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Article: Mutation of conserved aspartates affects maturation of both aspartate mutant and endogenous presenilin 1 and presenilin 2 complexes

TitleMutation of conserved aspartates affects maturation of both aspartate mutant and endogenous presenilin 1 and presenilin 2 complexes
Authors
Issue Date2000
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 2000, v. 275 n. 35, p. 27348-27353 How to Cite?
Abstract
Presenilin (PS1 and PS2) holoproteins are transiently incorporated into low molecular weight (MW) complexes. During subsequent incorporation into a higher MW complex, they undergo endoproteolysis to generate stable N- and C-terminal fragments. Mutation of either of two conserved aspartate residues in transmembrane domains inhibits both presenilin-endoproteolysis and the proteolytic processing of β-amyloid precursor protein and Notch. We show that although PS1/PS2 endoproteolysis is not required for inclusion into the higher MW N- and C-terminal fragment-containing complex, aspartate mutant holoprotein presenilins are not incorporated into the high MW complexes. Aspartate mutant presenilin holoproteins also preclude entry of endogenous wild type PS1/PS2 into the high MW complexes but do not affect the incorporation of wild type holoproteins into lower MW holoprotein complexes. These data suggest that the loss of function effects of the aspartate mutants results in altered PS complex maturation and argue that the functional presenilin moieties are contained in the high molecular weight complexes.
Persistent Identifierhttp://hdl.handle.net/10722/134762
ISSN
2013 Impact Factor: 4.600
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorYu, Gen_HK
dc.contributor.authorChen, Fen_HK
dc.contributor.authorNishimura, Men_HK
dc.contributor.authorSteiner, Hen_HK
dc.contributor.authorTandon, Aen_HK
dc.contributor.authorKawarai, Ten_HK
dc.contributor.authorArawaka, Sen_HK
dc.contributor.authorSupala, Aen_HK
dc.contributor.authorSong, YQen_HK
dc.contributor.authorRogaeva, Een_HK
dc.contributor.authorHolmes, Een_HK
dc.contributor.authorZhang, DMen_HK
dc.contributor.authorMilman, Pen_HK
dc.contributor.authorFraser, PEen_HK
dc.contributor.authorHaass, Cen_HK
dc.contributor.authorSt GeorgeHyslop, Pen_HK
dc.date.accessioned2011-07-14T07:02:57Z-
dc.date.available2011-07-14T07:02:57Z-
dc.date.issued2000en_HK
dc.identifier.citationJournal Of Biological Chemistry, 2000, v. 275 n. 35, p. 27348-27353en_HK
dc.identifier.issn0021-9258en_HK
dc.identifier.urihttp://hdl.handle.net/10722/134762-
dc.description.abstractPresenilin (PS1 and PS2) holoproteins are transiently incorporated into low molecular weight (MW) complexes. During subsequent incorporation into a higher MW complex, they undergo endoproteolysis to generate stable N- and C-terminal fragments. Mutation of either of two conserved aspartate residues in transmembrane domains inhibits both presenilin-endoproteolysis and the proteolytic processing of β-amyloid precursor protein and Notch. We show that although PS1/PS2 endoproteolysis is not required for inclusion into the higher MW N- and C-terminal fragment-containing complex, aspartate mutant holoprotein presenilins are not incorporated into the high MW complexes. Aspartate mutant presenilin holoproteins also preclude entry of endogenous wild type PS1/PS2 into the high MW complexes but do not affect the incorporation of wild type holoproteins into lower MW holoprotein complexes. These data suggest that the loss of function effects of the aspartate mutants results in altered PS complex maturation and argue that the functional presenilin moieties are contained in the high molecular weight complexes.en_HK
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_HK
dc.relation.ispartofJournal of Biological Chemistryen_HK
dc.subject.meshAspartic Acid/*geneticsen_US
dc.subject.meshCell Lineen_US
dc.subject.meshHumansen_US
dc.subject.meshMembrane Proteins/genetics/*physiologyen_US
dc.subject.meshMutagenesisen_US
dc.subject.meshPresenilin-1en_US
dc.subject.meshPresenilin-2en_US
dc.subject.meshProtein Processing, Post-Translationalen_US
dc.titleMutation of conserved aspartates affects maturation of both aspartate mutant and endogenous presenilin 1 and presenilin 2 complexesen_HK
dc.typeArticleen_HK
dc.identifier.emailSong, YQ:songy@hkucc.hku.hken_HK
dc.identifier.authoritySong, YQ=rp00488en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1074/jbc.M002982200en_HK
dc.identifier.pmid10856299en_HK
dc.identifier.scopuseid_2-s2.0-0034282749en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0034282749&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume275en_HK
dc.identifier.issue35en_HK
dc.identifier.spage27348en_HK
dc.identifier.epage27353en_HK
dc.identifier.isiWOS:000089144800091-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridYu, G=35370376900en_HK
dc.identifier.scopusauthoridChen, F=7404907428en_HK
dc.identifier.scopusauthoridNishimura, M=7403650959en_HK
dc.identifier.scopusauthoridSteiner, H=7203037540en_HK
dc.identifier.scopusauthoridTandon, A=7103281816en_HK
dc.identifier.scopusauthoridKawarai, T=7003632751en_HK
dc.identifier.scopusauthoridArawaka, S=6602984633en_HK
dc.identifier.scopusauthoridSupala, A=6602797868en_HK
dc.identifier.scopusauthoridSong, YQ=7404921212en_HK
dc.identifier.scopusauthoridRogaeva, E=35372614800en_HK
dc.identifier.scopusauthoridHolmes, E=7201667388en_HK
dc.identifier.scopusauthoridZhang, DM=23017363200en_HK
dc.identifier.scopusauthoridMilman, P=7004252433en_HK
dc.identifier.scopusauthoridFraser, PE=35408135200en_HK
dc.identifier.scopusauthoridHaass, C=7006070304en_HK
dc.identifier.scopusauthoridSt GeorgeHyslop, P=7005637468en_HK

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