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OS-9 regulates the secretory transport of TRPV4 and appears to protect TRPV4 subunits from the precocious ubiquitination and ER-associated degradation.
Data suggest renal cell lines exhibit an OS9-mediated ERAD (endoplasmic reticulum-associated degradation) pathway that degrades Nkcc2/Slc12a1 (solute carrier family 12 member 1) prior to glycosylation/processing.
The depletion of OS-9 in 3T3-L1 adipocytes impaired cell function in terms of triacylglycerol storage, and slightly influenced cell differentiation.
The relative expression of OS9 and XTP3B and the distribution of glycan and non-glycan degrons within the same protein contribute to the fidelity.
The endoplasmic reticulum-associated protein, OS-9, behaves as a lectin in targeting the immature calcium-sensing receptor.
OS-9 up-regulates occludin and claudin-1 by activating the MAP kinase (MAPK) pathway, and thus protects the epithelial barrier function of Caco-2 monolayer under hypoxia condition.
EDEM2 and OS-9 are required for ER-associated degradation of non-glycosylated sonic hedgehog
Unique regions mediate the interaction between OS-9 and GRP94.
It delivers mutant neuroserpin to ERAD by recognition of glycan side chains and provide the first in vivo proof of involvement of ERAD in degradation of mutant neuroserpin.
long non-coding RNA ENST00000480739 suppresses tumour cell invasion by regulating OS-9 and HIF-1alpha in pancreatic ductal adenocarcinoma.
Data indicate that the interaction of OS-9 and XTP3-B with CD147(CG) was inhibited by mutations to conserved residues in their lectin domains.
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
It regulates endoplasmic reticulum-associated degradation. (review)
The OS-9 specifically recognizes Manalpha1,6Manalpha1,6Man residues on the processed C-arm through the continuous double tryptophan (WW) motif.
The sugar-binding ability of human OS-9 and its involvement in ER-associated degradation
Identification of a peptide, resulting from a point mutation in gene OS-9, recognized by cytolytic T lymphocytes on a human melanoma.
OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD
Xbp1-responsive OS-9 variants in the mammalian endoplasmic reticulum inhibit secretion of misfolded protein conformers and enhancing their disposal
OS9 is critically involved in the modulation of ER-to-Golgi transport of DC-STAMP in response to TLR triggering, suggesting a novel role for OS9 in myeloid differentiation and cell fusion.
OS-9 recognises terminally misfolded proteins via polypeptide-based rather than glycan-based signals, but is only required for transferring those bearing N-glycans to the ubiquitination machinery.
model for mannose trimming and the requirement for OS-9 lectin activity in glycoprotein ERAD in which N-glycans lacking the terminal mannose from the C branch are recognized by OS-9 and targeted for degradation
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.
amplified in osteosarcoma
, osteosarcoma amplified 9, endoplasmic reticulum associated protein
, protein OS-9
, osteosarcoma amplified 9
, amplified in osteosarcoma 9
, endoplasmic reticulum lectin 2
, erlectin 2