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• Phosphorylation-dependent regulation of the interaction of amyloid precursor protein with Fe65 affects the production of beta-amyloid.
• Citation:
  Ando K, Iijima K, Elliott J, Kirino Y, Suzuki T
  

  Phosphorylation-dependent regulation of the interaction of amyloid precursor protein with Fe65 affects the production of beta-amyloid.

  The Journal of biological chemistry. 2001 Oct 26;276(43):40353-61
  [PubMed] [Alzforum]
• Supporting:
  • APP phosphorylation at Thr668 regulates another function of APP, the interaction of APP with neuronal Fe65, or intracellular trafficking, rather than direct regulation of APP metabolism.

    SHOW Details   Supporting(2)   Inconsistent(1)   Alternative to: (1)

    Experimental Approach: Mechanism - biochemistry and structural biology
    Pathogenic Narrative Tags: Initial condition
    Supporting Evidence
    

    • Sano Y, Nakaya T, Pedrini S, Takeda S, Iijima-Ando K, Iijima K, Mathews P, Itohara S, Gandy S, Suzuki T
      Physiological mouse brain Abeta levels are not related to the phosphorylation state of threonine-668 of Alzheimer's APP.
      PLoS ONE. 2006;1:e51
    • Ando K, Iijima K, Elliott J, Kirino Y, Suzuki T
      Phosphorylation-dependent regulation of the interaction of amyloid precursor protein with Fe65 affects the production of beta-amyloid.
      The Journal of biological chemistry. 2001 Oct 26;276(43):40353-61

    Inconsistent statements
    

    • Cell cycle-dependent phosphorylation of APP at Thr668 is associated with altered APP metabolism. Suzuki T  Oishi M  Marshak D  Czernik A  Nairn A  Greengard P 

    Alternative statements
    

    • The site of phosphorylation of APP by cdc2 kinase (Thr668) is within the proposed domain of interaction of APP with Go, suggesting the possibility that phosphorylation could modulate this process. Suzuki T  Oishi M  Marshak D  Czernik A  Nairn A  Greengard P 
• Created On: Wed, Jun 04 20:43:43 EDT 2008
• Last Modified On: Wed Jun 04 20:43:43 EDT 2008