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Osteosarcoma amplified 9, endoplasmic reticulum lectin

This gene encodes a protein that is highly expressed in osteosarcomas. This protein binds to the hypoxia-inducible factor 1 (HIF-1), a key regulator of the hypoxic response and angiogenesis, and promotes the degradation of one of its subunits. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: SEL1L, CD45, TMEM66, HRD1, Ubiquitin
Papers on OS-9
OS9 interacts with NKCC2 and targets its immature form for the endoplasmic-reticulum-associated degradation pathway.
Laghmani et al., France. In J Biol Chem, Jan 2016
We identified OS9 (amplified in osteosarcomas) as a novel and specific binding partner of NKCC2.
IRE1α is an endogenous substrate of endoplasmic-reticulum-associated degradation.
Qi et al., Ithaca, United States. In Nat Cell Biol, Dec 2015
ERAD-mediated IRE1α degradation occurs under basal conditions in a BiP-dependent manner, requires both the intramembrane hydrophilic residues of IRE1α and the lectin protein OS9, and is attenuated by ER stress.
[Research Progress in the Core Proteins of the Classical Swine Fever Virus].
Zhang et al., In Bing Du Xue Bao, Sep 2015
In this review, we combine study of this protein with its disorders, structural/functional characteristics, as well as its interactions with the non-structural proteins NS3, NS5B and host proteins such as SUMO-1, UBC9, OS9 and IQGAP1.
Promotion of Endoplasmic Reticulum-Associated Degradation of Procathepsin D by Human Herpesvirus 8-Encoded Viral Interleukin-6.
Nicholas et al., Baltimore, United States. In J Virol, Aug 2015
Coprecipitation assays identified direct or indirect interactions of VKORC1v2, vIL-6, and pCatD with translocon proteins (SEL1L and/or HRD1) and ERAD-associated lectins OS9 and XTP3-B.
Crystal Structure and Functional Analyses of the Lectin Domain of Glucosidase II: Insights into Oligomannose Recognition.
Dahms et al., Milwaukee, United States. In Biochemistry, Aug 2015
Comparison of the MRH domains of GIIβ, MPRs, and the ER lectin OS-9 identified conserved residues that are critical for the structural integrity and architecture of the carbohydrate binding pocket.
A context-independent N-glycan signal targets the misfolded extracellular domain of Arabidopsis STRUBBELIG to endoplasmic-reticulum-associated degradation.
Strasser et al., Vienna, Austria. In Biochem J, 2015
Stable expression in Arabidopsis thaliana knockout mutants revealed that SUBEX-C57Y degradation is dependent on the ER lectin OS9 and its associated ERAD factor SEL1L. SUBEX-C57Y was also stabilized in plants lacking the α-mannosidases MNS4 and MNS5 that generate a terminal α1,6-linked mannose on the C-branch of N-glycans.
Glucosidase II and MRH-domain containing proteins in the secretory pathway.
Dahms et al., Buenos Aires, Argentina. In Curr Protein Pept Sci, 2014
These include the beta subunit of glucosidase II (GII), a key enzyme in the early processing of the transferred glycan that removes middle and innermost glucoses and is involved in quality control of glycoprotein folding in the ER (QC), the lectins OS-9 and XTP3-B, proteins involved in the delivery of ER misfolded proteins to degradation (ERAD), the gamma subunit of the Golgi GlcNAc-1-phosphotransferase, an enzyme involved in generating the mannose 6-phosphate (M6P) signal for sorting acidic hydrolases to lysosomes, and finally the MPRs that deliver those hydrolytic enzymes to the lysosome.
A Novel Role of OS-9 in the Maintenance of Intestinal Barrier Function from Hypoxia-induced Injury via p38-dependent Pathway.
Yang et al., Chongqing, China. In Int J Biol Sci, 2014
OS-9 is a lectin required for efficient ubquitination of glycosylated substrates of endoplasmic reticulum-associated degradation (ERAD).
Comprehensive phylogenetic reconstructions of Rift Valley fever virus: the 2010 northern Mauritania outbreak in the Camelus dromedarius species.
