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Gene Review

HRD3  -  ubiquitin ligase complex subunit HRD3

Saccharomyces cerevisiae S288c

Synonyms: ERAD-associated E3 ubiquitin-protein ligase component HRD3, HMG-CoA reductase degradation protein 3, YLR207W
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High impact information on HRD3

  • We further demonstrate that Yos9p, together with Kar2p and Hrd3p, forms a luminal surveillance complex that both recruits nonnative proteins to the core ERAD machinery and assists a distinct sugar-dependent step necessary to commit substrates for degradation [1].
  • Therefore, we propose that Hrd3p acts as a substrate recruitment factor for the Hrd1p ligase complex [2].
  • We have identified a new pathway of ER-associated degradation in Saccharomyces cerevisiae that functions separately from the HRD/DER pathway comprised of Hrd1p, Hrd3p, Der1p, and Ubc7p [3].
  • Endoplasmic reticulum degradation requires lumen to cytosol signaling. Transmembrane control of Hrd1p by Hrd3p [4].
  • This machinery includes ER membrane proteins Hrd1p/Der3p and Hrd3p and the ER-associated ubiquitin-conjugating enzymes Ubc7p and Ubc6p [5].

Anatomical context of HRD3


Associations of HRD3 with chemical compounds

  • In this paper, we show that the product of EKS1/HRD3 is a type-I transmembrane glycoprotein and resides in the ER [7].

Physical interactions of HRD3


Other interactions of HRD3

  • In contrast, HRD1 and HRD3 genes encoded previously unknown proteins predicted to be membrane bound [9].
  • EKS1 turns out to be identical to HRD3, which was independently isolated as a gene implicated in the degradation of an HMG-CoA reductase isozyme, Hmg2p [7].
  • The eks1/hrd3 disrupted cells are normal in growth and transport of cargo proteins, but missecrete BiP (Kar2p) [7].


  1. A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation. Denic, V., Quan, E.M., Weissman, J.S. Cell (2006) [Pubmed]
  2. The Hrd1p ligase complex forms a linchpin between ER-lumenal substrate selection and Cdc48p recruitment. Gauss, R., Sommer, T., Jarosch, E. EMBO J. (2006) [Pubmed]
  3. An HRD/DER-independent ER quality control mechanism involves Rsp5p-dependent ubiquitination and ER-Golgi transport. Haynes, C.M., Caldwell, S., Cooper, A.A. J. Cell Biol. (2002) [Pubmed]
  4. Endoplasmic reticulum degradation requires lumen to cytosol signaling. Transmembrane control of Hrd1p by Hrd3p. Gardner, R.G., Swarbrick, G.M., Bays, N.W., Cronin, S.R., Wilhovsky, S., Seelig, L., Kim, C., Hampton, R.Y. J. Cell Biol. (2000) [Pubmed]
  5. HRD gene dependence of endoplasmic reticulum-associated degradation. Wilhovsky, S., Gardner, R., Hampton, R. Mol. Biol. Cell (2000) [Pubmed]
  6. Genetic interactions of Hrd3p and Der3p/Hrd1p with Sec61p suggest a retro-translocation complex mediating protein transport for ER degradation. Plemper, R.K., Bordallo, J., Deak, P.M., Taxis, C., Hitt, R., Wolf, D.H. J. Cell. Sci. (1999) [Pubmed]
  7. Identification of SEC12, SED4, truncated SEC16, and EKS1/HRD3 as multicopy suppressors of ts mutants of Sar1 GTPase. Saito, Y., Yamanushi, T., Oka, T., Nakano, A. J. Biochem. (1999) [Pubmed]
  8. ER signaling in unfolded protein response. Kaneko, M., Nomura, Y. Life Sci. (2003) [Pubmed]
  9. Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein. Hampton, R.Y., Gardner, R.G., Rine, J. Mol. Biol. Cell (1996) [Pubmed]
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