Gene Symbol: CDC48
Description: AAA family ATPase CDC48
Alias: AAA family ATPase CDC48
Species: Saccharomyces cerevisiae S288c
Products:     CDC48

Top Publications

  1. Richly H, Rape M, Braun S, Rumpf S, Hoege C, Jentsch S. A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting. Cell. 2005;120:73-84 pubmed
    ..Recent studies suggest the involvement of the AAA ATPase CDC48, its cofactors, and other ubiquitin binding factors in protein degradation, but how these proteins work together ..
  2. Schuberth C, Buchberger A. Membrane-bound Ubx2 recruits Cdc48 to ubiquitin ligases and their substrates to ensure efficient ER-associated protein degradation. Nat Cell Biol. 2005;7:999-1006 pubmed
    ..ubiquitin-proteasome system - a process involving dedicated ubiquitin ligases and the chaperone-like AAA ATPase Cdc48 (also known as p97). How the activities of these proteins are coupled remains unclear...
  3. Hsieh M, Chen R. Cdc48 and cofactors Npl4-Ufd1 are important for G1 progression during heat stress by maintaining cell wall integrity in Saccharomyces cerevisiae. PLoS ONE. 2011;6:e18988 pubmed publisher
    The ubiquitin-selective chaperone Cdc48, a member of the AAA (ATPase Associated with various cellular Activities) ATPase superfamily, is involved in many processes, including endoplasmic reticulum-associated degradation (ERAD), ubiquitin-..
  4. Cheng Y, Chen R. The AAA-ATPase Cdc48 and cofactor Shp1 promote chromosome bi-orientation by balancing Aurora B activity. J Cell Sci. 2010;123:2025-34 pubmed publisher
    ..The ubiquitin-selective chaperone Cdc48 (p97 in Metazoa), an AAA-ATPase, might facilitate such processes in the cell cycle...
  5. Gauss R, Sommer T, Jarosch E. The Hrd1p ligase complex forms a linchpin between ER-lumenal substrate selection and Cdc48p recruitment. EMBO J. 2006;25:1827-35 pubmed
    ..Thus, the Hrd1p ligase complex unites substrate selection in the ER lumen and polyubiquitination in the cytoplasm and links these processes to the release of ER proteins via the Cdc48p complex. ..
  6. Mullally J, Chernova T, Wilkinson K. Doa1 is a Cdc48 adapter that possesses a novel ubiquitin binding domain. Mol Cell Biol. 2006;26:822-30 pubmed
    b>Cdc48 (p97/VCP) is an AAA-ATPase molecular chaperone whose cellular functions are facilitated by its interaction with ubiquitin binding cofactors (e.g., Npl4-Ufd1 and Shp1)...
  7. Shcherbik N, Haines D. Cdc48p(Npl4p/Ufd1p) binds and segregates membrane-anchored/tethered complexes via a polyubiquitin signal present on the anchors. Mol Cell. 2007;25:385-97 pubmed
    ..These results provide biochemical evidence that Cdc48p(Npl4p/Ufd1p) functions as a polyubiquitin-selective segregase and that a polyubiquitin-Cdc48p pathway modulates protein interactions at cell membranes. ..
  8. Medicherla B, Kostova Z, Schaefer A, Wolf D. A genomic screen identifies Dsk2p and Rad23p as essential components of ER-associated degradation. EMBO Rep. 2004;5:692-7 pubmed
    ..factors for ubiquitinated ER substrates to the proteasome, following their removal from the membrane via the Cdc48-Ufd1-Npl4p complex...
  9. Rape M, Hoppe T, Gorr I, Kalocay M, Richly H, Jentsch S. Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone. Cell. 2001;107:667-77 pubmed
    ..Subsequently, p90 is liberated from its partner for nuclear targeting by the activity of the chaperone-like CDC48(UFD1/NPL4) complex...

More Information


  1. Latterich M, Fröhlich K, Schekman R. Membrane fusion and the cell cycle: Cdc48p participates in the fusion of ER membranes. Cell. 1995;82:885-93 pubmed
    ..A temperature-sensitive cdc48 mutant is conditionally defective in ER fusion in vitro...
  2. Neuber O, Jarosch E, Volkwein C, Walter J, Sommer T. Ubx2 links the Cdc48 complex to ER-associated protein degradation. Nat Cell Biol. 2005;7:993-8 pubmed
    ..The AAA ATPase Cdc48 (known as p97 or VCP in mammals) has a crucial, but poorly understood role in this transport step...
