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Article: Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processing

TitleNicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processing
Authors
Issue Date2000
PublisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/nature
Citation
Nature, 2000, v. 407 n. 6800, p. 48-54 How to Cite?
AbstractNicastrin, a transmembrane glycoprotein, forms high molecular weight complexes with presenilin 1 and presenilin 2. Suppression of nicastrin expression in Caenorhabditis elegans embryos induces a subset of notch/glp-1 phenotypes similar to those induced by simultaneous null mutations in both presenilin homologues of C. elegans (sel-12 and hop-1). Nicastrin also binds carboxy-terminal derivatives of β-amyloid precursor protein (βAPP), and modulates the production of the amyloid β-peptide (Aβ) from these derivatives. Missense mutations in a conserved hydrophilic domain of nicastrin increase Aβ 42 and Aβ 40 peptide secretion. Deletions in this domain inhibit Aβ production. Nicastrin and presenilins are therefore likely to be functional components of a multimeric complex necessary for the intramembranous proteolysis of proteins such as Notch/GLP-1 and βAPP.
Persistent Identifierhttp://hdl.handle.net/10722/134764
ISSN
2023 Impact Factor: 50.5
2023 SCImago Journal Rankings: 18.509
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorYu, Gen_HK
dc.contributor.authorNishimura, Men_HK
dc.contributor.authorArawaka, Sen_HK
dc.contributor.authorLevitan, Den_HK
dc.contributor.authorZhang, Len_HK
dc.contributor.authorTandon, Aen_HK
dc.contributor.authorSong, YQen_HK
dc.contributor.authorRogaeva, Een_HK
dc.contributor.authorChen, Fen_HK
dc.contributor.authorKawarai, Ten_HK
dc.contributor.authorSupala, Aen_HK
dc.contributor.authorLevesque, Len_HK
dc.contributor.authorYu, Hen_HK
dc.contributor.authorYang, DSen_HK
dc.contributor.authorHolmes, Een_HK
dc.contributor.authorMilman, Pen_HK
dc.contributor.authorLiang, Yen_HK
dc.contributor.authorZhang, DMen_HK
dc.contributor.authorXu, DHen_HK
dc.contributor.authorSato, Cen_HK
dc.contributor.authorRogaev, Een_HK
dc.contributor.authorSmith, Men_HK
dc.contributor.authorJanus, Cen_HK
dc.contributor.authorZhang, Yen_HK
dc.contributor.authorAebersold, Ren_HK
dc.contributor.authorFarrer, Len_HK
dc.contributor.authorSorbl, Sen_HK
dc.contributor.authorBruni, Aen_HK
dc.contributor.authorFraser, Pen_HK
dc.contributor.authorGeorgeHyslop, PSen_HK
dc.date.accessioned2011-07-14T07:03:03Z-
dc.date.available2011-07-14T07:03:03Z-
dc.date.issued2000en_HK
dc.identifier.citationNature, 2000, v. 407 n. 6800, p. 48-54en_HK
dc.identifier.issn0028-0836en_HK
dc.identifier.urihttp://hdl.handle.net/10722/134764-
dc.description.abstractNicastrin, a transmembrane glycoprotein, forms high molecular weight complexes with presenilin 1 and presenilin 2. Suppression of nicastrin expression in Caenorhabditis elegans embryos induces a subset of notch/glp-1 phenotypes similar to those induced by simultaneous null mutations in both presenilin homologues of C. elegans (sel-12 and hop-1). Nicastrin also binds carboxy-terminal derivatives of β-amyloid precursor protein (βAPP), and modulates the production of the amyloid β-peptide (Aβ) from these derivatives. Missense mutations in a conserved hydrophilic domain of nicastrin increase Aβ 42 and Aβ 40 peptide secretion. Deletions in this domain inhibit Aβ production. Nicastrin and presenilins are therefore likely to be functional components of a multimeric complex necessary for the intramembranous proteolysis of proteins such as Notch/GLP-1 and βAPP.en_HK
dc.publisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/natureen_HK
dc.relation.ispartofNatureen_HK
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAmyloid Precursor Protein Secretasesen_US
dc.subject.meshAmyloid beta-Protein Precursor/*metabolismen_US
dc.subject.meshAnimalsen_US
dc.subject.meshAspartic Acid Endopeptidasesen_US
dc.subject.meshCaenorhabditis elegansen_US
dc.subject.mesh*Caenorhabditis elegans Proteinsen_US
dc.subject.meshDNA, Complementaryen_US
dc.subject.meshEndopeptidases/metabolismen_US
dc.subject.meshHumansen_US
dc.subject.meshMembrane Glycoproteins/genetics/*metabolism/*physiologyen_US
dc.subject.meshMembrane Proteins/*metabolismen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshPresenilin-1en_US
dc.subject.meshPresenilin-2en_US
dc.subject.meshReceptors, Notchen_US
dc.subject.meshSequence Homology, Amino Aciden_US
dc.subject.mesh*Signal Transductionen_US
dc.subject.meshTransfectionen_US
dc.titleNicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processingen_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.doi10.1038/35024009en_HK
dc.identifier.pmid10993067en_HK
dc.identifier.scopuseid_2-s2.0-0034618715en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0034618715&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume407en_HK
dc.identifier.issue6800en_HK
dc.identifier.spage48en_HK
dc.identifier.epage54en_HK
dc.identifier.isiWOS:000089124000036-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridYu, G=35370376900en_HK
dc.identifier.scopusauthoridNishimura, M=7403650959en_HK
dc.identifier.scopusauthoridArawaka, S=6602984633en_HK
dc.identifier.scopusauthoridLevitan, D=23044813300en_HK
dc.identifier.scopusauthoridZhang, L=9280030900en_HK
dc.identifier.scopusauthoridTandon, A=7103281816en_HK
dc.identifier.scopusauthoridSong, YQ=7404921212en_HK
dc.identifier.scopusauthoridRogaeva, E=35372614800en_HK
dc.identifier.scopusauthoridChen, F=7404907428en_HK
dc.identifier.scopusauthoridKawarai, T=7003632751en_HK
dc.identifier.scopusauthoridSupala, A=6602797868en_HK
dc.identifier.scopusauthoridLevesque, L=7007053389en_HK
dc.identifier.scopusauthoridYu, H=23092412900en_HK
dc.identifier.scopusauthoridYang, DS=7404800601en_HK
dc.identifier.scopusauthoridHolmes, E=7201667388en_HK
dc.identifier.scopusauthoridMilman, P=7004252433en_HK
dc.identifier.scopusauthoridLiang, Y=26642980800en_HK
dc.identifier.scopusauthoridZhang, DM=37053272500en_HK
dc.identifier.scopusauthoridXu, DH=36792596900en_HK
dc.identifier.scopusauthoridSato, C=7201887342en_HK
dc.identifier.scopusauthoridRogaev, E=35391858800en_HK
dc.identifier.scopusauthoridSmith, M=8625780500en_HK
dc.identifier.scopusauthoridJanus, C=7005274261en_HK
dc.identifier.scopusauthoridZhang, Y=7601331778en_HK
dc.identifier.scopusauthoridAebersold, R=20833452100en_HK
dc.identifier.scopusauthoridFarrer, L=7005139839en_HK
dc.identifier.scopusauthoridSorbl, S=6504619577en_HK
dc.identifier.scopusauthoridBruni, A=7102347222en_HK
dc.identifier.scopusauthoridFraser, P=35408135200en_HK
dc.identifier.scopusauthoridGeorgeHyslop, PS=6601991234en_HK
dc.identifier.issnl0028-0836-

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