CDC48-NPL4-UFD1 AAA ATPase complex

CDC48-NPL4-UFD1 AAA ATPase complex Literature

Unique References: 28
Aliases: CDC48(UFD1/NPL4) complex , Cdc48-Ufd1-Npl4 complex , Cdc48p-Npl4p-Ufd1p AAA ATPase complex , UNC complex , Ufd1-Npl4-Cdc48/p97 (UNC) complex

Primary Literature

Li H, et al. (2024) Bidirectional substrate shuttling between the 26S proteasome and the Cdc48 ATPase promotes protein degradation. Mol Cell. PMID: 38401542
Lee HG, et al. (2023) SUMO enhances unfolding of SUMO-polyubiquitin-modified substrates by the Ufd1/Npl4/Cdc48 complex. Proc Natl Acad Sci U S A 120(1):e2213703120 PMID: 36574706
Oppenheim T, et al. (2023) The Cdc48 N-terminal domain has a molecular switch that mediates the Npl4-Ufd1-Cdc48 complex formation. Structure 31(7):764-779.e8 PMID: 37311459
Ohkuni K, et al. (2022) Cdc48Ufd1/Npl4 segregase removes mislocalized centromeric histone H3 variant CENP-A from non-centromeric chromatin. Nucleic Acids Res 50(6):3276-3291 PMID: 35234920
Deegan TD, et al. (2020) CMG helicase disassembly is controlled by replication fork DNA, replisome components and a ubiquitin threshold. Elife 9 PMID: 32804080
Higgins R, et al. (2020) The Cdc48 Complex Alleviates the Cytotoxicity of Misfolded Proteins by Regulating Ubiquitin Homeostasis. Cell Rep 32(2):107898 PMID: 32668237
Sato Y, et al. (2019) Structural insights into ubiquitin recognition and Ufd1 interaction of Npl4. Nat Commun 10(1):5708 PMID: 31836717
Twomey EC, et al. (2019) Substrate processing by the Cdc48 ATPase complex is initiated by ubiquitin unfolding. Science 365(6452) PMID: 31249135
Parisi E, et al. (2018) Cdc48/p97 segregase is modulated by cyclin-dependent kinase to determine cyclin fate during G1 progression. EMBO J 37(16) PMID: 29950310
Finley D, et al. (2012) The ubiquitin-proteasome system of Saccharomyces cerevisiae. Genetics 192(2):319-60 PMID: 23028185
Barbin L, et al. (2010) The Cdc48-Ufd1-Npl4 complex is central in ubiquitin-proteasome triggered catabolite degradation of fructose-1,6-bisphosphatase. Biochem Biophys Res Commun 394(2):335-41 PMID: 20206597
Shcherbik N and Haines DS (2007) Cdc48p(Npl4p/Ufd1p) binds and segregates membrane-anchored/tethered complexes via a polyubiquitin signal present on the anchors. Mol Cell 25(3):385-97 PMID: 17289586
Gauss R, et al. (2006) The Hrd1p ligase complex forms a linchpin between ER-lumenal substrate selection and Cdc48p recruitment. EMBO J 25(9):1827-35 PMID: 16619026
Park S, et al. (2005) Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites. Structure 13(7):995-1005 PMID: 16004872
Bays NW, et al. (2001) HRD4/NPL4 is required for the proteasomal processing of ubiquitinated ER proteins. Mol Biol Cell 12(12):4114-28 PMID: 11739805
Hitchcock AL, et al. (2001) The conserved npl4 protein complex mediates proteasome-dependent membrane-bound transcription factor activation. Mol Biol Cell 12(10):3226-41 PMID: 11598205
Rape M, et al. (2001) Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone. Cell 107(5):667-77 PMID: 11733065

Additional Literature

Lehner MH, et al. (2022) Yeast Smy2 and its human homologs GIGYF1 and -2 regulate Cdc48/VCP function during transcription stress. Cell Rep 41(4):111536 PMID: 36288698

Li J, et al. (2022) The CDC48 complex mediates ubiquitin-dependent degradation of intra-chloroplast proteins in plants. Cell Rep 39(2):110664 PMID: 35417702

Metzger MB, et al. (2020) A protein quality control pathway at the mitochondrial outer membrane. Elife 9 PMID: 32118579

Verma R, et al. (2011) Cdc48/p97 mediates UV-dependent turnover of RNA Pol II. Mol Cell 41(1):82-92 PMID: 21211725

Heo JM, et al. (2010) A stress-responsive system for mitochondrial protein degradation. Mol Cell 40(3):465-80 PMID: 21070972

Metzger MB, et al. (2008) Degradation of a cytosolic protein requires endoplasmic reticulum-associated degradation machinery. J Biol Chem 283(47):32302-16 PMID: 18812321

Rumpf S and Jentsch S (2006) Functional division of substrate processing cofactors of the ubiquitin-selective Cdc48 chaperone. Mol Cell 21(2):261-9 PMID: 16427015

Neuber O, et al. (2005) Ubx2 links the Cdc48 complex to ER-associated protein degradation. Nat Cell Biol 7(10):993-8 PMID: 16179953

Schuberth C and Buchberger A (2005) Membrane-bound Ubx2 recruits Cdc48 to ubiquitin ligases and their substrates to ensure efficient ER-associated protein degradation. Nat Cell Biol 7(10):999-1006 PMID: 16179952

Rabinovich E, et al. (2002) AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation. Mol Cell Biol 22(2):626-34 PMID: 11756557

Fröhlich KU, et al. (1995) 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 1253(1):25-32 PMID: 7492595

CDC48-NPL4-UFD1 AAA ATPase complex Literature TEXT HERE

Primary Literature TEXT HERE

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CDC48-NPL4-UFD1 AAA ATPase complex Literature

Primary Literature

Additional Literature