  3. Sato B, Schulz D, Do P, Hampton R. Misfolded membrane proteins are specifically recognized by the transmembrane domain of the Hrd1p ubiquitin ligase. Mol Cell. 2009;34:212-22 pubmed publisher
    ..From in vitro and interaction studies, we suggest a model in which the Hrd1p membrane domain employs intramembrane residues to evaluate substrate misfolding, leading to selective ubiquitination of appropriate ERAD-M clients...
  4. Wilcox A, Laney J. A ubiquitin-selective AAA-ATPase mediates transcriptional switching by remodelling a repressor-promoter DNA complex. Nat Cell Biol. 2009;11:1481-6 pubmed publisher
    ..This disassembly of alpha2 from DNA depends on the ubiquitin-selective AAA-ATPase Cdc48. Our findings expand the functional targets of Cdc48 to include active transcriptional regulatory complexes in the ..
  5. Zhao G, Li G, Schindelin H, Lennarz W. An Armadillo motif in Ufd3 interacts with Cdc48 and is involved in ubiquitin homeostasis and protein degradation. Proc Natl Acad Sci U S A. 2009;106:16197-202 pubmed publisher
    The yeast AAA-ATPase Cdc48 and the ubiquitin fusion degradation (UFD) proteins play important, evolutionarily conserved roles in ubiquitin dependent protein degradation...
  6. Fröhlich K, Fries H, Rudiger M, Erdmann R, Botstein D, Mecke D. Yeast cell cycle protein CDC48p shows full-length homology to the mammalian protein VCP and is a member of a protein family involved in secretion, peroxisome formation, and gene expression. J Cell Biol. 1991;114:443-53 pubmed
    Yeast mutants of cell cycle gene cdc48-1 arrest as large budded cells with microtubules spreading aberrantly throughout the cytoplasm from a single spindle plaque. The gene was cloned and disruption proved it to be essential...
  7. Wang C, Lee S. The ubiquitin-like (UBX)-domain-containing protein Ubx2/Ubxd8 regulates lipid droplet homeostasis. J Cell Sci. 2012;125:2930-9 pubmed publisher
    ..The mammalian Ubxd8 (also known as FAF2), when expressed in yeast, complements the defect of ubx2?, implying a functional conservation for these UBX-domain-containing proteins in lipid homeostasis...
  8. Verma R, Oania R, Fang R, Smith G, Deshaies R. Cdc48/p97 mediates UV-dependent turnover of RNA Pol II. Mol Cell. 2011;41:82-92 pubmed publisher
    b>Cdc48/p97 is an essential ATPase whose role in targeting substrates to the ubiquitin-proteasome system (UPS) remains unclear. Existing models posit that Cdc48 acts upstream of UPS receptors...
  9. Sato B, Hampton R. Yeast Derlin Dfm1 interacts with Cdc48 and functions in ER homeostasis. Yeast. 2006;23:1053-64 pubmed
    ..Furthermore, Dfm1p interacts with Cdc48p through its SHP boxes, and so defines a new motif for interaction with this widely-employed AAA-ATPase. ..
  10. Madeo F, Schlauer J, Zischka H, Mecke D, Fröhlich K. Tyrosine phosphorylation regulates cell cycle-dependent nuclear localization of Cdc48p. Mol Biol Cell. 1998;9:131-41 pubmed
    ..Two-hybrid studies indicate that the phosphorylation results in a conformational change of the protein, exposing the nuclear import signal sequence previously masked by a stretch of acidic residues. ..
  11. Rabinovich E, Kerem A, Frohlich K, Diamant N, Bar Nun S. AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation. Mol Cell Biol. 2002;22:626-34 pubmed well as soluble lumenal CPY*, two short-lived ERAD substrates, are markedly stabilized in conditional cdc48 yeast mutants...
  12. Böhm S, Lamberti G, Fernández Sáiz V, Stapf C, Buchberger A. Cellular functions of Ufd2 and Ufd3 in proteasomal protein degradation depend on Cdc48 binding. Mol Cell Biol. 2011;31:1528-39 pubmed publisher
    The chaperone-related AAA ATPase Cdc48 (p97/VCP in higher eukaryotes) segregates ubiquitylated proteins for subsequent degradation by the 26S proteasome or for nonproteolytic fates...
