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Death effector domain containing

This gene encodes a protein that contains a death effector domain (DED). DED is a protein-protein interaction domain shared by adaptors, regulators and executors of the programmed cell death pathway. Overexpression of this gene was shown to induce weak apoptosis. Upon stimulation, this protein was found to translocate from cytoplasm to nucleus and colocalize with UBTF, a basal factor required for RNA polymerase I transcription, in the nucleolus. At least three transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: PrP, CAN, ACID, exoribonuclease, caspase-8
Papers on DEDD
Identification and Testing of Novel CARP-1 Functional Mimetic Compounds as Inhibitors of Non-Small Cell Lung and Triple Negative Breast Cancers.
Rishi et al., In J Biomed Nanotechnol, Sep 2015
Cell growth suppression by CFM-4 and -4.6 involved interaction and elevated expression of CARP-1/CCAR1 and Death Effector Domain (DED) containing DNA binding (DEDD)2 proteins.
Metazoan Maelstrom is an RNA-binding protein that has evolved from an ancient nuclease active in protists.
Pillai et al., Grenoble, France. In Rna, May 2015
The overall architecture resembles that found in Mg(2+)- or Mn(2+)-dependent DEDD nucleases, but a clear distinguishing feature is the presence of a structural Zn(2+) ion coordinated by the conserved ECHC residues.
Tandem DEDs and CARDs suggest novel mechanisms of signaling complex assembly.
Tung et al., Tainan City, Taiwan. In Apoptosis, Feb 2015
There are seven DED-containing proteins in human, including FADD, c-FLIP, caspase-8, caspase-10, DEDD, DEDD2, and PEA-15.
Divergence of the expression and subcellular localization of CCR4-associated factor 1 (CAF1) deadenylase proteins in Oryza sativa.
Lu et al., Taiwan. In Plant Mol Biol, 2014
CAF1 belongs to the RNase D group in the DEDD superfamily, and is a protein conserved through evolution from yeast to humans and plants.
Structure and function of RNase AS, a polyadenylate-specific exoribonuclease affecting mycobacterial virulence in vivo.
Berisio et al., Napoli, Italy. In Structure, 2014
The structure of RNase AS reveals a resemblance to RNase T from Escherichia coli, an RNase of the DEDD family involved in RNA maturation.
Integrative analysis of 1q23.3 copy-number gain in metastatic urothelial carcinoma.
Rosenberg et al., Sabadell, Spain. In Clin Cancer Res, 2014
The F11R, PFDN2, PPOX, USP21, and DEDD genes, all located on 1q23.3, were closely associated with poor outcome.
A fluorescence-based assay suitable for quantitative analysis of deadenylase enzyme activity.
Winkler et al., Nottingham, United Kingdom. In Nucleic Acids Res, 2014
The ribonuclease activity of deadenylase enzymes is attributed to either a DEDD (Asp-Glu-Asp-Asp) or an endonuclease-exonuclease-phosphatase domain.
Mycobacterium tuberculosis Rv2179c protein establishes a new exoribonuclease family with broad phylogenetic distribution.
Grundner et al., Washington, D.C., United States. In J Biol Chem, 2014
Active site residues are equivalent to those in the DEDD family of RNases, and Rv2179c has close structural homology to Escherichia coli RNase T. Consistent with the DEDD fold, Rv2179c has exoribonuclease activity, cleaving the 3' single-strand overhangs of duplex RNA.
Molecular evolution of the primate α-/θ-defensin multigene family.
Huang et al., Kunming, China. In Plos One, 2013
Although previous studies have reported that α-/θ-defensin (DEFA/DEFT) genes are under birth-and-death evolution with frequent duplication and rapid evolution, the phylogenetic relationships of the primate DEFA/DEFT genes; the genetic bases for the existence of similar antimicrobial spectra among closely related species; and the evolutionary processes involved in the emergence of cyclic θ-defensins in Old World monkeys and their subsequent loss of function in humans, chimpanzees and gorillas require further investigation.
Use of the tumor repressor DEDD as a prognostic marker of cancer metastasis.
