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ProteomicsTranslocation of polyubiquitinated protein substrates by the hexameric Cdc48 ATPase
The hexameric Cdc48 ATPase (p97 or VCP in mammals) cooperates with its cofactor Ufd1/Npl4 to extract polyubiquitinated proteins from membranes or macromolecular complexes for degradation by the proteasome. Here, we clarify how the Cdc48 complex unfolds its substrates and translocates polypeptides wi...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2022-01-19 | PXD027639 | Pride
Hydrogen deuterium exchange mass spectrometry Npl4 Unfolding Ufd1 Translocation Ubiquitin Vcp Hdx-ms P97 Aaa atpase 
Genomicscdc48-353 suppressors identified by whole genome sequencing
Single site suppressors of a fission yeast temperature-sensitive mutant in cdc48 identified by whole genome sequencing
PRJEB7979 | ENA
ProteomicsComparative proteome-wide abundance profiling of yeast strains deleted for Cdc48 adaptors
The yeast ATPase Cdc48 (known as p97/VCP in human cells) plays an important role in the Ubiquitin Proteasome System. VCP is essential for cancer cell proliferation and its dysregulation has been implicated in several neurodegenerative diseases. Cdc48 functions by extracting ubiquitylated proteins fr...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2025-05-07 | PXD055137 | Pride
Ubiquitin proteasome system S. cerevisiae Ubx domain-containing proteins Tmt proteomics Cdc48 Proteome 
ProteomicsVisualization of the Cdc48 AAA+ ATPase protein unfolding pathway: Substrate Identification
The Cdc48 AAA+ ATPase is an abundant and essential enzyme that unfolds substrates in multiple protein quality control pathways. The enzyme includes two conserved AAA+ ATPase cassettes, D1 and D2, that assemble as hexameric rings with D1 stacked above D2. Here, we report an ensemble of structures of ...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2024-10-17 | PXD048280 | Pride
Human Shp1 pulldown 
ProteomicsBidirectional substrate shuttling between the 26S proteasome and the Cdc48 ATPase promotes protein degradation
Most eukaryotic proteins are degraded by the 26S proteasome after modification with a polyubiquitin chain. Substrates lacking unstructured segments cannot be degraded directly and require prior unfolding by the Cdc48 ATPase (p97 or VCP in mammals) in complex with its ubiquitin-binding partner Ufd1-N...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2024-02-23 | PXD042878 | Pride
Erad Aaa atpase Protein degradation Ubiquitin Cdc48 Shuttling factor P97 Proteasome Protein unfolding 
ProteomicsCdc48’s interactions play a role in the cellular oxidative response in an aging-dependent manner
The cellular redox status has long been linked to different cellular functions, including protein quality control (PQC) and aging. The prominent molecular machine Cdc48 (p97/VCP in mammals) is one of the key players involved in PQC, shuttling misfolded proteins to degradation. Through a range of N-t...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2025-05-28 | PXD045122 | Pride
Redox Yeast Aging 
UnknownToward an understanding of the Cdc48/p97 ATPase.
Not available
S-EPMC5543420 | biostudies-literature
UnknownThe Cdc48-Vms1 complex maintains 26S proteasome architecture.
Not available
S-EPMC4135392 | biostudies-literature
UnknownCdc48 regulates a deubiquitylase cascade critical for mitochondrial fusion.
Not available
S-EPMC5798933 | biostudies-literature
ProteomicsTargeting of SUMO substrates to a Cdc48-Ufd1-Npl4 segregase and STUbL pathway in fission yeast
In eukaryotes, the conjugation of proteins to the small ubiquitin-like modifier SUMO regulates numerous cellular functions. A proportion of SUMO conjugates are targeted for degradation by SUMO-targeted ubiquitin ligases (STUbLs) and it has been proposed that the ubiquitin-selective chaperone Cdc48/p...
ORGANISM(S): Schizosaccharomyces pombe 
2015-10-30 | PXD002972 | Pride
Lc-msms S. pombe Stubl Cdc48-ufd1-npl4 Sumo modification sites 
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