Regulation of key proteins in Alzheimer’s disease molecular pathogenesis by ubiquilin-1
| Autor: | Mari Takalo, Hilkka Soininen, Heikki Tanila, Jayashree Viswanathan, Mikko Hiltunen, Annakaisa Haapasalo, Teemu Natunen, Kaisa M.A. Kurkinen, Rudolph E. Tanzi |
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| Rok vydání: | 2013 |
| Předmět: |
biology
business.industry Alternative splicing Clinical Neurology Bioinformatics Molecular medicine Presenilin UBQLN1 Cell biology Pathogenesis Cellular and Molecular Neuroscience Proteasome Poster Presentation Genetic variation Amyloid precursor protein biology.protein Medicine Neurology (clinical) business Molecular Biology |
| Zdroj: | Molecular Neurodegeneration |
| ISSN: | 1750-1326 |
| Popis: | Background Ubiquilin-1 is a ubiquitin-like protein involved in the pathogenesis of Alzheimer’s disease (AD) and other neurodegenerative disorders via different mechanisms. UBQLN1 UBQ-8i genetic variation associates with increased AD risk. Ubiquilin-1 protein functions as a molecular chaperone controlling amyloid precursor protein (APP) trafficking and processing and presenilin (PS) levels and subcellular targeting. Ubiquilin-1 harbors a ubiquitin-like (UBL) domain interacting with the proteasome and a ubiquitinassociated (UBA) domain binding polyubiquitinated proteins. Thus, it may target polyubiquitinated proteins to degradation. Alternative splicing of UBQLN1 generates four transcript variants (TV) with varying domain structures, suggesting that diverse variants may specifically interact with and regulate different proteins and cellular functions. |
| Databáze: | OpenAIRE |
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