Cêtre-Sossah et al., Nouakchott, Mauritania. In Vector Borne Zoonotic Dis, 2014
Phylogenetic analyses suggested a shared ancestor between the Mauritania 2010 strain and strains from Zimbabwe (2269, 763, and 2373), Kenya (155_57 and 56IB8), South Africa (Kakamas, SA75 and SA51VanWyck), Uganda (Entebbe), and other strains linked to the 1987 outbreak of RVF in Mauritania (OS1, OS3, OS8, and OS9).
A novel long non-coding RNA ENST00000480739 suppresses tumour cell invasion by regulating OS-9 and HIF-1α in pancreatic ductal adenocarcinoma.
Cao et al., Shanghai, China. In Br J Cancer, 2014
METHODS: We examined the expression levels of lncRNA ENST00000480739 and osteosarcoma amplified-9 (OS-9) mRNA in a cohort of 35 PDAC patients.
How viruses hijack the ERAD tuning machinery.
Molinari et al., Bellinzona, Switzerland. In J Virol, 2014
Recent reports highlight the analogies between mouse hepatitis virus-, equine arteritis virus-, and Japanese encephalitis virus-induced replication platforms and ER-associated degradation (ERAD) tuning vesicles (or EDEMosomes) that display nonlipidated LC3 at their cytosolic face and segregate the ERAD factors EDEM1, OS-9, and SEL1L from the ER lumen.
[Proteomics research of bufalin-induced apoptosis in osteosarcoma cell lines].
Shen et al., In Zhongguo Zhong Yao Za Zhi, 2014
METHOD: MTT assay was used to detect the growth inhibition rates of osteosarcoma cells U-20S, U-20S/MTX300, SaOS-2, IOR/OS9 treated with bufalin in different concentrations and times.
Mannose 6-phosphate receptor homology (MRH) domain-containing lectins in the secretory pathway.
Dahms et al., Milwaukee, United States. In Biochim Biophys Acta, 2011
BACKGROUND: The mannose 6-phosphate receptor homology (MRH) domain-containing family of proteins, which include recycling receptors (mannose 6-phosphate receptors, MPRs), resident endoplasmic reticulum (ER) proteins (glucosidase II β-subunit, XTP3-B, OS-9), and a Golgi glycosyltransferase (GlcNAc-phosphotransferase γ-subunit), are characterized by the presence of one or more MRH domains.
[OS-9 and XTP3-B: lectins that regulate endoplasmic reticulum-associated degradation (ERAD)].
Hosokawa, Kyoto, Japan. In Seikagaku, 2011
It regulates endoplasmic reticulum-associated degradation. (review)
Structural basis for oligosaccharide recognition of misfolded glycoproteins by OS-9 in ER-associated degradation.
Yamaguchi et al., Saitama, Japan. In Mol Cell, 2011
The OS-9 specifically recognizes Manalpha1,6Manalpha1,6Man residues on the processed C-arm through the continuous double tryptophan (WW) motif.
The function of hypoxia-inducible factor (HIF) is independent of the endoplasmic reticulum protein OS-9.
Metzen et al., Essen, Germany. In Plos One, 2010
OS-9 plays no direct functional role in HIF degradation since physical interaction of OS-9 with oxygen sensing HIF prolyl hydroxylases cannot occur in vivo due to their different subcellular localization
The sugar-binding ability of human OS-9 and its involvement in ER-associated degradation.
Yamamoto et al., Chiba, Japan. In Glycobiology, 2010
The sugar-binding ability of human OS-9 and its involvement in ER-associated degradation
Mannose 6-phosphate receptor homology domain-containing lectins in mammalian endoplasmic reticulum-associated degradation.
Kamiya et al., Kyoto, Japan. In Methods Enzymol, 2009
OS-9 and XTP3-B/Erlectin, mannose 6-phosphate receptor homology (MRH) domain-containing lectins in mammals, were recently identified as ER luminal glycoproteins that participate in ER-associated degradation (ERAD) of misfolded proteins.
[The cooperation of OS-9 and PHDs in hypoxia-induced pulmonary hypertension of rats].
Hu et al., Changsha, China. In Zhongguo Ying Yong Sheng Li Xue Za Zhi, 2009
HIF-1alpha, procollagen-proline dioxygenases and OS-9 are all involved in the pathogenesis of hypoxic pulmonary hypertension in rats.
OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD.
Kopito et al., Stanford, United States. In Nat Cell Biol, 2008
OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD
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