roger Craig
8. Christopher M Yengo

• Curated by eLife

  Evaluation Summary:

  This study seeks to develop the use of a FRET-based sensor for the formation of the folded 'interacting heads motif' structure for cardiac myosin, which is thought by some to represent a super-relaxed state with lower basal ATPase activity. This study offers some evidence that there is a relationship between the super-relaxed state and the 'interacting heads motif' structure, and that a specific dilated cardiomyopathy mutant in this myosin stabilizes the 'interacting heads motif' conformation. This paper will be of interest to muscle and cardiovascular biologists as it provides important insights into the correlation of structural and functional states of motor proteins in the context of cardiac muscle. The data qualitatively support this correlation and suggest a new mode of action of disease-causing mutations that lead to impaired contractile function.

  (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 agreed to share their name with the authors.)

Reviewed by eLife

In situ single particle classification reveals distinct 60S maturation intermediates in cells

1. Bronwyn A Lucas
2. Kexin Zhang
3. Sarah Loerch
4. Nikolaus Grigorieff

• Curated by eLife

  Evaluation Summary:

  This paper explores the use of 2D high-resolution template-matching (2DTM) to locate and discriminate highly similar macromolecules within cryo-EM images of focused ion beam-milled cells. It demonstrates that differences in the 2DTM signal-to-noise ratios for located targets against multiple search templates can effectively segregate a mixed population of similar structures, as well as present a formal analysis strategy for probabilistic assignment of species within the mixed population. Because the identification of distinct structural states of macromolecular complexes inside the cell is a fundamental problem in 3D visual proteomics, this paper will be of broad interest to both structural and cell biologists.

  (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 and Reviewer #3 agreed to share their name with the authors.)

Reviewed by eLife

Trapped Pore Waters in the Open Proton Channel H _V 1

1. Danila Boytsov
2. Stefania Brescia
3. Gustavo Chaves
4. Sabina Koefler
5. Christof Hannesschlaeger
6. Christine Siligan
7. Nikolaus Goessweiner‐Mohr
8. Boris Musset
9. Peter Pohl

Reviewed by Review Commons

Vein fate determined by flow-based but time-delayed integration of network architecture

1. Sophie Marbach
2. Noah Ziethen
3. Leonie Bastin
4. Felix K Bäuerle
5. Karen Alim

• Curated by eLife

  Evaluation Summary:

  Fluid flows in networks are ubiquitous, and in many living systems the networks are not static but instead can rearrange over time. Using vascular networks formed by the slime mold Physarum polycephalum, Marcbach et al. demonstrate that there is a time delay between the change in the flow and the change in the network geometry. They present a mechanical model of vein-radius adaptation leveraging the negative normal stress response of the actin cytoskeletal network lining the vein walls. More generally, the authors make use of the unique advantage of this simple model vascular system to connect the local shear rate to the network reorganisation and how it depends on its architecture. There are features to their work that are new to the literature and that can be impactful in advancing the field.

  (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. The reviewers remained anonymous to the authors.)

Reviewed by eLife

Activation mechanism of small heat shock protein HSPB5 revealed by disease-associated mutants

1. Christopher N. Woods
2. Maria K. Janowska
3. Lindsey D. Ulmer
4. Jasleen Kaur Sidhu
5. Natalie L. Stone
6. Ellie I. James
7. Miklos Guttman
8. Matthew F. Bush
9. Rachel E. Klevit

• Curated by eLife

  Evaluation Summary:

  The human small heat shock protein (sHSP) HSPB5 is an ATP-independent molecular chaperone involved in maintaining protein homeostasis. This manuscript reports on dynamic interactions between the disordered N-terminal region (NTR) and the structured alpha-crystallin domain (ACD) in HSPB5 oligomers. The authors show that two mutations, associated with early cataract and myopathy development, disrupt the interaction of the ACD core with the unfolded NTRs and generate a much more dynamic and hyperactive version of the chaperone. These findings will be of interest to colleagues studying molecular chaperones and their implications for disease in humans.

  (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. The reviewers remained anonymous to the authors.)

Reviewed by eLife

Multivalency, autoinhibition, and protein disorder in the regulation of interactions of dynein intermediate chain with dynactin and the nuclear distribution protein

1. Kayla A Jara
2. Nikolaus M Loening
3. Patrick N Reardon
4. Zhen Yu
5. Prajna Woonnimani
6. Coban Brooks
7. Cat H Vesely
8. Elisar J Barbar

• Curated by eLife

  Evaluation Summary:

  The identification of an autoinhibitory mechanism of the dynein intermediate chain provides an important contribution to our understanding of dynein assembly and illustrates the plethora of regulatory mechanisms attainable by intrinsically disordered proteins. This paper provides insight into the autoinhibited inactive state of dynein as well as the activation mechanism. A wide range of biophysical approaches is used, providing a very nice example of how these diverse technologies can be applied in concert and in a synergistic manner to study an important question in the realm of "unstructured biology".

  (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. The reviewers remained anonymous to the authors.)

Reviewed by eLife