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Presenilin enhancer 2 homolog

Presenilins, which are components of the gamma-secretase protein complex, are required for intramembranous processing of some type I transmembrane proteins, such as the Notch proteins and the beta-amyloid precursor protein. Signaling by Notch receptors mediates a wide range of developmental cell fates. Processing of the beta-amyloid precursor protein generates neurotoxic amyloid beta peptides, the major component of senile plaques associated with Alzheimer's disease. This gene encodes a protein that is required for Notch pathway signaling, and for the activity and accumulation of gamma-secretase. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Presenilin-1, Nicastrin, APH-1, APH, APP
Papers on PEN-2
Immobilized subpopulations of leaf epidermal mitochondria mediate PEN2-dependent pathogen entry control in Arabidopsis.
Lipka et al., Göttingen, Germany. In Plant Cell, Jan 2016
UNASSIGNED: The atypical myrosinase PEN2 is required for broad-spectrum invasion resistance to filamentous plant pathogens.
Nicastrin is required for APP but not Notch processing, while Aph-1 is dispensable for processing of both APP and Notch.
Xu et al., Knoxville, United States. In J Neurochem, Jan 2016
UNASSIGNED: The γ-secretase complex is composed of at least four components: presenilin (PS1 or PS2), nicastrin (NCT), anterior pharynx-defective 1 (Aph-1), and presenilin enhancer 2 (pen-2).
Hydrogen Sulfide Selectively Inhibits γ-Secretase Activity and Decreases Mitochondrial Aβ Production in Neurons from APP/PS1 Transgenic Mice.
Yan et al., Chongqing, China. In Neurochem Res, Jan 2016
Meanwhile, NaHS did not changed BACE-1 and ADAM10 (a disintegrin and metalloprotease 10) protein levels, but NaHS (30 μM) significantly increased the levels of presenilin 1(PS1), PEN-2, and NCT, as well as improved the γ-secretase activity, while NaHS (50 μM) exhibits the opposing effects.
DHA suppresses chronic apoptosis in the lung caused by perinatal inflammation.
Rogers et al., Bonn, Germany. In Am J Physiol Lung Cell Mol Physiol, Oct 2015
Modest but inconsistent differences were observed in Notch-pathway proteins Jagged 1, DLL 1, PEN2, and presenilin-2.
The topology of pen-2, a γ-secretase subunit, revisited: evidence for a reentrant loop and a single pass transmembrane domain.
Sisodia et al., Chicago, United States. In Mol Neurodegener, 2014
BACKGROUND: The γ-secretase complex, composed of transmembrane proteins termed presenilin (PS), anterior pharynx defective (APH), nicastrin (NCT), and presenilin enhancer-2 (Pen-2) catalyzes intramembranous hydrolysis of a variety of Type I membrane protein substrates.
Three-dimensional structure of human γ-secretase.
Shi et al., Beijing, China. In Nature, 2014
The γ-secretase complex, comprising presenilin 1 (PS1), PEN-2, APH-1 and nicastrin, is a membrane-embedded protease that controls a number of important cellular functions through substrate cleavage.
Structural biology of presenilin 1 complexes.
St George-Hyslop et al., Cambridge, United Kingdom. In Mol Neurodegener, 2013
Subsequent work has shown that the presenilin proteins are the catalytic subunits of a hetero-tetrameric complex containing APH1, nicastrin and PEN-2.
The γ-secretase complex: from structure to function.
Zhang et al., Xiamen, China. In Front Cell Neurosci, 2013
γ-secretase is a high molecular weight complex minimally composed of four components: presenilins (PS), nicastrin, anterior pharynx defective 1 (APH-1), and presenilin enhancer 2 (PEN-2).
Protein quality control by Rer1p in the early secretory pathway: from mechanism to implication in Alzheimer's disease.
Annaert et al., Leuven, Belgium. In Alzheimers Res Ther, 2012
γ-Secretase is a multimeric transmembrane complex consisting of the catalytic presenilin, nicastrin, presenilin enhancer 2 (PEN2) and anterior-pharynx defective-1 (APH1) subunits.
Contribution of the γ-secretase subunits to the formation of catalytic pore of presenilin 1 protein.
Iwatsubo et al., Tokyo, Japan. In J Biol Chem, 2012
secretase subunits restrict the arrangement of the transmembrane domains of presenilin during the formation of the functional structure of the catalytic pore.
Assembly of the presenilin γ-/ε-secretase complex.
Fraser et al., Toronto, Canada. In J Neurochem, 2012
The presenilin complex is composed of four core proteins (presenilin 1 or presenilin 2, APH1, nicastrin, and PEN2).
Calsenilin regulates presenilin 1/γ-secretase-mediated N-cadherin ε-cleavage and β-catenin signaling.
Choi et al., Anyang, South Korea. In Faseb J, 2011
expression of calsenilin leads to a disruption of presenilin 1/gamma-secretase-mediated epsilon-cleavage of N-cadherin, which results in the significant accumulation of N-cadherin C-terminal fragment 1
Modulation of γ-secretase activity by multiple enzyme-substrate interactions: implications in pathogenesis of Alzheimer's disease.
Sendula-Jengić et al., Rijeka, Croatia. In Plos One, 2011
Studies indicate that gradual saturation of gamma-secretase with its substrate can be the pathogenic process in different alleged causes of Alzheimer's disease (AD).
[Presenilin gene].
Tomita, Tokyo, Japan. In Nihon Rinsho, 2011
The molecular state of gamma-secretase and its enzymological characteristics are described.
Structure of gamma-secretase and its trimeric pre-activation intermediate by single-particle electron microscopy.
Ubarretxena-Belandia et al., New York City, United States. In J Biol Chem, 2011
structural analysis of PEN-2 conformation by single-particle electron microscopy
Glucosinolate metabolites required for an Arabidopsis innate immune response.
Ausubel et al., Boston, United States. In Science, 2009
Two genes, PEN2 and PEN3, are also necessary for resistance to pathogens and are required for both callose deposition and glucosinolate activation, suggesting that the pathogen-triggered callose response is required for resistance to microbial pathogens.
A glucosinolate metabolism pathway in living plant cells mediates broad-spectrum antifungal defense.
Schulze-Lefert et al., Köln, Germany. In Science, 2009
CYP81F2 gene encodes a P450 monooxygenase that is essential for the pathogen-induced accumulation of 4-methoxyindol-3-ylmethylglucosinolate, which in turn is activated by the atypical PEN2 myrosinase for antifungal defense
The structure and function of Alzheimer's gamma secretase enzyme complex.
Martins et al., Australia. In Crit Rev Clin Lab Sci, 2008
Four core components (presenilin, nicastrin, aph-1, and pen-2) interact in a high-molecular-weight complex to perform intramembrane proteolysis on a number of membrane-bound proteins, including APP and Notch.
TMP21 is a presenilin complex component that modulates gamma-secretase but not epsilon-secretase activity.
Fraser et al., Toronto, Canada. In Nature, 2006
The presenilin proteins (PS1 and PS2) and their interacting partners nicastrin, aph-1 (refs 4, 5) and pen-2 (ref.
Pre- and postinvasion defenses both contribute to nonhost resistance in Arabidopsis.
Schulze-Lefert et al., Köln, Germany. In Science, 2005
PEN2 restricts pathogen entry of two ascomycete powdery mildew fungi that in nature colonize grass and pea species; the PEN2 glycosyl hydrolase localizes to peroxisomes and acts as a component of an inducible preinvasion resistance mechanism. [PEN2]
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