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Retrotranslocation of a misfolded luminal ER protein by the ubiquitin-ligase Hrd1p.

Carvalho P, Stanley AM, Rapoport TA.

Cell. 2010 Nov 12;143(4):579-91. doi: 10.1016/j.cell.2010.10.028.


Key steps in ERAD of luminal ER proteins reconstituted with purified components.

Stein A, Ruggiano A, Carvalho P, Rapoport TA.

Cell. 2014 Sep 11;158(6):1375-88. doi: 10.1016/j.cell.2014.07.050.


The Hrd1p ligase complex forms a linchpin between ER-lumenal substrate selection and Cdc48p recruitment.

Gauss R, Sommer T, Jarosch E.

EMBO J. 2006 May 3;25(9):1827-35. Epub 2006 Apr 13.


Usa1p is required for optimal function and regulation of the Hrd1p endoplasmic reticulum-associated degradation ubiquitin ligase.

Carroll SM, Hampton RY.

J Biol Chem. 2010 Feb 19;285(8):5146-56. doi: 10.1074/jbc.M109.067876. Epub 2009 Nov 24.


In vitro analysis of Hrd1p-mediated retrotranslocation of its multispanning membrane substrate 3-hydroxy-3-methylglutaryl (HMG)-CoA reductase.

Garza RM, Sato BK, Hampton RY.

J Biol Chem. 2009 May 29;284(22):14710-22. doi: 10.1074/jbc.M809607200. Epub 2009 Mar 26.


Recognition of an ERAD-L substrate analyzed by site-specific in vivo photocrosslinking.

Stanley AM, Carvalho P, Rapoport T.

FEBS Lett. 2011 May 6;585(9):1281-6. doi: 10.1016/j.febslet.2011.04.009. Epub 2011 Apr 8.


Misfolded membrane proteins are specifically recognized by the transmembrane domain of the Hrd1p ubiquitin ligase.

Sato BK, Schulz D, Do PH, Hampton RY.

Mol Cell. 2009 Apr 24;34(2):212-22. doi: 10.1016/j.molcel.2009.03.010.


Cytosolic entry of Shiga-like toxin a chain from the yeast endoplasmic reticulum requires catalytically active Hrd1p.

Li S, Spooner RA, Hampton RY, Lord JM, Roberts LM.

PLoS One. 2012;7(7):e41119. doi: 10.1371/journal.pone.0041119. Epub 2012 Jul 19.


Genetic interactions of Hrd3p and Der3p/Hrd1p with Sec61p suggest a retro-translocation complex mediating protein transport for ER degradation.

Plemper RK, Bordallo J, Deak PM, Taxis C, Hitt R, Wolf DH.

J Cell Sci. 1999 Nov;112 ( Pt 22):4123-34.


Autoubiquitination of the Hrd1 Ligase Triggers Protein Retrotranslocation in ERAD.

Baldridge RD, Rapoport TA.

Cell. 2016 Jul 14;166(2):394-407. doi: 10.1016/j.cell.2016.05.048. Epub 2016 Jun 16.


Endoplasmic reticulum degradation requires lumen to cytosol signaling. Transmembrane control of Hrd1p by Hrd3p.

Gardner RG, Swarbrick GM, Bays NW, Cronin SR, Wilhovsky S, Seelig L, Kim C, Hampton RY.

J Cell Biol. 2000 Oct 2;151(1):69-82.


Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multispanning membrane protein and a soluble luminal protein.

Huyer G, Piluek WF, Fansler Z, Kreft SG, Hochstrasser M, Brodsky JL, Michaelis S.

J Biol Chem. 2004 Sep 10;279(37):38369-78. Epub 2004 Jul 12.


Yos9p and Hrd1p mediate ER retention of misfolded proteins for ER-associated degradation.

Izawa T, Nagai H, Endo T, Nishikawa S.

Mol Biol Cell. 2012 Apr;23(7):1283-93. doi: 10.1091/mbc.E11-08-0722. Epub 2012 Feb 1.


A stalled retrotranslocation complex reveals physical linkage between substrate recognition and proteasomal degradation during ER-associated degradation.

Nakatsukasa K, Brodsky JL, Kamura T.

Mol Biol Cell. 2013 Jun;24(11):1765-75, S1-8. doi: 10.1091/mbc.E12-12-0907. Epub 2013 Mar 27.


Previously unknown role for the ubiquitin ligase Ubr1 in endoplasmic reticulum-associated protein degradation.

Stolz A, Besser S, Hottmann H, Wolf DH.

Proc Natl Acad Sci U S A. 2013 Sep 17;110(38):15271-6. doi: 10.1073/pnas.1304928110. Epub 2013 Aug 29.


Folding-competent and folding-defective forms of ricin A chain have different fates after retrotranslocation from the endoplasmic reticulum.

Li S, Spooner RA, Allen SC, Guise CP, Ladds G, Schnöder T, Schmitt MJ, Lord JM, Roberts LM.

Mol Biol Cell. 2010 Aug 1;21(15):2543-54. doi: 10.1091/mbc.E09-08-0743. Epub 2010 Jun 2.


SEL1L protein critically determines the stability of the HRD1-SEL1L endoplasmic reticulum-associated degradation (ERAD) complex to optimize the degradation kinetics of ERAD substrates.

Iida Y, Fujimori T, Okawa K, Nagata K, Wada I, Hosokawa N.

J Biol Chem. 2011 May 13;286(19):16929-39. doi: 10.1074/jbc.M110.215871. Epub 2011 Mar 24.

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