Stress granules display bistable dynamics modulated by Cdk

Yahya, Galal; Pérez, Alexis P.; Mendoza, Mònica B.; Parisi, Eva; Moreno, David F.; Artés, Marta H.; Gallego, Carme; Aldea, Martí

doi:10.1083/jcb.202005102

Cited by 14 publications

(13 citation statements)

References 57 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This result suggests that Pak1 at stress granules is poised to promote rapid release of its substrate Sts5 as cells re-enter polarized growth. This model is consistent with several other protein kinases that localize to RNP granules during specific stress conditions and function to dissolve granules upon removal of stress (Rai et al, 2018;Shattuck et al, 2019;Wippich et al, 2013;Yahya et al, 2021). Alternatively, stress granules could represent a storage depot for inactive Pak1 when cells stop growth during glucose starvation.…”

Section: Regulation and Function Of Pak1 At Stress Granulessupporting

confidence: 84%

Pak1 kinase controls cell shape through ribonucleoprotein granules

Magliozzi

Moseley

2021

eLife

View full text Add to dashboard Cite

Fission yeast cells maintain a rod shape due to conserved signaling pathways that organize the cytoskeleton for polarized growth. We discovered a mechanism linking the conserved protein kinase Pak1 with cell shape through the RNA-binding protein Sts5. Pak1 (also called Shk1 and Orb2) prevents Sts5 association with P bodies by directly phosphorylating its intrinsically disordered region (IDR). Pak1 and the cell polarity kinase Orb6 both phosphorylate the Sts5 IDR but at distinct residues. Mutations preventing phosphorylation in the Sts5 IDR cause increased P body formation and defects in cell shape and polarity. Unexpectedly, when cells encounter glucose starvation, PKA signaling triggers Pak1 recruitment to stress granules with Sts5. Through retargeting experiments, we reveal that Pak1 localizes to stress granules to promote rapid dissolution of Sts5 upon glucose addition. Our work reveals a new role for Pak1 in regulating cell shape through ribonucleoprotein granules during normal and stressed growth conditions.

show abstract

Section: Regulation and Function Of Pak1 At Stress Granulessupporting

confidence: 84%

Pak1 kinase controls cell shape through ribonucleoprotein granules

Magliozzi

Moseley

2021

eLife

View full text Add to dashboard Cite

show abstract

“…The presence of CDKA;1 in SGs was hypothesized to allow a cell to resume cell division activity in Arabidopsis after attenuation of the stress ( Kosmacz et al, 2019 ). CDKs typically require a co-factor, called cyclin, for their activity; in budding yeast, the RNA-binding protein WHISKEY 8 (WHI8) was shown to bind to and recruit the mRNA of the cyclin CLN3 to SGs upon heat stress, causing the inhibition of CLN3 mRNA translation ( Yahya et al, 2021 ). Interestingly, Cell Division Cycle 28, the homolog of CDKA;1 in budding yeast, is itself also recruited to SGs by WHI8 and has been found to play an important role in SG dissolution and the translation of SG-recruited mRNAs, such as for CLN3 , upon release from stress.…”

Section: Discussionmentioning

confidence: 99%

Heat stress reveals a specialized variant of the pachytene checkpoint in meiosis of Arabidopsis thaliana

et al. 2021

View full text Add to dashboard Cite

Plant growth and fertility strongly depend on environmental conditions such as temperature. Remarkably, temperature also influences meiotic recombination and thus, the current climate change will affect the genetic make-up of plants. To better understand the effects of temperature on meiosis, we followed male meiocytes in Arabidopsis thaliana by live cell imaging under three temperature regimes: at 21°C; at heat shock conditions of 30°C and 34°C; after an acclimatization phase of 1 week at 30°C. This work led to a cytological framework of meiotic progression at elevated temperature. We determined that an increase from 21°C to 30°C speeds up meiosis with specific phases being more amenable to heat than others. An acclimatization phase often moderated this effect. A sudden increase to 34°C promoted a faster progression of early prophase compared to 21°C. However, the phase in which cross-overs mature was prolonged at 34°C. Since mutants involved in the recombination pathway largely did not show the extension of this phase at 34°C, we conclude that the delay is recombination-dependent. Further analysis also revealed the involvement of the ATAXIA TELANGIECTASIA MUTATED kinase in this prolongation, indicating the existence of a pachytene checkpoint in plants, yet in a specialized form.

show abstract

“…Catalytic subunits of protein kinase A, Tpk2 and Tpk3, have also been identified in HS SGs [ 55 ]. Recently, the recruitment of Cdc28/Cdk1 to SGs by Whi8 has been reported with a function for Cdk1 in SGs disassembly [ 56 ].…”

Section: Introductionmentioning

confidence: 99%

eIF3a Destabilization and TDP-43 Alter Dynamics of Heat-Induced Stress Granules

Malcová

Senohrábková

Nováková

et al. 2021

IJMS

View full text Add to dashboard Cite

Stress granules (SGs) are membrane-less assemblies arising upon various stresses in eukaryotic cells. They sequester mRNAs and proteins from stressful conditions and modulate gene expression to enable cells to resume translation and growth after stress relief. SGs containing the translation initiation factor eIF3a/Rpg1 arise in yeast cells upon robust heat shock (HS) at 46 °C only. We demonstrate that the destabilization of Rpg1 within the PCI domain in the Rpg1-3 variant leads to SGs assembly already at moderate HS at 42 °C. These are bona fide SGs arising upon translation arrest containing mRNAs, which are components of the translation machinery, and associating with P-bodies. HS SGs associate with endoplasmatic reticulum and mitochondria and their contact sites ERMES. Although Rpg1-3-labeled SGs arise at a lower temperature, their disassembly is delayed after HS at 46 °C. Remarkably, the delayed disassembly of HS SGs after the robust HS is reversed by TDP-43, which is a human protein connected with amyotrophic lateral sclerosis. TDP-43 colocalizes with HS SGs in yeast cells and facilitates cell regrowth after the stress relief. Based on our results, we propose yeast HS SGs labeled by Rpg1 and its variants as a novel model system to study functions of TDP-43 in stress granules disassembly.

show abstract

Stress granules display bistable dynamics modulated by Cdk

Cited by 14 publications

References 57 publications

Pak1 kinase controls cell shape through ribonucleoprotein granules

Pak1 kinase controls cell shape through ribonucleoprotein granules

Heat stress reveals a specialized variant of the pachytene checkpoint in meiosis of Arabidopsis thaliana

eIF3a Destabilization and TDP-43 Alter Dynamics of Heat-Induced Stress Granules

Contact Info

Product

Resources

About