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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Synovial apoptosis inhibitor 1, synoviolin

HRD1, Hrd1p, Synoviolin, Der3
This gene encodes a protein involved in endoplasmic reticulum (ER)-associated degradation. The encoded protein removes unfolded proteins, accumulated during ER stress, by retrograde transport to the cytosol from the ER. This protein also uses the ubiquitin-proteasome system for additional degradation of unfolded proteins. Sequence analysis identified two transcript variants that encode different isoforms. [provided by RefSeq, May 2011] (from NCBI)
Top mentioned proteins: Ubiquitin, V1a, SEL1L, CAN, UBC7
Papers on HRD1
Association of the SEL1L protein transmembrane domain with HRD1 ubiquitin ligase regulates ERAD-L.
New
Wada et al., Kyoto, Japan. In Febs J, Jan 2016
Mammalian HRD1, an integral membrane ubiquitin ligase that ubiquitinates ERAD substrates, forms a large assembly in the ER membrane including SEL1L, a single-pass membrane protein, and additional components.
HRD1 suppresses the growth and metastasis of breast cancer cells by promoting IGF-1R degradation.
New
Su et al., Nanjing, China. In Oncotarget, Jan 2016
HRD1 (3-hydroxy-3-methylglutaryl reductase degradation) is an E3 ubiquitin ligase.
Epithelial Sel1L is required for the maintenance of intestinal homeostasis.
New
Qi et al., South Brisbane, Australia. In Mol Biol Cell, Jan 2016
Here we show that the expression of SEL1L and HRD1, the most conserved branch of mammalian ERAD, is significantly reduced in ileal Crohn's disease (CD).
gp78 functions downstream of Hrd1 to promote degradation of misfolded proteins of the endoplasmic reticulum.
New
Ye et al., Bethesda, United States. In Mol Biol Cell, Jan 2016
Hrd1 and gp78 are mammalian ubiquitin ligases homologous to Hrd1p, an ubiquitin ligase essential for ERAD in Saccharomyces cerevisiae.
Identifying the ERAD ubiquitin E3 ligases for viral and cellular targeting of MHC class I.
Review
New
Lehner et al., Cambridge, United Kingdom. In Mol Immunol, Dec 2015
Free US11 either rebinds more MHC-I or is itself degraded by the HRD1/SEL1L E3 ligase complex.
Selective multifaceted E3 ubiquitin ligases barricade extreme defense: Potential therapeutic targets for neurodegeneration and ageing.
Review
New
Mishra et al., Jodhpur, India. In Ageing Res Rev, Nov 2015
Here, we review recent literature on the roles of E6-AP, HRD1 and ITCH E3 ubiquitin ligases in the neuro-pathobiological mechanisms, with precise focus on the processes of neurodegeneration, and thereby propose new lines of potential targets for therapeutic interventions.
Loss of p53 enhances the function of the endoplasmic reticulum through activation of the IRE1α/XBP1 pathway.
New
Lee et al., Kōchi, Japan. In Oncotarget, Sep 2015
We also show that wild-type p53 interacts with synoviolin (SYVN1)/HRD1/DER3, a transmembrane E3 ubiquitin ligase localized to ER during ER stress and removes unfolded proteins by reversing transport to the cytosol from the ER, and its interaction stimulates IRE1α degradation.
Molecular mechanisms of Nrf2 regulation and how these influence chemical modulation for disease intervention.
Review
New
Zhang et al., Tucson, United States. In Biochem Soc Trans, Sep 2015
Recently, both beta-transducin repeat-containing E3 ubiquitin protein ligase (β-TrCP) and E3 ubiquitin-protein ligase synoviolin (Hrd1) have been identified as novel E3 ubiquitin ligases that negatively regulate Nrf2 through Keap1-independent mechanisms.
The Keap1/Nrf2 pathway in health and disease: from the bench to the clinic.
