Localized Proteasomal Degradation: From the Nucleus to Cell Periphery

Guo, Xing

doi:10.3390/biom12020229

Cited by 17 publications

(23 citation statements)

References 180 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The research on protein proteasomal degradation and quality control has been growing for decades and recently has acquired renewed impetus with the awareness on the importance of protein condensation in these cellular functions. For a recent review on this subject we refer the reader to the work of Xing Guo (2022) . Finally, many examples of the various mechanisms through which condensation affects biological function at molecular scale were collected by Lyon et al.…”

Section: Promising Trends In Biomolecular Condensationmentioning

confidence: 99%

Protein conformation and biomolecular condensates

Vazquez

Toledo

Gianotti

et al. 2022

Current Research in Structural Biology

View full text Add to dashboard Cite

Section: Promising Trends In Biomolecular Condensationmentioning

confidence: 99%

Protein conformation and biomolecular condensates

Vazquez

Toledo

Gianotti

et al. 2022

Current Research in Structural Biology

View full text Add to dashboard Cite

“…A majority of proteins anchored in membrane-containing organelles have been reported to be degraded via the cytosolic proteasome system(Guo, 2022; Ramachandran et al, 2018). The spatial separation between substrate selection and degradation requires either membrane-anchored substrates extraction from the membrane or recruitment of 26S proteasomes to the membrane.…”

Section: Discussionmentioning

confidence: 99%

A host E3 ubiquitin ligase regulatesSalmonellavirulence by targeting an SPI-2 effector involved in SIF biogenesis

Meng

Yang

Xue

et al. 2022

Preprint

View full text Add to dashboard Cite

Salmonella Typhimurium creates an intracellular niche for its replication by utilizing a large cohort of effectors, including several that function to interfere with host ubiquitin signaling. Although the mechanism of action of many such effectors has been elucidated, how the interplay between the host ubiquitin network and bacterial virulence factors dictates the outcome of infection largely remains undefined. Here we found that the SPI-2 effector SseK3 inhibits SNARE pairing to promote the formation of Salmonella-induced filament by Arg-GlcNAcylation of SNARE proteins, including SNAP25, VAMP8, and Syntaxin. Further study reveals that host cells counteract the activity of SseK3 by inducing the expression of the ubiquitin E3 ligase TRIM32, which catalyzes K48-linked ubiquitination on SseK3 and targets its membrane-associated portion for degradation. Hence, TRIM32 antagonizes SNAP25 Arg-GlcNAcylation induced by SseK3 to restrict SIF biogenesis and Salmonella replication. Our study reveals a mechanism by which host cells inhibit bacterial replication by eliminating specific virulence factor.

show abstract

“…In addition to phosphorylation, other post-translational modifications have been reported. These include O-linked N-acetylglucosamination [61], ADP-ribosylation [62], acetylation, and myristylation [63,64]. O-linked N-acetylglucosamination leads to inhibition of ATPase activity of the 26S complex and inhibits proteolytic activity of proteasomes.…”

Section: Structure and Functions Of Proteasomesmentioning

confidence: 99%

Proteasome Interactome and Its Role in the Mechanisms of Brain Plasticity

Buneeva

Kopylov²,

Медведев³

2023

Biochemistry Moscow

View full text Add to dashboard Cite

Proteasomes are highly conserved multienzyme complexes responsible for proteolytic degradation of the short-lived, regulatory, misfolded, and damaged proteins. They play an important role in the processes of brain plasticity, and decrease in their function is accompanied by the development of neurodegenerative pathology. Studies performed in different laboratories both on cultured mammalian and human cells and on preparations of the rat and rabbit brain cortex revealed a large number of proteasome-associated proteins. Since the identified proteins belong to certain metabolic pathways, multiple enrichment of the proteasome fraction with these proteins indicates their important role in proteasome functioning. Extrapolation of the experimental data, obtained on various biological objects, to the human brain suggests that the proteasome-associated proteins account for at least 28% of the human brain proteome. The proteasome interactome of the brain contains a large number of proteins involved in the assembly of these supramolecular complexes, regulation of their functioning, and intracellular localization, which could be changed under different conditions (for example, during oxidative stress) or in different phases of the cell cycle. In the context of molecular functions of the Gene Ontology (GO) Pathways, the proteins of the proteasome interactome mediate cross-talk between components of more than 30 metabolic pathways annotated in terms of GO. The main result of these interactions is binding of adenine and guanine nucleotides, crucial for realization of the nucleotide-dependent functions of the 26S and 20S proteasomes. Since the development of neurodegenerative pathology is often associated with regioselective decrease in the functional activity of proteasomes, a positive therapeutic effect would be obviously provided by the factors increasing proteasomal activity. In any case, pharmacological regulation of the brain proteasomes seems to be realized through the changes in composition and/or activity of the proteins associated with proteasomes (deubiquitinase, PKA, CaMKIIα, etc.).

show abstract

Localized Proteasomal Degradation: From the Nucleus to Cell Periphery

Cited by 17 publications

References 180 publications

Protein conformation and biomolecular condensates

Protein conformation and biomolecular condensates

A host E3 ubiquitin ligase regulatesSalmonellavirulence by targeting an SPI-2 effector involved in SIF biogenesis

Proteasome Interactome and Its Role in the Mechanisms of Brain Plasticity

Contact Info

Product

Resources

About