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ER degradation enhancer, mannosidase alpha-like 2

EDEM2, C20orf31
In the endoplasmic reticulum (ER), misfolded proteins are retrotranslocated to the cytosol and degraded by the proteasome in a process known as ER-associated degradation (ERAD). EDEM2 belongs to a family of proteins involved in ERAD of glycoproteins (Mast et al., 2005 [PubMed 15537790]).[supplied by OMIM, Mar 2008] (from NCBI)
Top mentioned proteins: CD45, CAN, Calnexin, Alpha-1, p97
Papers on EDEM2
Forcible destruction of severely misfolded mammalian glycoproteins by the non-glycoprotein ERAD pathway.
Mori et al., Okazaki, Japan. In J Cell Biol, Dec 2015
We recently showed that this process is initiated by EDEM2 and completed by EDEM3/EDEM1.
Role of Drosophila EDEMs in the degradation of the alpha-1-antitrypsin Z variant.
Kang et al., Seoul, South Korea. In Int J Mol Med, Apr 2015
We previously established a Drosophila model of this disease by overexpressing the null Hong Kong (NHK) allele of this gene and found that the Drosophila lectin, ER degradation-enhancing α-mannosidase-like protein 2 (EDEM2), can accelerate the degradation of A1AT when overexpressed.
Hydrophobicity of protein determinants influences the recognition of substrates by EDEM1 and EDEM2 in human cells.
Słomińska-Wojewódzka et al., In Bmc Cell Biol, 2014
BACKGROUND: EDEM1 and EDEM2 are crucial regulators of the endoplasmic reticulum (ER)-associated degradation (ERAD) that extracts misfolded glycoproteins from the calnexin chaperone system.
EDEM2 initiates mammalian glycoprotein ERAD by catalyzing the first mannose trimming step.
Mori et al., Kyoto, Japan. In J Cell Biol, 2014
Most surprisingly, the upstream mannose trimming from Man9GlcNAc2 to Man8GlcNAc2 is conducted mainly by EDEM2, which was previously considered to lack enzymatic activity.
The role of EDEM2 compared with EDEM1 in ricin transport from the endoplasmic reticulum to the cytosol.
Sandvig et al., Gdańsk, Poland. In Biochem J, 2014
EDEM1 [ER (endoplasmic reticulum)-degradation-enhancing α-mannosidase I-like protein 1] and EDEM2 are crucial regulators of ERAD (ER-associated degradation) that extracts non-native glycoproteins from the calnexin chaperone system.
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
While EDEM2 was required for ERAD of both glycosylated and non-glycosylated SHHs, EDEM3 was only necessary for glycosylated SHH and EDEM1 was dispensable for both.
Genetic associations for activated partial thromboplastin time and prothrombin time, their gene expression profiles, and risk of coronary artery disease.
Folsom et al., Minneapolis, United States. In Am J Hum Genet, 2012
For PT, significant associations were identified and confirmed in F7 (rs561241, p = 3.71 × 10(-56)) and PROCR/EDEM2 (rs2295888, p = 5.25 × 10(-13)).
Activation of ERAD pathway by human hepatitis B virus modulates viral and subviral particle production.
Branza-Nichita et al., Bucureşti, Romania. In Plos One, 2011
We found that synthesis of EDEMs (EDEM1 and its homologues, EDEM2 and EDEM3) is significantly up-regulated in cells with persistent or transient HBV replication.
High levels of protein C are determined by PROCR haplotype 3.
Reitsma et al., Leiden, Netherlands. In J Thromb Haemost, 2011
Four haplotypes of PROCR, two SNPs in the neighboring gene EDEM2 and critical SNPs encountered during resequencing were genotyped in the family and in a large group of healthy individuals (the Leiden Thrombophilia Study (LETS) controls).
Genome-wide association study identifies novel loci for plasma levels of protein C: the ARIC study.
Folsom et al., Minneapolis, United States. In Blood, 2011
(EDEM2, rs6120849, P = 7.19 × 10(-37) and 5.23 × 10(-17) before and after conditional analysis, respectively).
Glycoprotein folding and the role of EDEM1, EDEM2 and EDEM3 in degradation of folding-defective glycoproteins.
Molinari et al., Bellinzona, Switzerland. In Febs Lett, 2007
Folding-incompetent proteins carrying N-glycans are extracted from futile folding cycles in the calnexin chaperone system upon intervention of EDEM1, EDEM2 and EDEM3, three ER-stress-induced members of the glycosyl hydrolase 47 family.
Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation.
Mori et al., Kyoto, Japan. In J Cell Biol, 2006
Both Derlin-2 and -3 are up-regulated by the UPR, and at least Derlin-2 is a target of the IRE1 branch of the response, which is known to up-regulate ER degradation enhancing alpha-mannosidase-like protein (EDEM) and EDEM2, receptor-like molecules for misfolded glycoprotein.
Human EDEM2, a novel homolog of family 47 glycosidases, is involved in ER-associated degradation of glycoproteins.
Moremen et al., Athens, United States. In Glycobiology, 2005
Overexpression of EDEM2 accelerates the degradation of misfolded alpha1-antitrypsin, indicating that the protein is involved in endoplasmic reticulum associated degradation.
A novel stress-induced EDEM variant regulating endoplasmic reticulum-associated glycoprotein degradation.
Molinari et al., Bellinzona, Switzerland. In J Biol Chem, 2005
EDEM2 regulates endoplasmic reticulum-associated glycoprotein degradation
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