Hu et al., Beijing, China. In Methods Mol Biol, 2013
DEDD, a member of a family of death effector domain-containing proteins, plays crucial roles in mediating apoptosis, regulating cell cycle, and inhibiting cell mitosis.
Heterogeneity and complexity within the nuclease module of the Ccr4-Not complex.
Balacco et al., Nottingham, United Kingdom. In Front Genet, 2012
In addition to at least six non-catalytic subunits, it contains two distinct subunits with ribonuclease activity: a Caf1 subunit, characterized by a DEDD (Asp-Glu-Asp-Asp) domain, and a Ccr4 component containing an endonuclease-exonuclease-phosphatase (EEP) domain.
Deadenylation of cytoplasmic mRNA by the mammalian Ccr4-Not complex.
Winkler et al., Nottingham, United Kingdom. In Biochem Soc Trans, 2012
This multi-subunit protein complex is composed of at least seven stably associated subunits in mammalian cells including two enzymatic deadenylase subunits: one DEDD (Asp-Glu-Asp-Asp)-type deadenylase (either CNOT7/human Caf1/Caf1a or CNOT8/human Pop2/Caf1b/Calif) and one EEP (endonuclease-exonuclease-phosphatase)-type enzyme (either CNOT6/human Ccr4/Ccr4a or CNOT6L/human Ccr4-like/Ccr4b).
DEDD interacts with PI3KC3 to activate autophagy and attenuate epithelial-mesenchymal transition in human breast cancer.
Hu et al., Beijing, China. In Cancer Res, 2012
Via direct interaction with the class III PI-3-kinase (PI3KC3)/Beclin1, DEDD activated autophagy and induced the degradation of Snail and Twist, two master regulators of EMT
Death effector domain-containing protein (DEDD) is required for uterine decidualization during early pregnancy in mice.
Miyazaki et al., Tokyo, Japan. In J Clin Invest, 2011
In uteri of Dedd-/- mice, development of the decidual zone and the surrounding edema after embryonic implantation was defective. This was accompanied by disintegration of implantation site structure, leading to embryonic death before placentation.
Dissimilar roles of the four conserved acidic residues in the thermal stability of poly(A)-specific ribonuclease.
Yan et al., Beijing, China. In Int J Mol Sci, 2010
Poly(A)-specific ribonuclease (PARN) belongs to the DEDD superfamily of 3'-exonucleases, and the active site of PARN contains four conserved acidic amino acid residues that coordinate two Mg(2+) ions.
The structural basis for deadenylation by the CCR4-NOT complex.
Yamamoto et al., Tianjin, China. In Protein Cell, 2010
The complex contains two types of deadenylase enzymes, one belonging to the DEDD-type family and one belonging to the EEP-type family, which shorten the poly(A) tails of mRNA.
Localization of the death effector domain of Fas-associated death domain protein into the membrane of Escherichia coli induces reactive oxygen species-involved cell death.
Lee et al., Seoul, South Korea. In Biochemistry, 2010
FAS-associated death domain (FADD)-DED-induced reactive oxygen species (ROS) generation is triggered by membrane localization of FADD-DED, which shifts the cells into a state that stimulates and fuels ROS and ultimately results in cell death.
The death effector domain-containing DEDD forms a complex with Akt and Hsp90, and supports their stability.
Miyazaki et al., Tokyo, Japan. In Biochem Biophys Res Commun, 2010
DEDD plays an important role in maintenance of the Akt protein level, which in consequence supports the efficient incorporation of glucose into skeletal muscles and adipose tissues.
[Cell cycle and cell sizing regulation via death effector domain].
Miyazaki et al., Tokyo, Japan. In Seikagaku, 2009
It regulates cell cycle and cell sizing. (review)
Exoribonucleases and Endoribonucleases.
Deutscher et al., In Ecosal Plus, 2004
These are the RNR family, including RNase II and RNase R; the DEDD family, including RNase D, RNase T, and ORNase; the RBN family, consisting of RNase BN; and the PDX family, including PNPase and RNase PH.
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