  13. Rumpf S, Jentsch S. Functional division of substrate processing cofactors of the ubiquitin-selective Cdc48 chaperone. Mol Cell. 2006;21:261-9 pubmed
    ..A central element in a major escort pathway is Cdc48, a chaperone-like AAA ATPase that collects ubiquitylated substrates via alternative substrate-recruiting cofactors...
  14. Ye Y, Meyer H, Rapoport T. The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature. 2001;414:652-6 pubmed
    ..Here we demonstrate that another member of this family, Cdc48 in yeast and p97 in mammals, is required for the export of ER proteins into the cytosol...
  15. Carvalho P, Stanley A, Rapoport T. Retrotranslocation of a misfolded luminal ER protein by the ubiquitin-ligase Hrd1p. Cell. 2010;143:579-91 pubmed publisher
    ..Our results suggest a model for how Hrd1p promotes polypeptide movement through the ER membrane. ..
  16. Horn S, Hanna J, Hirsch C, Volkwein C, Schütz A, Heinemann U, et al. Usa1 functions as a scaffold of the HRD-ubiquitin ligase. Mol Cell. 2009;36:782-93 pubmed publisher
    ..Our data demonstrate that scaffold proteins are required to adapt ubiquitin ligase activities toward different classes of substrates. ..
  17. Carvalho P, Goder V, Rapoport T. Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins. Cell. 2006;126:361-73 pubmed
    ..All three pathways converge at the Cdc48p ATPase complex. These results lead to a unifying concept for ERAD that may also apply to mammalian cells. ..
  18. Heo J, Livnat Levanon N, Taylor E, Jones K, Dephoure N, Ring J, et al. A stress-responsive system for mitochondrial protein degradation. Mol Cell. 2010;40:465-80 pubmed publisher
    We show that Ydr049 (renamed VCP/Cdc48-associated mitochondrial stress-responsive--Vms1), a member of an unstudied pan-eukaryotic protein family, translocates from the cytosol to mitochondria upon mitochondrial stress...
  19. Moir D, Stewart S, Osmond B, Botstein D. Cold-sensitive cell-division-cycle mutants of yeast: isolation, properties, and pseudoreversion studies. Genetics. 1982;100:547-63 pubmed alleles of CDC11, while the remaining mutants defined at least six new cell-division-cycle genes: CDC44, CDC45, CDC48, CDC49, CDC50 and CDC51...
  20. Hitchcock A, Krebber H, Frietze S, Lin A, Latterich M, Silver P. The conserved npl4 protein complex mediates proteasome-dependent membrane-bound transcription factor activation. Mol Biol Cell. 2001;12:3226-41 pubmed
    ..Mutations in NPL4, UFD1, and CDC48 cause a block in Mga2p and Spt23p processing, with concomitant loss of OLE1 expression...
  21. Braun S, Matuschewski K, Rape M, Thoms S, Jentsch S. Role of the ubiquitin-selective CDC48(UFD1/NPL4 )chaperone (segregase) in ERAD of OLE1 and other substrates. EMBO J. 2002;21:615-21 pubmed
    ..and the subsequent mobilization of the cleaved, ubiquitylated transcription factor from its partner molecule by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone-like enzyme...
  22. Fu X, Ng C, Feng D, Liang C. Cdc48p is required for the cell cycle commitment point at Start via degradation of the G1-CDK inhibitor Far1p. J Cell Biol. 2003;163:21-6 pubmed
    ..Because previous cdc48 mutants have exclusive G2/M arrest, Cdc48p was thought to play an essential role only during mitosis...
  23. Decottignies A, Evain A, Ghislain M. Binding of Cdc48p to a ubiquitin-related UBX domain from novel yeast proteins involved in intracellular proteolysis and sporulation. Yeast. 2004;21:127-39 pubmed
    The Cdc48/p97 AAA-ATPase functions in membrane fusion and ubiquitin-dependent protein degradation...
  24. Denic V, Quan E, Weissman J. A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation. Cell. 2006;126:349-59 pubmed
  25. Ghislain M, Dohmen R, Levy F, Varshavsky A. Cdc48p interacts with Ufd3p, a WD repeat protein required for ubiquitin-mediated proteolysis in Saccharomyces cerevisiae. EMBO J. 1996;15:4884-99 pubmed
    ..The discovery of the Ufd3p--Cdc48p complex and the finding that this complex is a part of the Ub system open up a new direction for studies of the function of Ub in the cell cycle and membrane dynamics. ..
