Biochemistry

Structural basis for the Rad6 activation by the Bre1 N-terminal domain

1. Meng Shi
2. Jiaqi Zhao
3. Simin Zhang
4. Wei Huang
5. Mengfei Li
6. Xue Bai
7. Wenxue Zhang
8. Kai Zhang
9. Xuefeng Chen
10. Song Xiang

• Curated by eLife

  eLife assessment

  This fundamental study presents a crystal structure of two proteins catalyzing histone H2B ubiquitination. Findings from the structural study are further validated by mutagenesis and functional assays. This is a well-executed study providing useful information to the field.

Reviewed by eLife

Cryo-EM structures of mitochondrial respiratory complex I from Drosophila melanogaster

1. Ahmed-Noor A Agip
2. Injae Chung
3. Alvaro Sanchez-Martinez
4. Alexander J Whitworth
5. Judy Hirst

• Curated by eLife

  eLife assessment

  This important study advances our understanding of respiratory complex I. The authors present convincing structural data for the enzyme from Drosophila melanogaster although the interpretation of conformational states is still not conclusively settled. This work will be of interest to researchers studying respiratory enzymes, the evolution of respiration, and mitochondrial diseases.

Reviewed by eLife

Nucleotide binding is the critical regulator of ABCG2 conformational transitions

1. Zsuzsanna Gyöngy
2. Gábor Mocsár
3. Éva Hegedűs
4. Thomas Stockner
5. Zsuzsanna Ritter
6. László Homolya
7. Anita Schamberger
8. Tamás I Orbán
9. Judit Remenyik
10. Gergely Szakacs
11. Katalin Goda

• Curated by eLife

  eLife assessment

  The ABC transporter ABCG2 extrudes chemotherapy reagents and other xenobiotics from a number of different tissues. How ABCG2 operates at the molecular level has been largely derived from structures and dynamics carried out in non-physiological environments. The paper presents convincing cell-based evidence describing the relationship between structural changes of ABCG2 and substrate binding using flow cytometry, confocal microscopy, and fluorescence-correlation spectroscopy methods. Both the mechanistic conclusions and methodology employed offer important insights, which will be of general interest to the biochemistry and transport biology communities.

Reviewed by eLife

Inhibition of the proton-activated chloride channel PAC by PIP2

1. Ljubica Mihaljević
2. Zheng Ruan
3. James Osei-Owusu
4. Wei Lü
5. Zhaozhu Qiu

• Curated by eLife

  eLife assessment

  Combining electrophysiology, site-directed mutagenesis, lipid pharmacology, and single particle cryo-electron microscopy, this study provides solid evidence identifying a site on the extracellular half of the transmembrane domain of Proton-Activated Chloride (PAC) channels that could be occupied by PIP2 and related lipids to promote channel desensitization. These findings are important because pharmacological information for these biologically relevant ion channels is absent.

Reviewed by eLife

Simultaneous membrane and RNA binding by tick-borne encephalitis virus capsid protein

1. Lauri Ilmari Aurelius Pulkkinen
2. Sarah Victoria Barrass
3. Marie Lindgren
4. Hudson Pace
5. Anna K. Överby
6. Maria Anastasina
7. Marta Bally
8. Richard Lundmark
9. Sarah Jane Butcher

Reviewed by Review Commons

Mechanism of Ca2+ transport by ferroportin

1. Jiemin Shen
2. Azaan Saalim Wilbon
3. Ming Zhou
4. Yaping Pan

• Curated by eLife

  eLife assessment

  This study makes an important contribution to the function of the iron transporter Ferroportin (Fpn). By using a combination of proteoliposome assays, mutagenesis and structural studies by cryo EM, the authors are able to demonstrate that the H+-driven transporter for Fe2+-efflux is also capable of passive Ca2+ influx. The evidence supporting the conclusions is convincing, but the rate of Ca2+ influx and the physiological relevance of Ca2+ entry is yet to be established. The work will be of broad interest to cell biologists and biochemists.

Reviewed by eLife

Structures of ferroportin in complex with its specific inhibitor vamifeport

1. Elena Farah Lehmann
2. Márton Liziczai
3. Katarzyna Drożdżyk
4. Patrick Altermatt
5. Cassiano Langini
6. Vania Manolova
7. Hanna Sundstrom
8. Franz Dürrenberger
9. Raimund Dutzler
10. Cristina Manatschal

• Curated by eLife

  eLife assessment

  This important study reports cryo-EM structures of human ferroportin (FPN), a protein essential for iron transport in humans. This manuscript will be of interest to researchers studying membrane transport mechanisms as well as to those interested in drug design. The structures detail interactions between FPN and the small-molecule inhibitor vamifeport, which is currently in clinical trials for sickle cell disease, and ta new (occluded) protein conformation that is stabilized by a sybody (a nanobody selected from a synthetic library) is identified. Evidence for the mechanism of inhibition by vamifeport is convincing, but evidence for the physiological relevance of the occluded conformation is still incomplete.

Reviewed by eLife

Drosophila SUMM4 complex couples insulator function and DNA replication control

1. Evgeniya N Andreyeva
2. Alexander V Emelyanov
3. Markus Nevil
4. Lu Sun
5. Elena Vershilova
6. Christina A Hill
7. Michael-C Keogh
8. Robert J Duronio
9. Arthur I Skoultchi
10. Dmitry V Fyodorov

• Curated by eLife

  eLife assessment

  This paper will be of interest to those studying DNA replication in the context of chromatin and development. This important study uncovers a new interaction partner for the chromatin protein SuUR and tries to understand how this complex (SUMM4) functions to control under-replication in polytene chromosomes. While the experiments are of high quality and carefully controlled, the data currently do not fully support all the conclusions, particularly as they relate to conclusions about DNA replication timing.

Reviewed by eLife

How do Vampires Suck Blood?

1. Meng Gou
2. Xuyuan Duan
3. Jun Li
4. Yaocen Wang
5. Qingwei Li
6. Yue Pang
7. Yonghui Dong

Reviewed by Arcadia Science

Regulation of branched versus linear Arp2/3‐generated actin filaments

1. Luyan Cao
2. Foad Ghasemi
3. Michael Way
4. Antoine Jégou
5. Guillaume Romet‐Lemonne

Reviewed by Review Commons