Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b
about
BRICHOS - a superfamily of multidomain proteins with diverse functionsThe α-helical content of the transmembrane domain of the British dementia protein-2 (Bri2) determines its processing by signal peptide peptidase-like 2b (SPPL2b)Substrate requirements for SPPL2b-dependent regulated intramembrane proteolysisThe transferrin receptor-1 membrane stub undergoes intramembrane proteolysis by signal peptide peptidase-like 2bBRI3 inhibits amyloid precursor protein processing in a mechanistically distinct manner from its homologue dementia gene BRI2BRI2 (ITM2b) inhibits Abeta deposition in vivoSignal-peptide-peptidase-like 2a (SPPL2a) is targeted to lysosomes/late endosomes by a tyrosine motif in its C-terminal tailToward the structure of presenilin/γ-secretase and presenilin homologsItm2a, a target gene of GATA-3, plays a minimal role in regulating the development and function of T cellsDifferential Inhibition of Signal Peptide Peptidase Family Members by Established γ-Secretase InhibitorsProteomic profiling of gamma-secretase substrates and mapping of substrate requirementsThe chaperone domain BRICHOS prevents CNS toxicity of amyloid-β peptide in Drosophila melanogasterModeling familial Danish dementia in mice supports the concept of the amyloid hypothesis of Alzheimer's disease.Regulated intramembrane proteolysis of the frontotemporal lobar degeneration risk factor, TMEM106B, by signal peptide peptidase-like 2a (SPPL2a).A functional role for ADAM10 in human immunodeficiency virus type-1 replicationExpression and characterization of Drosophila signal peptide peptidase-like (sppL), a gene that encodes an intramembrane protease.Foamy virus envelope protein is a substrate for signal peptide peptidase-like 3 (SPPL3).Structure, mechanism and inhibition of gamma-secretase and presenilin-like proteasesRab GTPase mediated procollagen trafficking in ascorbic acid stimulated osteoblasts.Secretome analysis identifies novel signal Peptide peptidase-like 3 (Sppl3) substrates and reveals a role of Sppl3 in multiple Golgi glycosylation pathways.Increased tau phosphorylation and tau truncation, and decreased synaptophysin levels in mutant BRI2/tau transgenic mice.Shedding of glycan-modifying enzymes by signal peptide peptidase-like 3 (SPPL3) regulates cellular N-glycosylationDifferential surface expression of ADAM10 and ADAM17 on human T lymphocytes and tumor cells.Glycosylation of BRI2 on asparagine 170 is involved in its trafficking to the cell surface but not in its processing by furin or ADAM10.A Cell-Based Assay Reveals Nuclear Translocation of Intracellular Domains Released by SPPL Proteases.Signal-peptide-peptidase-like 2a is required for CD74 intramembrane proteolysis in human B cellsLessons from a Rare Familial Dementia: Amyloid and Beyond.Proteolytic Processing of Neuregulin 1 Type III by Three Intramembrane-cleaving ProteasesB cell survival, surface BCR and BAFFR expression, CD74 metabolism, and CD8- dendritic cells require the intramembrane endopeptidase SPPL2A.Cerebral amyloid angiopathy and parenchymal amyloid deposition in transgenic mice expressing the Danish mutant form of human BRI2.Toward structural elucidation of the gamma-secretase complex.Intramembrane proteolysisTrafficking of receptor tyrosine kinases to the nucleusIntramembrane proteolysis by signal peptide peptidases: a comparative discussion of GXGD-type aspartyl proteases.The intramembrane proteases signal Peptide peptidase-like 2a and 2b have distinct functions in vivoRegulated intramembrane proteolysis: signaling pathways and biological functions.Intramembrane proteolysis in regulated protein trafficking.BRICHOS domain associated with lung fibrosis, dementia and cancer--a chaperone that prevents amyloid fibril formation?BRI2 protein regulates β-amyloid degradation by increasing levels of secreted insulin-degrading enzyme (IDE).The familial dementia gene revisited: a missense mutation revealed by whole-exome sequencing identifies ITM2B as a candidate gene underlying a novel autosomal dominant retinal dystrophy in a large family.
P2860
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P248
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P2860
Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b
description
2008 nî lūn-bûn
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2008 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b
@ast
Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b
@en
Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b
@en-gb
Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b
@nl
type
label
Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b
@ast
Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b
@en
Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b
@en-gb
Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b
@nl
prefLabel
Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b
@ast
Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b
@en
Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b
@en-gb
Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b
@nl
P2860
P50
P921
P356
P1476
Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b
@en
P2093
Karina Reiss
Lucas Martin
P2860
P304
P356
10.1074/JBC.M706661200
P407
P577
2008-01-18T00:00:00Z