Presenilin 1 is required for maturation and cell surface accumulation of nicastrin
about
The Nicastrin-like protein Nicalin regulates assembly and stability of the Nicalin-nodal modulator (NOMO) membrane protein complexMammalian APH-1 interacts with presenilin and nicastrin and is required for intramembrane proteolysis of amyloid-beta precursor protein and NotchSyntaxin 5 interacts with presenilin holoproteins, but not with their N- or C-terminal fragments, and affects beta-amyloid peptide productionAssociation of gamma-secretase with lipid rafts in post-Golgi and endosome membranes.Nicastrin is critical for stability and trafficking but not association of other presenilin/gamma-secretase components.Presenilin-1 uses phospholipase D1 as a negative regulator of beta-amyloid formation.Nicalin and its binding partner Nomo are novel Nodal signaling antagonistsThe presenilinsDynamin 1 regulates amyloid generation through modulation of BACE-1Assembly, trafficking and function of gamma-secretasePen-2 is incorporated into the gamma-secretase complex through binding to transmembrane domain 4 of presenilin 1Gamma-secretase complex assembly within the early secretory pathwayPresenilin-1, nicastrin, amyloid precursor protein, and gamma-secretase activity are co-localized in the lysosomal membranePresenilin 1 and presenilin 2 have differential effects on the stability and maturation of nicastrin in Mammalian brainAn E3 ubiquitin ligase, Synoviolin, is involved in the degradation of immature nicastrin, and regulates the production of amyloid beta-proteinSpatial segregation of gamma-secretase and substrates in distinct membrane domains.Loss of modifier of cell adhesion reveals a pathway leading to axonal degeneration.Presenilin 1 and Presenilin 2 Target γ-Secretase Complexes to Distinct Cellular Compartments.Familial Alzheimer disease-linked presenilin 1 variants enhance production of both Abeta 1-40 and Abeta 1-42 peptides that are only partially sensitive to a potent aspartyl protease transition state inhibitor of "gamma-secretase".Assembly, maturation, and trafficking of the gamma-secretase complex in Alzheimer's disease.Accumulation of phosphorylated beta-catenin enhances ROS-induced cell death in presenilin-deficient cellsImpairments in fast axonal transport and motor neuron deficits in transgenic mice expressing familial Alzheimer's disease-linked mutant presenilin 1Stem cell models of Alzheimer's disease: progress and challenges.Cellular distribution of gamma-secretase subunit nicastrin in the developing and adult rat brains.Functional analysis of the transmembrane domains of presenilin 1: participation of transmembrane domains 2 and 6 in the formation of initial substrate-binding site of gamma-secretase.A presenilin-1 mutation identified in familial Alzheimer disease with cotton wool plaques causes a nearly complete loss of gamma-secretase activityRegulation of tyrosinase trafficking and processing by presenilins: partial loss of function by familial Alzheimer's disease mutation.Mutation analysis of the presenilin 1 N-terminal domain reveals a broad spectrum of gamma-secretase activity toward amyloid precursor protein and other substrates.Transcriptional regulation of PEN-2, a key component of the gamma-secretase complex, by CREBAlleles at the Nicastrin locus modify presenilin 1- deficiency phenotype.Phospholipase D1 corrects impaired betaAPP trafficking and neurite outgrowth in familial Alzheimer's disease-linked presenilin-1 mutant neuronsGamma-secretase is a membrane protein complex comprised of presenilin, nicastrin, Aph-1, and Pen-2.Characterization of presenilin complexes from mouse and human brain using Blue Native gel electrophoresis reveals high expression in embryonic brain and minimal change in complex mobility with pathogenic presenilin mutations.Evidence that CD147 modulation of beta-amyloid (Abeta) levels is mediated by extracellular degradation of secreted AbetaThe γ-secretase complex: from structure to function.Pathological and physiological functions of presenilins.Amyloid, presenilins, and Alzheimer's disease.Inhibitors of γ-secretase stabilize the complex and differentially affect processing of amyloid precursor protein and other substrates.Dissociation between the processivity and total activity of γ-secretase: implications for the mechanism of Alzheimer's disease-causing presenilin mutations.Insulin-degrading enzyme sorting in exosomes: a secretory pathway for a key brain amyloid-beta degrading protease
P2860
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P2860
Presenilin 1 is required for maturation and cell surface accumulation of nicastrin
description
2002 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի մայիսին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2002
@ast
im Mai 2002 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2002/05/24)
@sk
vědecký článek publikovaný v roce 2002
@cs
wetenschappelijk artikel (gepubliceerd op 2002/05/24)
@nl
наукова стаття, опублікована в травні 2002
@uk
name
Presenilin 1 is required for maturation and cell surface accumulation of nicastrin
@ast
Presenilin 1 is required for maturation and cell surface accumulation of nicastrin
@en
Presenilin 1 is required for maturation and cell surface accumulation of nicastrin
@nl
type
label
Presenilin 1 is required for maturation and cell surface accumulation of nicastrin
@ast
Presenilin 1 is required for maturation and cell surface accumulation of nicastrin
@en
Presenilin 1 is required for maturation and cell surface accumulation of nicastrin
@nl
prefLabel
Presenilin 1 is required for maturation and cell surface accumulation of nicastrin
@ast
Presenilin 1 is required for maturation and cell surface accumulation of nicastrin
@en
Presenilin 1 is required for maturation and cell surface accumulation of nicastrin
@nl
P2093
P2860
P921
P356
P1476
Presenilin 1 is required for maturation and cell surface accumulation of nicastrin
@en
P2093
Dongming Cai
Gopal Thinakaran
Jae Yoon Leem
Kryslaine O. Lopes
Margaret L. Veselits
Michael Machura
Shrijay Vijayan
P2860
P304
19236–19240
P356
10.1074/JBC.C200148200
P407
P577
2002-05-24T00:00:00Z