Researchers observe how the flexibility of a #protein_hinge is crucial to the transfer of #cell proteins.

#Ubiquitination

https://phys.org/news/2024-01-flexibility-protein-hinge-crucial-cell.html

Researchers observe how the flexibility of a protein hinge is crucial to the transfer of cell proteins

Ubiquitination—the addition of the protein ubiquitin—is a key stage in many cell processes, such as protein degradation, DNA repairs, and signal transduction. Using high-speed atomic force microscopy (HS-AFM) and molecular modeling, researchers led by Hiroki Konno and Holger Flechsig at WPI-NanoLSI, Kanazawa University have identified how the mobility of a ubiquitination-related enzyme hinge allows ubiquitination to take place.

Phys.org

#Review: 'Deciphering the protein ubiquitylation system in plants'

🧬 F-box genes have roles in #ubiquitination and control many processes in #plants.
🧬 Here, a deleterious F-box duplication #model is presented.

https://doi.org/10.1093/jxb/erad354

Deciphering the protein ubiquitylation system in plants

This review presents strategies in tackling the role of the protein ubiquitylation system in plant growth and development from the perspectives of bioinformatic

OUP Academic

This #review summarises how pathogenic #effectors can mimic or target the highly conserved #ubiquitin–#proteasome system to disrupt cellular processes in their #plant hosts.

https://doi.org/10.1093/jxb/erad191

#ubiquitination #immunity #PAMP #effector

Ubiquitination from the perspective of plant pathogens

A review focusing on the strategies adopted by plant pathogens to secrete effectors that either mimic E3 ligase properties or target the ubiquitin–proteasome sy

OUP Academic

What can bacteria teach us about unexplored areas of #ubiquitin signaling and regulation?
John Pruneda and colleagues discuss how #pathogens subvert the host cell #ubiquitination system by either adopting or breaking its rules
New review article as #weekendreading!

https://www.embopress.org/doi/full/10.15252/embj.2023114318

#MARCH5-dependent #NLRP3 #ubiquitination is required for #mitochondrial NLRP3-NEK7 complex formation and NLRP3 #inflammasome activation
https://www.embopress.org/doi/full/10.15252/embj.2023113481
Mutations in PARK15/FBXO7 cause #ParkinsonsDisease. @alsanchezmar @Aitor_Mtz & @whitworth_lab shows that its fly ortholog works antagonistically with USP30 to set the #ubiquitination threshold needed to regulate basal #mitophagy #PLOSBiology https://plos.io/3qfaUZ1
FBXO7/ntc and USP30 antagonistically set the ubiquitination threshold for basal mitophagy and provide a target for Pink1 phosphorylation in vivo

Mutations in PARK15/FBXO7 cause autosomal recessive Parkinson’s disease. This study shows that its Drosophila orthologue, ntc, works antagonistically with USP30 to set the ubiquitination threshold needed to regulate basal mitophagy, and provides a target for Pink1 phosphorylation required for parkin-dependent stress-induced mitophagy.

How are specific dysfunctional #mitochondria removed under steady-state conditions?

Julia Pagan and coworkers (University of Queensland) show that an #SCF #ubiquitin #ligase based on #FBXL4, mutated in #MTDPS13, limits basal #mitophagy via #ubiquitination of #NIX and #BNIP3 receptors

https://www.embopress.org/doi/10.15252/embj.2022112767

A #protelysis cascade fine-tunes homologous #recombination repair in plants:
Arp Schnittger and coworkers show #KNOTEN1, stabilized by #UBP12/13, triggering K63-linked #ubiquitination and #autophagic degradation of #BLM complex subunit #RMI1 upon #DNAdamage

https://www.embopress.org/doi/10.15252/embj.2022111980

Surprising interplay between #SMC5/6 and #transcription-regulating #PAF1 complexes in #Arabidopsis #DNAdamage response:
Shunping Yan and colleagues find them to interact and recruit E2/E3 enzymes for #histone H2B #ubiquitination at DNA double-strand breaks
https://www.embopress.org/doi/10.15252/embj.2022112756
Granted, the test case is—you guessed it—#BRD4. Nevertheless, this could be an exciting new #TPD modality if it is generalizable to other target proteins, such as those lacking accessible lysines or for which #ubiquitination is slow or inefficient.