alpha-synuclein and Fragile-X-Syndrome

Increasing evidence indicates that RNA plays an active role in a number of neurodegenerative diseases. We recently introduced a theoretical framework, catRAPID, to predict the binding ability of protein and RNA molecules. Here, we use catRAPID to investigate ribonucleoprotein interactions linked to inherited intellectual disability, amyotrophic lateral sclerosis, Creutzfeuld-Jakob, Alzheimer's, and Parkinson's diseases. We specifically focus on (1) RNA interactions with fragile X mental retardation protein FMRP; (2) protein sequestration caused by CGG repeats; (3) noncoding transcripts regulated by TAR DNA-binding protein 43 TDP-43; (4) autogenous regulation of TDP-43 and FMRP; (5) iron-mediated expression of amyloid precursor protein APP and α-synuclein; (6) interactions between prions and RNA aptamers. Our results are in striking agreement with experimental evidence and provide new insights in processes associated with neuronal function and misfunction.

Topics: Algorithms; alpha-Synuclein; Amyloid beta-Protein Precursor; Aptamers, Nucleotide; DNA-Binding Proteins; Female; Fragile X Mental Retardation Protein; Fragile X Syndrome; Gene Expression Regulation; Humans; Male; Models, Theoretical; Neurodegenerative Diseases; Prions; Protein Binding; Ribonucleoproteins; RNA; RNA-Binding Proteins; RNA, Untranslated