Biochemistry

CK-666 and CK-869 differentially inhibit Arp2/3 iso-complexes

1. LuYan Cao
2. Shaina Huang
3. Angika Basant
4. Miroslav Mladenov
5. Michael Way

Reviewed by Review Commons

Transcriptome-wide analysis of the function of Ded1 in translation preinitiation complex assembly in a reconstituted in vitro system

1. Fujun Zhou
2. Julie M Bocetti
3. Meizhen Hou
4. Daoming Qin
5. Alan G Hinnebusch
6. Jon R Lorsch

• Curated by eLife

  eLife assessment

  This is an important paper as it is the first to use a reconstituted translation system to study competition among mRNAs for the initiation machinery. Understanding the principles of the biochemistry of mRNA competition for initiation factors cannot be achieved without such a system. The authors provide compelling evidence that Ded1 is required for efficient initiation of highly structured mRNAs. The findings are significant and validate the in vitro reconstituted system by recapitulating the effects of in-vivo perturbations of translation initiation by Ded1 mutants.

Reviewed by eLife

Effects of phosphorylation on Drp1 activation by its receptors, actin, and cardiolipin

1. Ao Liu
2. Anna L. Hatch
3. Henry N. Higgs

Reviewed by Review Commons

Fascin-induced bundling protects actin filaments from disassembly by cofilin

1. Jahnavi Chikireddy
2. Léana Lengagne
3. Rémi Le Borgne
4. Catherine Durieu
5. Hugo Wioland
6. Guillaume Romet-Lemonne
7. Antoine Jégou

Reviewed by Review Commons

The Listeria monocytogenes persistence factor ClpL is a potent stand-alone disaggregase

1. Valentin Bohl
2. Nele Merret Hollmann
3. Tobias Melzer
4. Panagiotis Katikaridis
5. Lena Meins
6. Bernd Simon
7. Dirk Flemming
8. Irmgard Sinning
9. Janosch Hennig
10. Axel Mogk

• Curated by eLife

  eLife assessment

  This important manuscript details the characterization of ClpL from L. monocytogenes as an effective and autonomous AAA+ disaggregase that provides enhanced heat resistance to this food-borne pathogen. Supported by compelling evidence, the authors demonstrate that ClpL has DnaK-independent disaggregase activity towards a variety of aggregated model substrates, which is more potent than that observed with the endogenous canonical DnaK/ClpB bi-chaperone system. The work will be of broad interest to microbiologists and biochemists.

Reviewed by eLife

X-ray structure and enzymatic study of a bacterial NADPH oxidase highlight the activation mechanism of eukaryotic NOX

1. Isabelle Petit-Hartlein
2. Annelise Vermot
3. Michel Thepaut
4. Anne-Sophie Humm
5. Florine Dupeux
6. Jerome Dupuy
7. Vincent Chaptal
8. Jose Antonio Marquez
9. Susan ME Smith
10. Franck Fieschi

• Curated by eLife

  eLife assessment

  In this manuscript, the authors investigate the properties of prokaryotic NADPH oxidases (NOX) and discuss the implications for NOX regulation and function. The structure of the S. pneumoniae Nox protein is an important step forward in our understanding of procaryotic NOX enzymes and the characterization and interpretation are convincing. The results will be of interest to structural biologists as well as biochemists focusing on enzymatic functions.

Reviewed by eLife

The C-terminus of CFAP410 forms a tetrameric helical bundle that is essential for its localization to the basal body

1. Alexander Stadler
2. Laryssa V. De Liz
3. Heloisa B. Gabriel
4. Santiago Alonso-Gil
5. Robbie Crickley
6. Katharina Korbula
7. Bojan Žagrović
8. Sue Vaughan
9. Jack D. Sunter
10. Gang Dong

Reviewed by Review Commons

The cryo-EM structure of ASK1 reveals an asymmetric architecture allosterically modulated by TRX1

1. Karolina Honzejkova
2. Dalibor Kosek
3. Veronika Obsilova
4. Tomas Obsil

• Curated by eLife

  eLife assessment

  This important manuscript reports the cryo-EM structure of the ASK1 protein, which is a critical regulator of the MAPKs, JNKs, and p38 MAPKs in diverse cellular stress responses. The evidence of ASK1 interaction with TRX1 is compelling and will eventually allow the discovery of small molecule inhibitors of ASK1 activity.

Reviewed by eLife

Structure-guided mutagenesis of OSCAs reveals differential activation to mechanical stimuli

1. Sebastian Jojoa-Cruz
2. Adrienne E Dubin
3. Wen-Hsin Lee
4. Andrew B Ward

• Curated by eLife

  eLife assessment

  The manuscript seeks to dissect the molecular underpinnings of poke and stretch activation in OSCA channels. While the structural and functional experiments are well done, and the authors present some important data, the reviewers identified weaknesses in experimental design and interpretation that render the data incomplete in supporting some of the main conclusions of the paper. Nevertheless, this work will be of interest to those working in the fields of mechanosensation, sensory biology, and ion channels.

Reviewed by eLife

Structural mechanisms for VMAT2 inhibition by tetrabenazine

1. Michael P Dalton
2. Mary Hongying Cheng
3. Ivet Bahar
4. Jonathan A Coleman

• Curated by eLife

  eLife assessment

  The report presents the cryo-EM structure of human vesicular monoamine transporter 2 (VMAT2) bound to tetrabenazine, a clinical drug. VMAT2 is critical for neurotransmission, and the study constitutes an important milestone in neurotransmitter transport research. The evidence presented in the report is convincing and provides new opportunities for developing improved therapeutic interventions and furthering our understanding of this vital protein's function.

Reviewed by eLife