Mechanisms and regulation of substrate degradation by the 26S proteasome

C Arkinson, KC Dong, CL Gee, A Martin - Nature Reviews Molecular …, 2024 - nature.com
The 26S proteasome is involved in degrading and regulating the majority of proteins in
eukaryotic cells, which requires a sophisticated balance of specificity and promiscuity. In this …

[HTML][HTML] Control of p97 function by cofactor binding

A Buchberger, H Schindelin, P Hänzelmann - FEBS letters, 2015 - Elsevier
Abstract p97 (also known as Cdc48, Ter94, and VCP) is an essential, abundant and highly
conserved ATPase driving the turnover of ubiquitylated proteins in eukaryotes. Even though …

Origin and functional evolution of the Cdc48/p97/VCP AAA+ protein unfolding and remodeling machine

D Barthelme, RT Sauer - Journal of molecular biology, 2016 - Elsevier
Abstract The AAA+ Cdc48 ATPase (alias p97 or VCP) is a key player in multiple ubiquitin-
dependent cell signaling, degradation, and quality control pathways. Central to these broad …

[HTML][HTML] Neddylation and deneddylation in cardiac biology

S Kandala, I Kim, H Su - American journal of cardiovascular …, 2014 - ncbi.nlm.nih.gov
Neddylation is a post-translational protein modification that conjugates a ubiquitin-like
protein NEDD8 to target proteins. Similar to ubiquitination, neddylation is mediated by a …

Ubiquitin-like modifications in the DNA damage response

Z Wang, WG Zhu, X Xu - Mutation Research/Fundamental and Molecular …, 2017 - Elsevier
Genomic DNA is damaged at an extremely high frequency by both endogenous and
environmental factors. An improper response to DNA damage can lead to genome …

SVIP reduces IGFBP-2 expression and inhibits glioblastoma progression via stabilizing PTEN

Z Wang, X Qiao, Y Chen, N Peng, C Niu, Y Wang… - Cell Death …, 2024 - nature.com
Glioblastoma (GBM) presents significant challenges due to its invasive nature and genetic
heterogeneity. In this study, we investigated the impact of Small VCP/P97-Interacting Protein …

Characterization of an additional binding surface on the p97 N-terminal domain involved in bipartite cofactor interactions

P Hänzelmann, H Schindelin - Structure, 2016 - cell.com
Summary The type II AAA ATPase p97 interacts with a large number of cofactors that
regulate its function by recruiting it to different cellular pathways. Most of the cofactors …

Modular arrangements of sequence motifs determine the functional diversity of KDM proteins

Z Wang, D Liu, B Xu, R Tian, Y Zuo - Briefings in Bioinformatics, 2021 - academic.oup.com
Histone lysine demethylases (KDMs) play a vital role in regulating chromatin dynamics and
transcription. KDM proteins are given modular activities by its sequence motifs with obvious …

Aggregation of polyglutamine-expanded ataxin-3 sequesters its specific interacting partners into inclusions: implication in a loss-of-function pathology

H Yang, JJ Li, S Liu, J Zhao, YJ Jiang, AX Song… - Scientific reports, 2014 - nature.com
Expansion of polyglutamine (polyQ) tract may cause protein misfolding and aggregation that
lead to cytotoxicity and neurodegeneration, but the underlying mechanism remains to be …

IBMPFD disease-causing mutant VCP/p97 proteins are targets of autophagic-lysosomal degradation

O Bayraktar, O Oral, NM Kocaturk, Y Akkoc, K Eberhart… - PloS one, 2016 - journals.plos.org
The ubiquitin-proteasome system (UPS) degrades soluble proteins and small aggregates,
whereas macroautophagy (autophagy herein) eliminates larger protein aggregates, tangles …