  26. Bays N, Wilhovsky S, Goradia A, Hodgkiss Harlow K, Hampton R. HRD4/NPL4 is required for the proteasomal processing of ubiquitinated ER proteins. Mol Biol Cell. 2001;12:4114-28 pubmed
    ..We also found that each member of the Cdc48p-Ufd1p-Npl4p complex is individually required for ERAD. ..
  27. Jarosch E, Taxis C, Volkwein C, Bordallo J, Finley D, Wolf D, et al. Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48. Nat Cell Biol. 2002;4:134-9 pubmed
    ..Instead, a related AAA complex Cdc48, is required for ER-associated protein degradation upstream of the proteasome.
  28. Krick R, Bremer S, Welter E, Schlotterhose P, Muehe Y, Eskelinen E, et al. Cdc48/p97 and Shp1/p47 regulate autophagosome biogenesis in concert with ubiquitin-like Atg8. J Cell Biol. 2010;190:965-73 pubmed publisher
    ..We identify the Saccharomyces cerevisiae AAA-adenosine triphosphatase Cdc48 and its substrate-recruiting cofactor Shp1/Ubx1 as novel components needed for autophagosome biogenesis...
  29. Lipson C, Alalouf G, Bajorek M, Rabinovich E, Atir Lande A, Glickman M, et al. A proteasomal ATPase contributes to dislocation of endoplasmic reticulum-associated degradation (ERAD) substrates. J Biol Chem. 2008;283:7166-75 pubmed publisher
    ..involvement in ERAD reveals that it participates in CPY*-HA dislocation, a function previously attributed to p97/Cdc48, another AAA-ATPase essential for ERAD of CPY*-HA but dispensable for proteasomal degradation of DeltassCPY*-GFP...
  30. Alberts S, Sonntag C, Schafer A, Wolf D. Ubx4 modulates cdc48 activity and influences degradation of misfolded proteins of the endoplasmic reticulum. J Biol Chem. 2009;284:16082-9 pubmed publisher
    ..they are extracted from the cytosolic side of the ER membrane through a complex consisting of the AAA ATPase Cdc48 (p97 in mammals), Ufd1, and Npl4. This complex delivers misfolded proteins to the proteasome for final degradation...
  31. Schuberth C, Richly H, Rumpf S, Buchberger A. Shp1 and Ubx2 are adaptors of Cdc48 involved in ubiquitin-dependent protein degradation. EMBO Rep. 2004;5:818-24 pubmed
    Known activities of the ubiquitin-selective AAA ATPase Cdc48 (p97) require one of the mutually exclusive cofactors Ufd1/Npl4 and Shp1 (p47)...
  32. Cao K, Nakajima R, Meyer H, Zheng Y. The AAA-ATPase Cdc48/p97 regulates spindle disassembly at the end of mitosis. Cell. 2003;115:355-67 pubmed
    ..Here, we report that the AAA-ATPase Cdc48/p97 and its adapters Ufd1-Npl4, which have a well-established role in membrane functions, also regulate spindle ..
  33. Goder V, Carvalho P, Rapoport T. The ER-associated degradation component Der1p and its homolog Dfm1p are contained in complexes with distinct cofactors of the ATPase Cdc48p. FEBS Lett. 2008;582:1575-80 pubmed publisher
    ..These data suggest distinct functions for the Der1p and Dfm1p complexes. ..
  34. Stein A, Ruggiano A, Carvalho P, Rapoport T. Key steps in ERAD of luminal ER proteins reconstituted with purified components. Cell. 2014;158:1375-1388 pubmed publisher
    ..Cdc48p-dependent membrane extraction of polyubiquitinated proteins can be reproduced with reconstituted proteoliposomes. Our results suggest a model for retrotranslocation in which Hrd1p forms a membrane conduit for misfolded proteins. ..
  35. Braun R, Zischka H, Madeo F, Eisenberg T, Wissing S, Buttner S, et al. Crucial mitochondrial impairment upon CDC48 mutation in apoptotic yeast. J Biol Chem. 2006;281:25757-67 pubmed
    Mutation in CDC48 (cdc48(S565G)), a gene essential in the endo-plasmic reticulum (ER)-associated protein degradation (ERAD) pathway, led to the discovery of apoptosis as a mechanism of cell death in the unicellular organism Saccharomyces ..
