Featured
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News & Views |
Saving ribosomal proteins for later
Disruption of ribosome assembly results in the accumulation of aggregation-prone ‘orphaned’ ribosomal proteins that are toxic to cells if left unchecked. A study finds that cells store such ribosomal proteins during heat shock to enable a quick recovery of ribosome assembly after the removal of this stress.
- Joshua J. Black
- & Rachel Green
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Article |
Adaptive preservation of orphan ribosomal proteins in chaperone-dispersed condensates
Ali et al. show that, during heat shock, aggregation-prone orphan ribosomal proteins form nucleolar-associated condensates that are kept in a liquid-like and reusable state through Hsp70 and its co-chaperones.
- Asif Ali
- , Rania Garde
- & David Pincus
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News & Views |
Chaperoning the nuclear envelope
FG-nucleoporins of the nuclear pore complexes form a permeability barrier between the nucleus and the cytosol. FG-nucleoporins contain disordered regions and are prone to aggregation. Two studies identify the chaperone DNAJB6 as a key factor that prevents aggregation of FG-nucleoporins and assists in the biogenesis of nuclear pore complexes.
- Janine Kirstein
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Letter |
The chaperone DNAJB6 surveils FG-nucleoporins and is required for interphase nuclear pore complex biogenesis
Kuiper et al. and Prophet et al. implicate DNAJB6/HSP70 chaperone activities in the biogenesis of the nuclear pore complex permeability barrier and find that disease-linked nuclear envelope blebs are enriched in nucleoporin and chaperone condensates.
- E. F. Elsiena Kuiper
- , Paola Gallardo
- & Steven Bergink
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Article |
Atypical nuclear envelope condensates linked to neurological disorders reveal nucleoporin-directed chaperone activities
Kuiper et al. and Prophet et al. implicate DNAJB6/HSP70 chaperone activities in the biogenesis of the nuclear pore complex permeability barrier and find that disease-linked nuclear envelope blebs are enriched in nucleoporin and chaperone condensates.
- Sarah M. Prophet
- , Anthony J. Rampello
- & Christian Schlieker
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News & Views |
Finding a chaperone for TDP-43
Aggregation of the RNA-binding protein TDP-43 is commonly observed in neurodegenerative disorders. A new study reveals that this process may be blocked by HSPB1, a small heat shock protein that can also regulate TDP-43 phase separation. This may be relevant to neurodegeneration, as loss of HSPB1 correlates with TDP-43 pathology.
- Yuna M. Ayala
- & Zachary R. Grese
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Article |
Reversible phase separation of HSF1 is required for an acute transcriptional response during heat shock
Zhang, Shao and coworkers report that HSF1 forms small condensates at its target gene loci to promote their transcription during acute heat stress. The produced HSP70 proteins in turn disperse HSF1 condensates to shut off the heat-shock response.
- Hongchen Zhang
- , Shipeng Shao
- & Yujie Sun
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News & Views |
Metabolites control stress granule disassembly
Cells respond to stimuli by reorganizing their contents into subcellular structures. New research demonstrates that yeast pyruvate kinase Cdc19 interacts with fructose-1,6-bisphosphate to coordinate disassembly of stress granules. These findings reveal how proteins can directly sense the cellular energy state to facilitate adaptive reorganization.
- Christopher M. Jakobson
- & Daniel F. Jarosz
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Article |
Reversible amyloids of pyruvate kinase couple cell metabolism and stress granule disassembly
Cereghetti et al. report that the glycolytic metabolite fructose-1,6-bisphosphate initiates the disassembly of amyloids formed by the yeast pyruvate kinase Cdc19 to resume ATP production during stress recovery.
- Gea Cereghetti
- , Caroline Wilson-Zbinden
- & Matthias Peter
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News & Views |
Protein homeostasis from the outside in
Secretory proteins undergo multiple rounds of co- and post-translational quality control checks inside the cell, but how their integrity is maintained outside the cell is an emerging topic. A study establishes a model system to investigate how the extracellular proteome is protected and integrates its findings into existing immune pathways.
- Brant M. Webster
- , Holly K. Gildea
- & Andrew Dillin
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Letter |
HSF1 phase transition mediates stress adaptation and cell fate decisions
Gaglia et al. show, using single-cell imaging and analysis in human tumours, that phase transition of heat-shock factor 1 (HSF1) to form intranuclear stress bodies mediates cell-fate decisions underlying cell survival or death.
- Giorgio Gaglia
- , Rumana Rashid
- & Sandro Santagata
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Article |
Mitochondrial protein-induced stress triggers a global adaptive transcriptional programme
Boos et al. show that impairing mitochondrial protein import induces a global transcriptional response to activate the ubiquitin–proteasome system and heat stress response and repress oxidative phosphorylation genes.
- Felix Boos
- , Lena Krämer
- & Johannes M. Herrmann
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News & Views |
Preserving protein function through reversible aggregation
It is generally accepted that protein function depends on a defined 3D structure, with unfolding and aggregation dealing a final blow to functionality. A study now shows that the regulated exposure of an unstructured region in yeast pyruvate kinase triggers reversible aggregation to preserve protein function under stress.
- Jörg Höhfeld
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Article |
Reversible protein aggregation is a protective mechanism to ensure cell cycle restart after stress
Saad et al. identify stress-induced reversible protein aggregation as a protective mechanism to ensure cell cycle resumption and cell survival after stress in yeast.
- Shady Saad
- , Gea Cereghetti
- & Reinhard Dechant
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Cyclophilin A supports translation of intrinsically disordered proteins and affects haematopoietic stem cell ageing