Novel functions of ubiquitin ligase HRD1 with transmembrane and proline-rich domains.
Journal of Pharmacological Sciences, 2008 Human ubiquitin ligase HRD1 is involved in endoplasmic reticulum-associated degradation (ERAD). We recently reported that HRD1 interacts with Parkin-associated endothelin receptor-like receptor (Pael-R), a substrate of Parkin, and promotes Pael-R ...
Tomohiro Omura +2 more
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Correlation Between Decrease in Protein Levels of Ubiquitin Ligase HRD1 and Amyloid-β Production
Journal of Pharmacological Sciences, 2010 Endoplasmic reticulum–associated degradation (ERAD) is a quality control mechanism in which unfolded proteins are retro-translocated to the cytosol for degradation. Our recent study showed that suppression of expression of ubiquitin ligase HRD1, which is
Masayuki Kaneko, Yasunobu Okuma
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Structural basis and pathological implications of the dimeric OS9-SEL1L-HRD1 ERAD Core Complex [PDF]
Nature CommunicationsThe SEL1L-HRD1 complex represents the most conserved branch of endoplasmic reticulum (ER)-associated degradation (ERAD), a critical quality-control pathway that clears misfolded ER proteins.
Liangguang Leo Lin +4 more
doaj +3 more sources
SEL1L3 suppresses colorectal cancer cell growth and metastasis by preventing endoplasmic reticulum-associated degradation of STING [PDF]
Cell Death and DiseaseEndoplasmic reticulum associated degradation (ERAD) plays pivotal role in protein homeostasis and quality control in normal and cancer cells, yet the regulatory mechanism of ERAD remains elusive, especially regarding its ubiquitination function mediated ...
Hui Zhang +12 more
doaj +2 more sources
Molecular Oncology, 2021 Dependence on glutamine and acceleration of fatty acid oxidation (FAO) are both metabolic characteristics of triple‐negative breast cancer (TNBC). With the rapid growth of tumors, accelerated glutamine catabolism depletes local glutamine, resulting in ...
Linlin Fang +2 more
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Ubiquitin and ubiquitin-like modifications in the endoplasmic reticulum stress response. [PDF]
FEBS JEndoplasmic reticulum (ER) stress activates various proteostasis control processes, including the unfolded protein response, ribosome‐associated quality control, and ER‐associated degradation. Ubiquitin and ubiquitin‐like modifications dynamically regulate these processes to determine cell fate, promoting adaptation or inducing cell death.
Avril T, Le Gallo M, Lafont E.
europepmc +2 more sources
Ubiquitination by HRD1 is essential for TLR3 trafficking and its innate immune signaling [PDF]
Nature CommunicationsToll-like receptor 3 (TLR3), an innate immune sensor for double-stranded RNA (dsRNA), traffics from the endoplasmic reticulum (ER) after synthesis to endolysosomes for proteolytic cleavage and activation.
Lianfeng Zhao +9 more
doaj +2 more sources
Limiting ER-associated degradation capacity triggers acute and chronic effects on insulin biosynthesis [PDF]
The Journal of Clinical InvestigationIn pancreatic β cells, misfolded proinsulin is a substrate for ER-associated protein degradation (ERAD) via HRD1/SEL1L. Alternately, β cell HRD1 activity is reported to improve, or impair, insulin biogenesis. Further, while β cell SEL1L deficiency causes
Anoop Arunagiri +14 more
doaj +2 more sources
Cell Reports, 2016 Endoplasmic reticulum (ER)-associated degradation (ERAD) is a principal mechanism that targets ER-associated proteins for cytosolic proteasomal degradation.
Ling Qi, Qiaoming Long, Liu Yang
exaly +3 more sources
E3 Ubiquitin Ligases in MASH-Associated Liver Fibrosis: Mechanisms and Therapeutic Opportunities. [PDF]
Liver IntABSTRACT Metabolic dysfunction‐associated steatohepatitis (MASH) is a major cause of progressive liver fibrosis and can ultimately lead to cirrhosis and hepatocellular carcinoma (HCC). MASH‐associated liver fibrosis develops through a complex interplay among lipotoxic hepatocyte injury, oxidative and endoplasmic reticulum stress, inflammatory ...
Oh AR +8 more
europepmc +2 more sources