Probing the Mint2 Protein-Protein Interaction Network Relevant to the Pathophysiology of Alzheimer's Disease
| Autor: | Kristian Strømgaard, Christian R. O. Bartling, Thomas M. T. Jensen, Louise Albertsen, Linda M. Haugaard-Kedström |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
chemistry.chemical_classification biology Chemistry Organic Chemistry Signal transducing adaptor protein Computational biology Biochemistry Protein–protein interaction Amino acid Pathogenesis 03 medical and health sciences 030104 developmental biology 0302 clinical medicine Interaction network Amyloid precursor protein biology.protein Molecular Medicine Phosphorylation Molecular Biology 030217 neurology & neurosurgery Intracellular |
| Zdroj: | ChemBioChem. 19:1119-1122 |
| ISSN: | 1439-4227 |
| Popis: | The intracellular adaptor protein Mint2 binds amyloid precursor protein (APP) and presenilin-1, which are both central constituents of the amyloidogenic pathway associated with Alzheimer's disease (AD). Additional interaction partners have also been suggested for Mint2; several of them are also pertinent to AD pathogenesis. However, no comparative mapping of the Mint2 protein-protein interaction network is available. Here we provide a systematic characterization of seven interaction partners and address their specificities towards the different binding domains of Mint2, which reveal domain-specific and -nonspecific interaction partners. Moreover, we show that the last two C-terminal amino acids of Mint2 are both important for the intramolecular interaction with the PDZ1 domain and for the stability of Mint2. |
| Databáze: | OpenAIRE |
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