Biochemistry

Genome-wide screen reveals Rab12 GTPase as a critical activator of Parkinson’s disease-linked LRRK2 kinase

1. Herschel S Dhekne
2. Francesca Tonelli
3. Wondwossen M Yeshaw
4. Claire Y Chiang
5. Charles Limouse
6. Ebsy Jaimon
7. Elena Purlyte
8. Dario R Alessi
9. Suzanne R Pfeffer

• Curated by eLife

  eLife assessment

  Dhekne et al report a novel pathway for activation of the multi-domain LRRK2 protein kinase by Rab12 GTPase. LRRK2, which is mutated in Parkinson's Disease phosphorylates a subset of Rab proteins involved in intracellular trafficking, and Parkinson's disease-linked mutations increase this phosphorylation. This work adds an important new layer of understanding of this highly complex pathway by revealing that LRRK2's binding to Rab12 enhances its ability to phosphorylate Rab10. This conclusion is supported by compelling evidence from a wide array of rigorous approaches.

Reviewed by eLife

Structural insights into the organization and channel properties of human Pannexin isoforms 1 and 3

1. Nazia Hussain
2. Ashish Apotikar
3. Shabareesh Pidathala
4. Sourajit Mukherjee
5. Ananth Prasad Burada
6. Sujit Kumar Sikdar
7. Vinothkumar R. Kutti
8. Aravind Penmatsa

Reviewed by Biophysics Colab

ChIP-MS reveals the local chromatin composition by label-free quantitative proteomics

1. Wai Khang Yong
2. Grishma Rane
3. Nurkaiyisah Zaal Anuar
4. Xiaoman Shao
5. Chai Yeen Goh
6. Vartika Khanchandani
7. Vivian L. S. Kuan
8. Maya Jeitany
9. H. Phillip Koeffler
10. Lih-Wen Deng
11. Takaomi Sanda
12. Dennis Kappei

Reviewed by Review Commons

Conformational regulation and target-myristoyl switch of calcineurin B homologous protein 3

1. Florian Becker
2. Simon Fuchs
3. Lukas Refisch
4. Friedel Drepper
5. Wolfgang Bildl
6. Uwe Schulte
7. Shuo Liang
8. Jonas Immanuel Heinicke
9. Sierra C Hansen
10. Clemens Kreutz
11. Bettina Warscheid
12. Bernd Fakler
13. Evgeny V Mymrikov
14. Carola Hunte

• Curated by eLife

  eLife assessment

  In this work, the authors provide important mechanistic insights into how the intracellular effector protein Calcineurin B homologous protein 3 (CHP3) can be regulated in a calcium-independent manner to expose its lipid binding site. Compelling evidence demonstrates a binding partner protein (NHE1) triggers a conformation change and exposure of the myristoyl group in CHP3 resulting in membrane association. This provides mechanistic insight into the signalling mechanisms achieved by CHP3 in a target-dependent manner, which will be of broad scientific interest.

Reviewed by eLife

Purification and biochemical characterization of the DNA binding domain of the nitrogenase transcriptional activator NifA from Gluconacetobacter diazotrophicus

1. Heidi G. Standke
2. Lois Kim
3. Cedric P. Owens

Reviewed by Arcadia Science

Changes in Active Site Loop Conformation Relate to the Transition toward a Novel Enzymatic Activity

1. Pauline Jacquet
2. Raphaël Billot
3. Amir Shimon
4. Nathan Hoekstra
5. Céline Bergonzi
6. Anthony Jenks
7. Eric Chabrière
8. David Daudé
9. Mikael H. Elias

Reviewed by Arcadia Science

Structural and biochemical characterisation of the N-Carbamoyl-β-Alanine Amidohydrolase from Rhizobium radiobacter MDC 8606

1. Ani Paloyan
2. Armen Sargsyan
3. Mariam D. Karapetyan
4. Artur Hambardzumyan
5. Sergey Kocharov
6. Henry Panosyan
7. Karine Dyukova
8. Marina Kinosyan
9. Anna Krüger
10. Cecilia Piergentili
11. Will A. Stanley
12. Arnaud Baslé
13. Jon Marles-Wright
14. Garabed Antranikian

Reviewed by Arcadia Science

Utilizing a nanobody recruitment approach for assessing serine palmitoyltransferase activity in ER sub-compartments of yeast

1. Bianca M. Esch
2. Stefan Walter
3. Oliver Schmidt
4. Florian Fröhlich

Reviewed by Review Commons

Structure of the connexin-43 gap junction channel in a putative closed state

1. Chao Qi
2. Silvia Acosta Gutierrez
3. Pia Lavriha
4. Alaa Othman
5. Diego Lopez-Pigozzi
6. Erva Bayraktar
7. Dina Schuster
8. Paola Picotti
9. Nicola Zamboni
10. Mario Bortolozzi
11. Francesco Luigi Gervasio
12. Volodymyr M Korkhov

• Curated by eLife

  eLife assessment

  Gap junctions, formed from connexins, are important in cell communication, allowing ions and small molecules to move directly between cells. By determining the Cryo EM structure of the structure of connexin 43 in a putative closed state involving lipids, the study makes an important contribution to the development of a mechanistic model for connexin activation. The connexin 43 structure is solid and its presentation will appeal to the channel and membrane protein communities.

Reviewed by eLife

Allosteric activation or inhibition of PI3Kγ mediated through conformational changes in the p110γ helical domain

1. Noah J Harris
2. Meredith L Jenkins
3. Sung-Eun Nam
4. Manoj K Rathinaswamy
5. Matthew AH Parson
6. Harish Ranga-Prasad
7. Udit Dalwadi
8. Brandon E Moeller
9. Eleanor Sheeky
10. Scott D Hansen
11. Calvin K Yip
12. John E Burke

• Curated by eLife

  eLife assessment

  This study presents fundamental new insight into the regulatory apparatus of PI3Kγ, a kinase in signaling pathways that control the immune response and cancer. A suite of biophysical and biochemical approaches provide convincing evidence for new sites of allosteric control over enzyme activity. The rigorous findings provide structure and dynamic information that may be exploited in efforts to control PI3Kγ activity in a therapeutic setting.

Reviewed by eLife