Presenilin-1 is indirectly implicated in Notch1 cleavage.
It has been previously demonstrated that the Notch1 signalling pathway is impaired in presenilin-1 null cells. This observation suggests a role for presenilin-1 in the Notch1 developmental pathway, possibly through physical interaction. Here, we show that presenilin-1 and Notch1 do not interact directly with each other but are associated in the cell. These findings raise the possibility that the gamma-secretase cleavage occurs via a presenilin complex in association with a putative co-factor specific for the molecule that is being cleaved (e.g. Notch1, (beta-amyloid precursor protein, E-cadherin and ErbB-4, all of which are gamma-secretase substrates).
D053829:Amyloid Precursor Protein Secretases; D016282:Aspartic Acid Endopeptidases; D002460:Cell Line; D010450:Endopeptidases / Q000235:genetics / Q000378:metabolism; D006801:Humans; D006868:Hydrolysis; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism* / Q000502:physiology*; D053764:Presenilin-1; D051881:Receptor, Notch1; D011956:Receptors, Cell Surface; D014157:Transcription Factors
D008565:Membrane Proteins; C497761:NOTCH1 protein, human; C508853:PSEN1 protein, human; D053764:Presenilin-1; D051881:Receptor, Notch1; D011956:Receptors, Cell Surface; D014157:Transcription Factors; D053829:Amyloid Precursor Protein Secretases; D010450:Endopeptidases; D016282:Aspartic Acid Endopeptidases; C509280:BACE1 protein, human