WeightNameValue
1000 Titel
  • Endoplasmic reticulum retention of the γ‐secretase complex component Pen2 by Rer1
1000 Autor/in
  1. Kaether, Christoph |
  2. Scheuermann, Johanna |
  3. Fassler, Matthias |
  4. Zilow, Sonja |
  5. Shirotani, Keiro |
  6. Valkova, Christina |
  7. Novak, Bozidar |
  8. Kacmar, Slavomir |
  9. Steiner, Harald |
  10. Haass, Christian |
1000 Erscheinungsjahr 2007
1000 Publikationstyp
  1. Artikel |
1000 Online veröffentlicht
  • 2007-07-06
1000 Erschienen in
1000 Quellenangabe
  • 8(8): 743-748
1000 FRL-Sammlung
1000 Verlagsversion
  • https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1978084/ |
  • https://doi.org/10.1038/sj.embor.7401027 |
1000 Ergänzendes Material
  • http://embor.embopress.org/content/8/8/743#sec-9 |
1000 Publikationsstatus
1000 Begutachtungsstatus
1000 Sprache der Publikation
1000 Abstract/Summary
  • γ‐Secretase is involved in the production of amyloid β‐peptide, which is the principal component of amyloid plaques in the brains of patients with Alzheimer disease. γ‐Secretase is a complex composed of presenilin (PS), nicastrin, anterior pharynx‐defective phenotype 1 (Aph1) and PS enhancer 2 (Pen2). We previously proposed a mechanism of complex assembly by which unassembled subunits are retained in the endoplasmic reticulum (ER) and only the fully assembled complex is exported from the ER. We have now identified Retention in endoplasmic reticulum 1 (Rer1) as a protein that is involved in the retention/retrieval of unassembled Pen2 to the ER. Direct binding of unassembled Pen2 to Rer1 is mediated by the first transmembrane domain of Pen2, and a conserved asparagine in this domain is required. Downregulation of Rer1 leads to increased surface localization of Pen2, whereas overexpression of Rer1 stabilizes unassembled Pen2. To our knowledge, Rer1 is the first identified interaction partner of mammalian transmembrane‐based retention/retrieval signals.
1000 Sacherschließung
lokal ER Retrieval
lokal ER Retention
lokal Alzheimer Disease
lokal Pen2
lokal γ-secretase
1000 Fachgruppe
  1. Medizin |
1000 Fächerklassifikation (DDC)
1000 Liste der Beteiligten
  1. https://frl.publisso.de/adhoc/creator/S2FldGhlciwgQ2hyaXN0b3Bo|https://frl.publisso.de/adhoc/creator/U2NoZXVlcm1hbm4sIEpvaGFubmE=|https://frl.publisso.de/adhoc/creator/RmFzc2xlciwgTWF0dGhpYXM=|https://frl.publisso.de/adhoc/creator/Wmlsb3csIFNvbmph|https://frl.publisso.de/adhoc/creator/U2hpcm90YW5pLCBLZWlybw==|https://frl.publisso.de/adhoc/creator/VmFsa292YSwgQ2hyaXN0aW5h|https://frl.publisso.de/adhoc/creator/Tm92YWssIEJvemlkYXI=|https://frl.publisso.de/adhoc/creator/S2FjbWFyLCBTbGF2b21pcg==|https://frl.publisso.de/adhoc/creator/U3RlaW5lciwgSGFyYWxk|https://frl.publisso.de/adhoc/creator/SGFhc3MsIENocmlzdGlhbg==
1000 Förderer
  1. Medical Faculty (FöFoLe), Ludwigs‐Maximilians‐Universität München |
  2. Deutsche Forschungsgemeinschaft (DFG) |
1000 Fördernummer
  1. -
  2. CIPSM; SFB596; SFB604
1000 Förderprogramm
  1. Molecular Medicine Program
  2. -
1000 Förderung
  1. 1000 joinedFunding-child
    1000 Förderer Medical Faculty (FöFoLe), Ludwigs‐Maximilians‐Universität München |
    1000 Förderprogramm Molecular Medicine Program
    1000 Fördernummer -
  2. 1000 joinedFunding-child
    1000 Förderer Deutsche Forschungsgemeinschaft (DFG) |
    1000 Förderprogramm -
    1000 Fördernummer CIPSM; SFB596; SFB604
1000 Objektart article
1000 Beschrieben durch
1000 @id frl:6406390.rdf
1000 Erstellt am 2018-01-18T18:52:29.475+0100
1000 Erstellt von 218
1000 beschreibt frl:6406390
1000 Bearbeitet von 218
1000 Zuletzt bearbeitet Mon May 14 14:24:13 CEST 2018
1000 Objekt bearb. Mon May 14 14:24:13 CEST 2018
1000 Vgl. frl:6406390
1000 Oai Id
  1. oai:frl.publisso.de:frl:6406390 |
1000 Sichtbarkeit Metadaten public
1000 Sichtbarkeit Daten public
1000 Gegenstand von

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