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Involvement of ubiquilin-1 transcript variants in protein degradation and accumulation

MPG-Autoren
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Bertram,  L.
Neuropsychiatric Genetics (Lars Bertram), Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society;

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Zitation

Haapasalo, A., Viswanathan, J., Kurkinen, K. M., Bertram, L., Soininen, H., Dantuma, N. P., et al. (2011). Involvement of ubiquilin-1 transcript variants in protein degradation and accumulation. Communicative & Integrative Biology, 4(4), 428-32. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/21966562 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3181512/pdf/cib0404_0428.pdf?tool=pmcentrez.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0010-78BA-0
Zusammenfassung
Controlled management of protein levels and quality is essential for normal cellular function. Specific molecular chaperones and foldases monitor the levels and assist correct folding of proteins. The ubiquitin-proteasome system recognizes and degrades misfolded proteins that can otherwise be harmful to cells. However, when misfolded or aggregated proteins excessively accumulate, they may be sequestered to the microtubule-organizing center to form aggresomes. These may then be removed from cells by autophagocytosis. Abnormal protein accumulation and aggregation is a common hallmark of many neurodegenerative diseases. In a recent study, we provide evidence that specific transcript variants (TVs) of ubiquilin-1, which are genetically and functionally associated to Alzheimer's disease (AD), regulate proteasomal and aggresomal targeting of presenilin-1 (PS1), a key player in AD pathogenesis. Our study together with current data provide interesting implications for ubiquilin-1 and its TVs in the pathogenesis of AD and other neurodegenerative diseases involving abnormal protein aggregation.