Cell Biology

PERK-ATAD3A interaction protects mitochondrial proteins synthesis during ER stress

1. Daniel T. Hughes
2. Karinder K. Brar
3. Jordan L. Morris
4. Kelly Subramanian
5. Shivaani Krishna
6. Fei Gao
7. Lara-Sophie Rieder
8. Joshua Freeman
9. Heather L. Smith
10. Rebekkah Jukes-Jones
11. Jodi Nunnari
12. Julien Prudent
13. Adrian J. Butcher
14. Giovanna R. Mallucci

Reviewed by ASAPbio crowd review

TTBK2 controls cilium stability through actin and the centrosomal compartment

1. Abraham Nguyen
2. Sarah C. Goetz

Reviewed by Review Commons

The Drosophila mitotic spindle orientation machinery requires activation, not just localization

1. Kathryn E Neville
2. Tara M Finegan
3. Nicholas Lowe
4. Philip M Bellomio
5. Daxiang Na
6. Dan T Bergstralh

Reviewed by Review Commons

A bifunctional kinase–phosphatase module balances mitotic checkpoint strength and kinetochore–microtubule attachment stability

1. Andrea Corno
2. Marilia H Cordeiro
3. Lindsey A Allan
4. Qian‐Wei Lim
5. Elena Harrington
6. Richard J Smith
7. Adrian T Saurin

Reviewed by Review Commons

Peroxiredoxin 5 regulates osteogenic differentiation through interaction with hnRNPK during bone regeneration

1. Eunjin Cho
2. Xiangguo Che
3. Mary Jasmin Ang
4. Seongmin Cheon
5. Jinkyung Lee
6. Kwang Soo Kim
7. Chang Hoon Lee
8. Sang-Yeop Lee
9. Hee-Young Yang
10. Changjong Moon
11. Chungoo Park
12. Je-Yong Choi
13. Tae-Hoon Lee

• Curated by eLife

  Evaluation Summary:

  The research presented in this manuscript is focused on testing the role of peroxiredoxin (Prdx5) and heterogeneous nuclear ribonucleoprotein K (hnRNPK) in bone biology and osteoporosis. Using cell-base and animal models, as well as various experimental methodologies the authors demonstrated that Prdx5 is upregulated during osteogenesis but suppressed during osteoclastogenesis. This novel function Prdx5 was found to be associated with binding and regulation of hnRNPK which controls the expression of genes involved in osteoclastogenesis, such as osteocalcin (Ocn).

  (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

Regulated degradation of the inner nuclear membrane protein SUN2 maintains nuclear envelope architecture and function

1. Logesvaran Krshnan
2. Wingyan Skyla Siu
3. Michael Van de Weijer
4. Daniel Hayward
5. Elena Navarro Guerrero
6. Ulrike Gruneberg
7. Pedro Carvalho

• Curated by eLife

  Evaluation Summary:

  The paper provides fundamental information through the identification of an E3 ligase and kinase/phosphatase regulatory machinery that regulates the inner nuclear membrane protein SUN2 using a GFP-based assay. The data reveal a model involving extraction of ubiquitylation of SUN2 from the membrane by p97, which is an important contribution to the field. Although the biochemical evidence is solid on the GFP-tagged SUN2 protein, one question is the extent to which this pathway works on endogenous SUN2 and the extent to which this is a quality control mechanism for turnover of unassembled SUN2 or whether it acts on the fully assembled complex.

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

Reviewed by eLife

Tau seeds translocate across the cell membrane to initiate aggregation

1. Dana A. Dodd
2. Michael LaCroix
3. Clarissa Valdez
4. Gregory M. Knox
5. Anthony R. Vega
6. Ashwani Kumar
7. Chao Xing
8. Charles L. White
9. Marc I. Diamond

• Curated by eLife

  Evaluation Summary:

  Deposition of hyperphosphorylated misfolded tau is a hallmark of many neurodegenerative diseases, but the exact mechanisms by which misfolded tau spreads to adjacent areas of the brain are not known. In this manuscript, which will be of broad interest to cell biologists and neuroscientists, the authors suggest that tau fibrils that translocate directly through the cell membrane induce aggregation of cytosolic tau. While the results appear stunning, there are alternative explanations to the authors' hypothesis that require further investigation.

  (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

Nucleophagy contributes to genome stability through degradation of type II topoisomerases A and B and nucleolar components

1. Gabriel Muciño-Hernández
2. Pilar Sarah Acevo-Rodríguez
3. Sandra Cabrera-Benitez
4. Adán Oswaldo Guerrero
5. Horacio Merchant-Larios
6. Susana Castro-Obregón

Reviewed by Review Commons

Mitochondrial‐derived vesicles retain membrane potential and contain a functional ATP synthase

1. Reut Hazan
2. Dvora Lintzer
3. Tamar Ziv
4. Koyeli Das
5. Irit Rosenhek‐Goldian
6. Ziv Porat
7. Hila Ben Ami Pilo
8. Sharon Karniely
9. Ann Saada
10. Neta Regev‐Rudzki
11. Ophry Pines

Reviewed by Review Commons

Disrupting the ciliary gradient of active Arl3 affects rod photoreceptor nuclear migration

1. Amanda M Travis
2. Samiya Manocha
3. Jason R Willer
4. Timothy S Wessler
5. Nikolai P Skiba
6. Jillian N Pearring

• Curated by eLife

  Evaluation Summary:

  The current paper is of interest to cell biologists studying ciliogenesis and specifically vertebrate photoreceptors, which are specialized cilia. The study shows that mutations in the small GTP binding protein ARL3 known to cause dominant inherited retinal dystrophies in humans result in ARL3 hyperactivity, disrupting the normal ciliary gradient of ARL3 activity and leading to altered retinal development. The authors demonstrate restored normal nuclear distribution by overexpression of ARL3 effectors, suggesting that the active mutants disrupt nuclear migration, at least in part, by sequestering ARL3 effectors. Overall, the experiments are properly controlled, executed, and analyzed and involve a series of extensive biochemical analyses complemented with in vivo phenotypic assessment. The development of a method to analyze snapshots of the interaction between ARL3 and its interactors is also a strength of the paper, however, significant concerns remain regarding links between nuclear migration failure and ciliogenesis in the outer segment, and alternative possibilities that could explain the phenotype of the ARL3 Y90C mutant with respect to its sequestration of the GEF ARL13B. Addressing these major concerns would improve the manuscript and could have considerable impact on 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. Reviewer #1 agreed to share their name with the authors.)

Reviewed by eLife