Review
New
Hayes et al., Dundee, United Kingdom. In Biochem Soc Trans, Sep 2015
Regulation of Nrf2 is complex and although much attention has focussed on its repression by Kelch-like ECH-associated protein-1 (Keap1), recently it has become increasingly apparent that it is also controlled by cross-talk with other signalling pathways including the glycogen synthase kinase-3 (GSK-3)-β-transducin repeat-containing protein (β-TrCP) axis, ERAD (endoplasmic reticulum-associated degradation)-associated E3 ubiquitin-protein ligase (Hrd1, also called synoviolin), nuclear factor-kappa B (NF-κB), Notch and AMP kinase.
Endoplasmic reticulum quality control in cancer: Friend or foe.
Review
New
Qi et al., Ithaca, United States. In Semin Cancer Biol, Aug 2015
Here we review recent advances in our understanding of the complex relationship between ER proteostasis and cancer pathology, with a focus on the two most conserved ER quality-control mechanisms--the IRE1α-XBP1 pathway of the UPR and SEL1L-HRD1 complex of the ERAD.
Key steps in ERAD of luminal ER proteins reconstituted with purified components.
Impact
Rapoport et al., Boston, United States. In Cell, 2014
Here, we use purified components from Saccharomyces cerevisiae to analyze the mechanism of retrotranslocation of luminal substrates (ERAD-L), recapitulating key steps in a basic process in which the ubiquitin ligase Hrd1p is the only required membrane protein.
The protein quality control system manages plant defence compound synthesis.
Impact
Goossens et al., Gent, Belgium. In Nature, 2014
This control apparatus is equivalent to the ERAD system that regulates sterol synthesis in yeasts and mammals but that uses distinct E3 ubiquitin ligases, of the HMGR degradation 1 (HRD1) type, to direct destruction of HMGR.
Aberrant substrate engagement of the ER translocon triggers degradation by the Hrd1 ubiquitin ligase.
GeneRIF
Hochstrasser et al., New Haven, United States. In J Cell Biol, 2012
Hrd1 therefore likely plays a general role in targeting proteins that persistently associate with and potentially obstruct the translocon.
Yos9p and Hrd1p mediate ER retention of misfolded proteins for ER-associated degradation.
GeneRIF
Nishikawa et al., Nagoya, Japan. In Mol Biol Cell, 2012
Yos9p and Hrd1p mediate ER retention of misfolded proteins in the early stage of ERAD, which constitutes a process separable from the later degradation step.
Hrd1 facilitates tau degradation and promotes neuron survival.
GeneRIF
Zhou et al., Hefei, China. In Curr Mol Med, 2012
Hrd1 functions as an E3 targeting tau or abnormal p-tau for proteasome degradation.
Derlin-1 deficiency is embryonic lethal, Derlin-3 deficiency appears normal, and Herp deficiency is intolerant to glucose load and ischemia in mice.
GeneRIF
Kokame et al., Suita, Japan. In Plos One, 2011
Derlin-1 deficiency is embryonic lethal, Derlin-3 deficiency appears normal, and Herp deficiency is intolerant to glucose load and ischemia in mice
Expression of the ubiquitin ligase HRD1 in neural stem/progenitor cells of the adult mouse brain.
GeneRIF
Okuma et al., Chiba, Japan. In J Pharmacol Sci, 2010
HRD1 is colocated with the neural stem cell marker protein nestin and glial fibrillary acidic protein in the endoplasmic reticulum membrane of the NSCs of the subventricular zone (SVZ astrocytes) but in the cell nucleus of in the dentate gyrus
Retrotranslocation of a misfolded luminal ER protein by the ubiquitin-ligase Hrd1p.
Impact
GeneRIF
Rapoport et al., Boston, United States. In Cell, 2010
Study shows that Hrd1p is the central membrane component in ERAD-L; its overexpression bypasses the need for the other components of the Hrd1p complex.
A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation.
Impact
Weissman et al., San Francisco, United States. In Cell, 2006
Here we show that Yos9p is part of a stable complex that organizes key components of ERAD machinery on both sides of the ER membrane, including the transmembrane ubiquitin ligase Hrd1p.
Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins.
Impact
Rapoport et al., Boston, United States. In Cell, 2006
Proteins with misfolded ER-luminal domains use the ERAD-L pathway, in which the Hrd1p/Hrd3p ligase forms a near stoichiometric membrane core complex by binding to Der1p via the linker protein Usa1p.
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