Presenilin mutants subvert chaperone function.
Mutant presenilin proteins, known to promote the development of Alzheimer's disease through increased generation of Abeta42 peptides, appear to compound this insult by downregulating the signalling pathway that adjusts levels of molecular chaperones in the endoplasmic reticulum in response to stress.
Gething
M J
MJ
D000544:Alzheimer Disease / Q000209:etiology / Q000378:metabolism*; D016564:Amyloid beta-Protein Precursor; D006801:Humans; D008565:Membrane Proteins / Q000235:genetics*; D018832:Molecular Chaperones / Q000378:metabolism*; D009154:Mutation; D053764:Presenilin-1; D053766:Presenilin-2
D016564:Amyloid beta-Protein Precursor; D008565:Membrane Proteins; D018832:Molecular Chaperones; C508853:PSEN1 protein, human; C508861:PSEN2 protein, human; D053764:Presenilin-1; D053766:Presenilin-2