  36. Fröhlich K, Fries H, Peters J, Mecke D. The ATPase activity of purified CDC48p from Saccharomyces cerevisiae shows complex dependence on ATP-, ADP-, and NADH-concentrations and is completely inhibited by NEM. Biochim Biophys Acta. 1995;1253:25-32 pubmed
    ..By electron microscopy, the enzyme was shown to consist of hexameric ring structures similar to its vertebrate homologue. ..
  37. Maculins T, Nkosi P, Nishikawa H, Labib K. Tethering of SCF(Dia2) to the Replisome Promotes Efficient Ubiquitylation and Disassembly of the CMG Helicase. Curr Biol. 2015;25:2254-9 pubmed publisher
    ..ubiquitylation of the CMG helicase at the end of replication, leading to a disassembly pathway that requires the Cdc48 segregase...
  38. Maric M, Maculins T, De Piccoli G, Labib K. Cdc48 and a ubiquitin ligase drive disassembly of the CMG helicase at the end of DNA replication. Science. 2014;346:1253596 pubmed publisher
    ..The Cdc48/p97 segregase then associates with ubiquitylated CMG, leading rapidly to helicase disassembly...
  39. Buchan J, Kolaitis R, Taylor J, Parker R. Eukaryotic stress granules are cleared by autophagy and Cdc48/VCP function. Cell. 2013;153:1461-74 pubmed publisher
    ..Analyses of such mutants, including CDC48 alleles, provide evidence that stress granules can be targeted to the vacuole by autophagy, in a process termed ..
  40. Tran J, Brodsky J. The Cdc48-Vms1 complex maintains 26S proteasome architecture. Biochem J. 2014;458:459-67 pubmed publisher
    ..After modification with ubiquitin, substrates are escorted to the proteasome by myriad factors, including Cdc48 (cell-division cycle 48)...
  41. Kimura Y, Yashiroda H, Kudo T, Koitabashi S, Murata S, Kakizuka A, et al. An inhibitor of a deubiquitinating enzyme regulates ubiquitin homeostasis. Cell. 2009;137:549-59 pubmed publisher
    ..We propose that free ubiquitin chains function as a ubiquitin reservoir that allows maintenance of monomeric ubiquitins at adequate levels under normal conditions and rapid supply for substrate conjugation under stress conditions. ..
  42. Stingele J, Schwarz M, Bloemeke N, Wolf P, Jentsch S. A DNA-dependent protease involved in DNA-protein crosslink repair. Cell. 2014;158:327-338 pubmed publisher
    ..Thus, our data suggest that Wss1 contributes to survival of DPC-harboring cells by acting on DPCs proteolytically. We propose that DPC proteolysis enables repair of these unique lesions via downstream canonical DNA repair pathways. ..
  43. Nakatsukasa K, Brodsky J, Kamura T. A stalled retrotranslocation complex reveals physical linkage between substrate recognition and proteasomal degradation during ER-associated degradation. Mol Biol Cell. 2013;24:1765-75, S1-8 pubmed publisher
    ..We propose that the actions of Cdc48p/p97 and the proteasome are tightly coupled during ERAD. Our data also support a model in which the Hrd1 complex links substrate recognition and degradation on opposite sides of the ER membrane. ..
  44. Messick T, Russell N, Iwata A, Sarachan K, Shiekhattar R, Shanks J, et al. Structural basis for ubiquitin recognition by the Otu1 ovarian tumor domain protein. J Biol Chem. 2008;283:11038-49 pubmed publisher
    ..We also show that Otu1 interacts with Cdc48, a regulator of the ER-associated degradation pathway...
  45. Wilson J, Liu Y, Bentivoglio C, Barlowe C. Sel1p/Ubx2p participates in a distinct Cdc48p-dependent endoplasmic reticulum-associated degradation pathway. Traffic. 2006;7:1213-23 pubmed
    ..Based on these findings, we conclude that Sel1p operates in the ERAD pathway by coupling Cdc48p to ER membranes and that Shp1p acts in a distinct Cdc48p-dependent protein degradation pathway...
