A Conserved Protein with AN1 Zinc Finger and Ubiquitin-like Domains Modulates Cdc48 (p97) Function in the Ubiquitin-Proteasome Pathway*
Explore this paper's citation graph
Summary
Cuz1 is a highly conserved Cdc48 cofactor that also binds proteasomes, especially in cells exposed to arsenite, and helps limit the accumulation of ubiquitin conjugates on both the proteasome and C DC48, suggesting a possible role in the transfer of ubiquitylated substrates from CDC48 to the prote asome or in their release from these complexes.
- Type
- article
- Published
- 2013-10-11
- Cited by
- 24
- References
- 77
- Access
- Open access
- OpenAlex
- https://openalex.org/W2065811505
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:21307361
Keywords
Proteasome, Ubiquitin, Zinc finger, Cell biology, Protein degradation
References
- The short-lived MAT alpha 2 transcriptional regulator is ubiquitinated in vivo.
- An abundant and ubiquitous homo‐oligomeric ring‐shaped ATPase particle related to the putative vesicle fusion proteins Sec18p and NSF.
- Disulfide Engineering to Map Subunit Interactions in the Proteasome and Other Macromolecular Complexes
- p47 is a cofactor for p97-mediated membrane fusion
- Distinct 19 S and 20 S subcomplexes of the 26 S proteasome and their distribution in the nucleus and the cytoplasm.
- The delitto perfetto approach to in vivo site-directed mutagenesis and chromosome rearrangements with synthetic oligonucleotides in yeast.
- Cdc48p interacts with Ufd3p, a WD repeat protein required for ubiquitin‐mediated proteolysis in Saccharomyces cerevisiae.
- Functional division of substrate processing cofactors of the ubiquitin-selective Cdc48 chaperone.
- The Cdc48 machine in endoplasmic reticulum associated protein degradation.
- Stalled Proteasomes Are Directly Relieved by P97 Recruitment*
- Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MAT alpha 2 repressor.
- ER Degradation of a Misfolded Luminal Protein by the Cytosolic Ubiquitin-Proteasome Pathway
- A Proteolytic Pathway That Recognizes Ubiquitin as a Degradation Signal (*)
- Proteasome-associated proteins: regulation of a proteolytic machine
- Role of the ubiquitin‐selective CDC48UFD1/NPL4 chaperone (segregase) in ERAD of OLE1 and other substrates
- Complete structure of p97/valosin-containing protein reveals communication between nucleotide domains
- An arsenite-inducible 19S regulatory particle-associated protein adapts proteasomes to proteotoxicity.
- Systematical Optimization of Reverse-phase Chromatography for Shotgun Proteomics
- Recognition of the polyubiquitin proteolytic signal
- Global analysis of protein expression in yeast
Cited by
- A protein interaction map of the LSU processome
- Cuz1/Ynl155w, a Zinc-dependent Ubiquitin-binding Protein, Protects Cells from Metalloid-induced Proteotoxicity*
- Ubiquitin Proteasome System as Target for Tumor Therapy
- Proteomic Analysis Identifies Ribosome Reduction as an Effective Proteotoxic Stress Response*
- Tmc1 Is a Dynamically Regulated Effector of the Rpn4 Proteotoxic Stress Response*
- Solution Structure of the Cuz1 AN1 Zinc Finger Domain: An Exposed LDFLP Motif Defines a Subfamily of AN1 Proteins
- Phospholipase Lpl1 links lipid droplet function with quality control protein degradation
- ZFAND1 Recruits p97 and the 26S Proteasome to Promote the Clearance of Arsenite-Induced Stress Granules.
- Isolation of multi-metal tolerant ubiquitin fusion protein from metal polluted soil by metatranscriptomic approach.
- ZFAND5/ZNF216 is an activator of the 26S proteasome that stimulates overall protein degradation
- An Allosteric Interaction Network Promotes Conformation State-Dependent Eviction of the Nas6 Assembly Chaperone from Nascent 26S Proteasomes
- The proteasome and its network: engineering for adaptability
- The Ulp2 SUMO protease promotes transcription elongation through regulation of histone sumoylation
- Coordinated Actions Between p97 and Cullin-RING Ubiquitin Ligases for Protein Degradation.
- Histone sumoylation promotes Set3 histone-deacetylase complex-mediated transcriptional regulation
- AN1-type zinc finger protein 3 (ZFAND3) is a transcriptional regulator that drives Glioblastoma invasion
- RGG-motif protein Sbp1 is required for Processing body (P-body) disassembly
- Low complexity RGG-motif sequence is required for Processing body (P-body) disassembly
- Yeast PI31 Inhibits the Proteasome by a Direct Multisite Mechanism
- Role of Proteostasis Regulation in the Turnover of Stress Granules
Related papers
- Proteasomal AAA-ATPases: structure and function.
- Autoregulation of the 26S proteasome by in situ ubiquitination
- HECT ubiquitin ligases as accessory proteins of the plant proteasome
- P53: Stability from the Ubiquitin–Proteasome System and Specific 26S Proteasome Inhibitors
- Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48
- Multi-Step Ubiquitin Decoding Mechanism for Proteasomal Degradation
- Ubiquitin-like Protein FAT10-mediated Proteasome Degradation
- Regulation of Protein Degradation by Proteasomes in Cancer
- Selective chemical inactivation of AAA proteins reveals distinct functions of proteasomal ATPases.