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

Der1-like domain family, member 2

Derlin-2, Carcinoma-related, FLAN I, DERL-2, hF-LANa, F-LANa
Proteins that are unfolded or misfolded in the endoplasmic reticulum (ER) must be refolded or degraded to maintain the homeostasis of the ER. DERL2 is involved in the degradation of misfolded glycoproteins in the ER (Oda et al., 2006 [PubMed 16449189]).[supplied by OMIM, Mar 2008] (from NCBI)
Top mentioned proteins: p97, Derlin-1, ATPase, V1a, HRD1
Papers on Derlin-2
Proteasomal Degradation of Proinsulin Requires Derlin-2, HRD1 and p97.
Wiertz et al., Utrecht, Netherlands. In Plos One, 2014
We demonstrate that specific silencing of Derlin-2, p97 and HRD1 by shRNAs increases steady state levels of proinsulin.
Cytolethal distending toxins require components of the ER-associated degradation pathway for host cell entry.
Bradley et al., Los Angeles, United States. In Plos Pathog, 2014
Here we show that three central components of the host ER associated degradation (ERAD) machinery, Derlin-2 (Derl2), the E3 ubiquitin-protein ligase Hrd1, and the AAA ATPase p97, are required for intoxication by some CDTs.
Integrative genomic and transcriptomic analysis identified candidate genes implicated in the pathogenesis of hepatosplenic T-cell lymphoma.
Wlodarska et al., Leuven, Belgium. In Plos One, 2013
We report here results of an integrative genomic and transcriptomic (expression microarray and RNA-sequencing) study of six i(7)(q10)-positive HSTL cases, including HSTL-derived cell line (DERL-2), and three cases with ring 7 [r(7)], the recently identified rare variant aberration.
A high-coverage shRNA screen identifies TMEM129 as an E3 ligase involved in ER-associated protein degradation.
Lebbink et al., Utrecht, Netherlands. In Nat Commun, 2013
TMEM129 is an unconventional C4C4-type RING finger E3 ubiquitin ligase that resides within a complex containing various other ERAD components, including Derlin-1, Derlin-2, VIMP and p97, indicating that TMEM129 is an integral part of the ER-resident dislocation complex mediating US11-induced HLA class I degradation.
Overexpression of TCL1 activates the endoplasmic reticulum stress response: a novel mechanism of leukemic progression in mice.
Hu et al., Tampa, United States. In Blood, 2012
This includes activation of the IRE-1/XBP-1 pathway and the transcriptionally up-regulated expression of Derlin-1, Derlin-2, BiP, GRP94, and PDI.
Selenoprotein K binds multiprotein complexes and is involved in the regulation of endoplasmic reticulum homeostasis.
Gladyshev et al., Boston, United States. In J Biol Chem, 2012
In this complex, SelK showed higher affinity for Derlin-1, whereas SelS had higher affinity for Derlin-2, suggesting that these selenoproteins could determine the nature of the substrate translocated through the Derlin channel.
Derlin-2-deficient mice reveal an essential role for protein dislocation in chondrocytes.
Ploegh et al., Cambridge, United States. In Mol Cell Biol, 2011
We generated conditional knockout mice to examine the in vivo role of Derlin-2, a component that nucleates cellular dislocation machinery.
Cholera toxin up-regulates endoplasmic reticulum proteins that correlate with sensitivity to the toxin.
Draper et al., Richardson, United States. In Exp Biol Med (maywood), 2008
We report here that treating cells with CT or CTB quickly up-regulates the levels of BiP, Derlin-1, and Derlin-2, known participants in the ER stress response and ERAD.
hF-LANa, a human homologue of Derlin family, regulating the expression of cancer-related genes promotes NIH3T3 cell transformation.
Xu et al., Shanghai, China. In Cancer Lett, 2008
hF-LANa, a member of Derlin family, is a putative proto-oncogene and has a direct role in oncogenic transformation.
EDEM1 reveals a quality control vesicular transport pathway out of the endoplasmic reticulum not involving the COPII exit sites.
Roth et al., Z├╝rich, Switzerland. In Proc Natl Acad Sci U S A, 2007
Some of the EDEM1 vesicles also contain Derlin-2 and the misfolded Hong Kong variant of alpha-1-antitrypsin, a substrate for EDEM1 and ERAD.
Murine polyomavirus requires the endoplasmic reticulum protein Derlin-2 to initiate infection.
Benjamin et al., Boston, United States. In J Virol, 2006
Required for Polyoma virus infection.
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
Findings indicate that Derlin-2 provides the missing link between EDEM and p97 in the process of degrading misfolded glycoproteins.
Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane.
Ploegh et al., Boston, United States. In Proc Natl Acad Sci U S A, 2005
Derlin-2 forms a robust multiprotein complex with the p97 AAA ATPase as well as the mammalian orthologs of the yeast Hrd1p/Hrd3p ubiquitin-ligase complex, and participates in the degradation of proteins from the ER.
[In silico cloning of evolutionarily conserved mouse F-LANa].
Xu et al., In Shi Yan Sheng Wu Xue Bao, 2002
In previous study, human F-LANa was identified as a differentially expressed gene, up-regulated in hepatocellular carcinoma.
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