  46. Howard G, Tansey W. Interaction of Gcn4 with target gene chromatin is modulated by proteasome function. Mol Biol Cell. 2016;27:2735-41 pubmed publisher
    ..effect of proteasome inhibition on Gcn4 activity is suppressed by mutations in the ubiquitin-selective chaperone Cdc48, revealing that proteolysis per se is not required for Gcn4 activity...
  47. Bosis E, Salomon D, Ohayon O, Sivan G, Bar Nun S, Rabinovich E. Ssz1 restores endoplasmic reticulum-associated protein degradation in cells expressing defective cdc48-ufd1-npl4 complex by upregulating cdc48. Genetics. 2010;184:695-706 pubmed publisher
    ..We identified SSZ1 in genetic screens for cdc48-10 suppressors and show that it upregulates Cdc48p via the pleiotropic drug resistance (PDR) network...
  48. Yen J, Flick K, Papagiannis C, Mathur R, Tyrrell A, Ouni I, et al. Signal-induced disassembly of the SCF ubiquitin ligase complex by Cdc48/p97. Mol Cell. 2012;48:288-97 pubmed publisher
    ..We show that cadmium stress induces selective recruitment of the AAA(+) ATPase Cdc48/p97 to catalyze dissociation of the F-box subunit from the yeast SCF(Met30) ligase to block substrate ..
  49. Gödderz D, Giovannucci T, Lalakova J, Menendez Benito V, Dantuma N. The deubiquitylating enzyme Ubp12 regulates Rad23-dependent proteasomal degradation. J Cell Sci. 2017;130:3336-3346 pubmed publisher
    The consecutive actions of the ubiquitin-selective segregase Cdc48 and the ubiquitin shuttle factor Rad23 result in the delivery of ubiquitylated proteins at the proteasome...
  50. Böhm S, Buchberger A. The budding yeast Cdc48(Shp1) complex promotes cell cycle progression by positive regulation of protein phosphatase 1 (Glc7). PLoS ONE. 2013;8:e56486 pubmed publisher
    The conserved, ubiquitin-selective AAA ATPase Cdc48 regulates numerous cellular processes including protein quality control, DNA repair and the cell cycle...
  51. Patel S, Indig F, Olivieri N, Levine N, Latterich M. Organelle membrane fusion: a novel function for the syntaxin homolog Ufe1p in ER membrane fusion. Cell. 1998;92:611-20 pubmed
  52. Ng W, Sergeyenko T, Zeng N, Brown J, Römisch K. Characterization of the proteasome interaction with the Sec61 channel in the endoplasmic reticulum. J Cell Sci. 2007;120:682-91 pubmed
    ..Mutations in the ATP-binding sites of individual Rpt proteins all reduced the affinity of 19S complexes for the ER, suggesting that the 19S base in the ATP-bound conformation docks at the Sec61 channel. ..
  53. Metzger M, Maurer M, Dancy B, Michaelis S. Degradation of a cytosolic protein requires endoplasmic reticulum-associated degradation machinery. J Biol Chem. 2008;283:32302-16 pubmed publisher
  54. Esaki M, Ogura T. Cdc48p/p97-mediated regulation of mitochondrial morphology is Vms1p-independent. J Struct Biol. 2012;179:112-20 pubmed publisher
    ..These results suggest that Cdc48p controls mitochondrial morphology by regulating turnover of proteins involved in mitochondrial morphology in a Vms1p-independent manner. ..
  55. Qiu L, Pashkova N, Walker J, Winistorfer S, Allali Hassani A, Akutsu M, et al. Structure and function of the PLAA/Ufd3-p97/Cdc48 complex. J Biol Chem. 2010;285:365-72 pubmed publisher
    ..In yeast, loss of Doa1 is suppressed by altering p97/Cdc48 function indicating that physical interaction between PLAA and p97 is functionally important...
  56. Gnann A, Riordan J, Wolf D. Cystic fibrosis transmembrane conductance regulator degradation depends on the lectins Htm1p/EDEM and the Cdc48 protein complex in yeast. Mol Biol Cell. 2004;15:4125-35 pubmed
    ..These proteins also were found to be necessary for ERAD of a mutated yeast "relative" of CFTR, Pdr5(*)p. ..
