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

Transmembrane protein 66

Top mentioned proteins: OS-9, HRD1, Ubiquitin, SEL1L, CD45
Papers on TMEM66
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.
Differential upregulation of the hypothetical transmembrane protein 66 (TMEM66) in multiple sclerosis patients with potential inflammatory response.
Bakhiet et al., Manama, Bahrain. In Biomed Rep, 2015
The results showed that out of ~50,000 genes, the hypothetical transmembrane protein-66 gene (TMEM66) exhibited a 3 times higher expression in MS patients compared to healthy subjects.
Human dCTP pyrophosphatase 1 promotes breast cancer cell growth and stemness through the modulation on 5-methyl-dCTP metabolism and global hypomethylation.
Wang et al., Shanghai, China. In Oncogenesis, 2014
Human DCTPP1 (dCTP pyrophosphatase 1), also known as XTP3-transactivated protein A, belongs to MazG-like nucleoside triphosphate pyrophosphatase (NTP-PPase) superfamily.
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.
Lectin OS-9 delivers mutant neuroserpin to endoplasmic reticulum associated degradation in familial encephalopathy with neuroserpin inclusion bodies.
Glatzel et al., Hamburg, Germany. In Neurobiol Aging, 2014
We show that the ER-lectin OS-9 but not XTP3-B is involved in ERAD of mutant neuroserpin.
The NTP pyrophosphatase DCTPP1 contributes to the homoeostasis and cleansing of the dNTP pool in human cells.
González-Pacanowska et al., Granada, Spain. In Biochem J, 2014
Human cells possess an all-α NTP (nucleoside triphosphate) pyrophosphatase named DCTPP1 [dCTP pyrophosphatase 1; also known as XTP3-TPA (XTP3-transactivated protein A)].
EDEM2 and OS-9 are required for ER-associated degradation of non-glycosylated sonic hedgehog.
Chen et al., Oxford, United Kingdom. In Plos One, 2013
Degradation of SHH and N278A also required OS-9, but not the related lectin XTP3-B.
Endoplasmic reticulum lectin XTP3-B inhibits endoplasmic reticulum-associated degradation of a misfolded α1-antitrypsin variant.
Hosokawa et al., Kyoto, Japan. In Febs J, 2013
Mammalian OS-9 and XTP3-B are ER-resident lectins that contain mannose 6-phosphate receptor homology (MRH) domains, which recognize sugar moieties; OS-9 has one MRH domain and XTP3-B has two.
A shared endoplasmic reticulum-associated degradation pathway involving the EDEM1 protein for glycosylated and nonglycosylated proteins.
Lederkremer et al., Tel Aviv-Yafo, Israel. In J Biol Chem, 2013
Two nonglycosylated BiP substrates, NS-1κ light chain and truncated Igγ heavy chain, interact with the ERAD complex lectins OS-9 and XTP3-B and require EDEM1 for degradation.
Unassembled CD147 is an endogenous endoplasmic reticulum-associated degradation substrate.
Kopito et al., Stanford, United States. In Mol Biol Cell, 2012
Degradation of folding- or assembly-defective proteins by the endoplasmic reticulum-associated degradation (ERAD) ubiquitin ligase, Hrd1, is facilitated by a process that involves recognition of demannosylated N-glycans by the lectin OS-9/XTP3-B via the adaptor protein SEL1L.
Changes in leukocyte gene expression profiles induced by antineoplastic chemotherapy.
Martín-Vasallo et al., La Laguna, Spain. In Oncol Lett, 2012
The genes that were studied in patients undergoing CT were ATM (ataxia-telangiectasia mutated gene), eIF4B (translation initiation factor 4B), MATR3 (Matrin 3), MORC3 (microrchidia 3), PCMTD2 (protein-L-isoaspartate O-methyltransferase), PDCD10 (programmed cell death gene 10), PSMB1 (proteasome subunit type β), RMND5A (required for meiotic nuclear division 5 homologue A), RUNX2 (runt-related transcription factor 2), SACM1L (suppressor of actin mutations 1-like), TMEM66 (transmembrane protein 66) and ZNF644 (zinc finger protein 644).
SARAF inactivates the store operated calcium entry machinery to prevent excess calcium refilling.
Reuveny et al., Israel. In Cell, 2012
Study shows that SARAF is an endoplasmic reticulum resident protein, which responds to cytosolic Ca2+ elevation after ER Ca2+ refilling by promoting a slow inactivation process of STIM2-dependent basal SOCE activity, as well as STIM1-mediated SOCE activity.
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.
The role of MRH domain-containing lectins in ERAD.
Kato et al., Kyoto, Japan. In Glycobiology, 2010
Meanwhile, the function of the mammalian homologues of Yos9p, OS-9 and XTP3-B remained elusive until recently.
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.
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
We report here that OS-9 and XTP3-B/Erlectin are ER-resident glycoproteins that bind to ERAD substrates and, through the SEL1L adaptor, to the ER-membrane-embedded ubiquitin ligase Hrd1.
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