HRD1 E3 ubiquitin ligase complex

HRD1 E3 ubiquitin ligase complex Literature

Unique References: 31
Aliases: Hrd1p ubiquitin ligase complex , Ubiquitin ligase ERAD-L complex

Primary Literature

Nakatsukasa K, et al. (2022) A positive genetic selection for transmembrane domain mutations in HRD1 underscores the importance of Hrd1 complex integrity during ERAD. Curr Genet 68(2):227-242 PMID: 35041076
Christiano R, et al. (2020) A Systematic Protein Turnover Map for Decoding Protein Degradation. Cell Rep 33(6):108378 PMID: 33176155
Wu X, et al. (2020) Structural basis of ER-associated protein degradation mediated by the Hrd1 ubiquitin ligase complex. Science 368(6489) PMID: 32327568
Schoebel S, et al. (2017) Cryo-EM structure of the protein-conducting ERAD channel Hrd1 in complex with Hrd3. Nature 548(7667):352-355 PMID: 28682307
Mehnert M, et al. (2014) Der1 promotes movement of misfolded proteins through the endoplasmic reticulum membrane. Nat Cell Biol 16(1):77-86 PMID: 24292014
Finley D, et al. (2012) The ubiquitin-proteasome system of Saccharomyces cerevisiae. Genetics 192(2):319-60 PMID: 23028185
Izawa T, et al. (2012) Yos9p and Hrd1p mediate ER retention of misfolded proteins for ER-associated degradation. Mol Biol Cell 23(7):1283-93 PMID: 22298424
Horn SC, et al. (2009) Usa1 functions as a scaffold of the HRD-ubiquitin ligase. Mol Cell 36(5):782-93 PMID: 20005842
Carvalho P, et al. (2006) Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins. Cell 126(2):361-73 PMID: 16873066
Denic V, et al. (2006) A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation. Cell 126(2):349-59 PMID: 16873065
Wilson JD, et al. (2006) Sel1p/Ubx2p participates in a distinct Cdc48p-dependent endoplasmic reticulum-associated degradation pathway. Traffic 7(9):1213-23 PMID: 16919153

Additional Literature

Michaelis AC, et al. (2023) The social and structural architecture of the yeast protein interactome. Nature 624(7990):192-200 PMID: 37968396

Stein A, et al. (2014) Key steps in ERAD of luminal ER proteins reconstituted with purified components. Cell 158(6):1375-1388 PMID: 25215493

Zattas D, et al. (2013) N-terminal acetylation of the yeast Derlin Der1 is essential for Hrd1 ubiquitin-ligase activity toward luminal ER substrates. Mol Biol Cell 24(7):890-900 PMID: 23363603

Hanna J, et al. (2012) Structural and biochemical basis of Yos9 protein dimerization and possible contribution to self-association of 3-hydroxy-3-methylglutaryl-coenzyme A reductase degradation ubiquitin-ligase complex. J Biol Chem 287(11):8633-40 PMID: 22262864

Goder V, et al. (2008) The ER-associated degradation component Der1p and its homolog Dfm1p are contained in complexes with distinct cofactors of the ATPase Cdc48p. FEBS Lett 582(11):1575-80 PMID: 18407841

Bazirgan OA, et al. (2006) Determinants of RING-E2 fidelity for Hrd1p, a membrane-anchored ubiquitin ligase. J Biol Chem 281(51):38989-9001 PMID: 17035235

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

Bhamidipati A, et al. (2005) Exploration of the topological requirements of ERAD identifies Yos9p as a lectin sensor of misfolded glycoproteins in the ER lumen. Mol Cell 19(6):741-51 PMID: 16168370

Kim W, et al. (2005) Yos9p detects and targets misfolded glycoproteins for ER-associated degradation. Mol Cell 19(6):753-64 PMID: 16168371

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

Szathmary R, et al. (2005) Yos9 protein is essential for degradation of misfolded glycoproteins and may function as lectin in ERAD. Mol Cell 19(6):765-75 PMID: 16168372

Schuberth C, et al. (2004) Shp1 and Ubx2 are adaptors of Cdc48 involved in ubiquitin-dependent protein degradation. EMBO Rep 5(8):818-24 PMID: 15258615

Haynes CM, et al. (2002) An HRD/DER-independent ER quality control mechanism involves Rsp5p-dependent ubiquitination and ER-Golgi transport. J Cell Biol 158(1):91-101 PMID: 12105183

Bays NW, et al. (2001) Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation. Nat Cell Biol 3(1):24-9 PMID: 11146622

Deak PM and Wolf DH (2001) Membrane topology and function of Der3/Hrd1p as a ubiquitin-protein ligase (E3) involved in endoplasmic reticulum degradation. J Biol Chem 276(14):10663-9 PMID: 11139575

Gardner RG, et al. (2001) In vivo action of the HRD ubiquitin ligase complex: mechanisms of endoplasmic reticulum quality control and sterol regulation. Mol Cell Biol 21(13):4276-91 PMID: 11390656

Knop M, et al. (1996) Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast. EMBO J 15(4):753-63 PMID: 8631297

Reviews

Piirainen MA and Frey AD (2022) The Impact of Glycoengineering on the Endoplasmic Reticulum Quality Control System in Yeasts. Front Mol Biosci 9:910709 PMID: 35720120

Zou L, et al. (2022) Viruses Hijack ERAD to Regulate Their Replication and Propagation. Int J Mol Sci 23(16) PMID: 36012666

Ninagawa S, et al. (2021) Mechanisms of productive folding and endoplasmic reticulum-associated degradation of glycoproteins and non-glycoproteins. Biochim Biophys Acta Gen Subj 1865(3):129812 PMID: 33316349

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Reviews

HRD1 E3 ubiquitin ligase complex Literature

Primary Literature

Additional Literature