  57. Li M, Koshi T, Emr S. Membrane-anchored ubiquitin ligase complex is required for the turnover of lysosomal membrane proteins. J Cell Biol. 2015;211:639-52 pubmed publisher
    ..Our study demonstrated that the Dsc complex can function at the vacuole to regulate the composition and lifetime of vacuolar membrane proteins. ..
  58. Nita Lazar M, Lennarz W. Pkc1p modifies CPY* degradation in the ERAD pathway. Biochem Biophys Res Commun. 2005;332:357-61 pubmed
    ..In addition, we show that Cdc48p interacts in the cytosol with the deglycosylation enzyme, PNGase, only when Cdc48p is associated with a misfolded glycoprotein. ..
  59. Ndoja A, Cohen R, Yao T. Ubiquitin signals proteolysis-independent stripping of transcription factors. Mol Cell. 2014;53:893-903 pubmed publisher
    ..We identify the AAA(+) ATPase Cdc48 and its cofactors as the Ub receptor responsible for extracting the monoubiquitinated activator from DNA...
  60. Bagola K, von Delbrück M, Dittmar G, Scheffner M, Ziv I, Glickman M, et al. Ubiquitin binding by a CUE domain regulates ubiquitin chain formation by ERAD E3 ligases. Mol Cell. 2013;50:528-39 pubmed publisher
    ..Hence, we demonstrate an unexpected function of a UBD in the regulation of ubiquitin chain synthesis. ..
  61. Defenouillère Q, Yao Y, Mouaikel J, Namane A, Galopier A, Decourty L, et al. Cdc48-associated complex bound to 60S particles is required for the clearance of aberrant translation products. Proc Natl Acad Sci U S A. 2013;110:5046-51 pubmed publisher
    ..and ribosome quality control 1 (Rqc1), two factors that we found associated, together with Ltn1 and the AAA-ATPase Cdc48, to 60S ribosomal subunits...
  62. Mandal A, Gibney P, Nillegoda N, Theodoraki M, Caplan A, Morano K. Hsp110 chaperones control client fate determination in the hsp70-Hsp90 chaperone system. Mol Biol Cell. 2010;21:1439-48 pubmed publisher
    ..These findings support a model in which Hsp110 chaperones contribute significantly to the decision made by Hsp70 to fold or degrade a client protein. ..
  63. Heo J, Nielson J, Dephoure N, Gygi S, Rutter J. Intramolecular interactions control Vms1 translocation to damaged mitochondria. Mol Biol Cell. 2013;24:1263-73 pubmed publisher
    ..We previously demonstrated that VCP/Cdc48-associated mitochondrial stress responsive 1 (Vms1) is a component of a mitochondrial surveillance system that ..
  64. Stapf C, Cartwright E, Bycroft M, Hofmann K, Buchberger A. The general definition of the p97/valosin-containing protein (VCP)-interacting motif (VIM) delineates a new family of p97 cofactors. J Biol Chem. 2011;286:38670-8 pubmed publisher
    ..depends on the physical interaction between its VIM and the critical N domain residues of the yeast p97 homolog, Cdc48. Thus, the VIM-N domain interaction characterized in this study is required for the physiological function of Vms1 ..
  65. Felberbaum R, Wilson N, Cheng D, Peng J, Hochstrasser M. Desumoylation of the endoplasmic reticulum membrane VAP family protein Scs2 by Ulp1 and SUMO regulation of the inositol synthesis pathway. Mol Cell Biol. 2012;32:64-75 pubmed publisher
    ..These results provide the first evidence of cross-regulation between the SUMO and inositol pathways, including the sumoylation of an ER membrane protein central to phospholipid synthesis and phosphoinositide signaling...
  66. Braun S, Jentsch S. SM-protein-controlled ER-associated degradation discriminates between different SNAREs. EMBO Rep. 2007;8:1176-82 pubmed
    ..Thus, our findings identify Sly1 as a discriminating regulator of SNARE levels and indicate that Sly1-controlled ERAD might regulate the balance between different Qa-SNARE proteins. ..
  67. Mirzaei H, Rogers R, Grimes B, Eng J, Aderem A, Aebersold R. Characterizing the connectivity of poly-ubiquitin chains by selected reaction monitoring mass spectrometry. Mol Biosyst. 2010;6:2004-14 pubmed publisher
    ..cerevisiae. We then applied the method to detect toxin induced changes in the poly-ubiquitination profile in complex and enriched protein samples. ..