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Anterior pharynx defective 1 homolog A

APH-1, APH-1a
This gene encodes a component of the gamma secretase complex that cleaves integral membrane proteins such as Notch receptors and beta-amyloid precursor protein. The gamma secretase complex contains this gene product, or the paralogous anterior pharynx defective 1 homolog B (APH1B), along with the presenilin, nicastrin, and presenilin enhancer-2 proteins. The precise function of this seven-transmembrane-domain protein is unknown though it is suspected of facilitating the association of nicastrin and presenilin in the gamma secretase complex as well as interacting with substrates of the gamma secretase complex prior to their proteolytic processing. Polymorphisms in a promoter region of this gene have been associated with an increased risk for developing sporadic Alzheimer's disease. Alternative splicing results in multiple protein-coding and non-protein-coding transcript variants. [provided by RefSeq, Aug 2011] (from NCBI)
Top mentioned proteins: APH, Presenilin-1, Nicastrin, PEN-2, APP
Papers on APH-1
Quinomycin A targets Notch signaling pathway in pancreatic cancer stem cells.
Subramaniam et al., Kansas City, United States. In Oncotarget, Jan 2016
The γ-secretase complex proteins, Presenilin 1, Nicastrin, Pen2, and APH-1, required for Notch activation also exhibited decreased expression.
An atomic structure of human γ-secretase.
Shi et al., Beijing, China. In Nature, Oct 2015
Component protein APH-1 serves as a scaffold, anchoring the lone transmembrane helix from nicastrin and supporting the flexible conformation of PS1.
Akt1 phosphorylates Nicastrin to regulate its protein stability and activity.
Park et al., Kwangju, South Korea. In J Neurochem, Sep 2015
The gamma-secretase complex consists of four essential proteins: presenilin (PS1 or PS2), presenilin enhancer 2 (PEN-2), anterior pharynx-defective 1 (APH-1), and the Nicastrin (NCT).
Lee et al., South Korea. In Arch Insect Biochem Physiol, Jul 2015
Several cell types were found to synthesize G3 LEA RNA, including neurons, muscular cells, APH-1(+) cells, and renal cells.
The effects and interactions of APOE and APH-1A polymorphisms in Alzheimer disease.
Gündüz et al., In Turk J Med Sci, 2014
One of the major components of y-secretase complex, anterior pharynx-defective-1 (APH-1), is responsible for the activity of the γ-secretase complex.
γ-Secretase Modulators and APH1 Isoforms Modulate γ-Secretase Cleavage but Not Position of ε-Cleavage of the Amyloid Precursor Protein (APP).
Koo et al., Singapore, Singapore. In Plos One, 2014
APH1A and APH1B, a subunit of the γ-secretase complex, also modulated Aβ42/Aβ40 ratio without any alterations in ε-cleavage, a result in contrast to what has been observed with PS1 and APP FAD mutations.
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.
Specific domains in anterior pharynx-defective 1 determine its intramembrane interactions with nicastrin and presenilin.
Wong et al., Baltimore, United States. In Neurobiol Aging, 2012
We propose a model that identifies critical TMDs of Aph-1 for associations with Nct and PS for the stepwise assembly of gamma-secretase components.
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).
The -980C/G polymorphism in APH-1A promoter confers risk of Alzheimer's disease.
Jia et al., Beijing, China. In Aging Cell, 2011
The -980C/G polymorphism in APH-1A promoter confers risk of Alzheimer's disease
Reduced Alzheimer's disease ß-amyloid deposition in transgenic mice expressing S-palmitoylation-deficient APH1aL and nicastrin.
Thinakaran et al., Chicago, United States. In J Neurosci, 2011
Coexpression of wild-type or S-palmitoylation-deficient APH1aL and nicastrin leads to marked stabilization of transgenic presenilin 1 in the brains of double-transgenic mice.
Localization and trafficking of endogenous anterior pharynx-defective 1, a component of Alzheimer's disease related gamma-secretase.
Fraser et al., Toronto, Canada. In Neurosci Lett, 2010
Endogenous Aph-1a and its proteolytic fragment have unique properties for cleavage control that may have implications for gamma-secretase regulation and intracellular distribution.
Human CRB2 inhibits gamma-secretase cleavage of amyloid precursor protein by binding to the presenilin complex.
Nishimura et al., Japan. In J Biol Chem, 2010
Co-overexpression of presenilin-1 or APH-1 abrogated gamma-secretase inhibition probably through prevention of the incorporation of CRB2 into the gamma-secretase complex
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.
Time-controlled transcardiac perfusion cross-linking for the study of protein interactions in complex tissues.
Baldwin et al., San Francisco, United States. In Nat Biotechnol, 2004
To validate tcTPC for identifying protein-protein interactions, we established that tcTPC allowed stringent immunoaffinity purification of the gamma-secretase complex in high salt concentrations and detergents and was compatible with mass spectrometric identification of cross-linked aph-1, presenilin-1 and nicastrin.
GSK-3alpha regulates production of Alzheimer's disease amyloid-beta peptides.
Klein et al., Philadelphia, United States. In Nature, 2003
Presenilin interacts with nicastrin, APH-1 and PEN-2 (ref.
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