de.mpg.escidoc.pubman.appbase.FacesBean
English
 
Help Guide Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

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

MPS-Authors
http://pubman.mpdl.mpg.de/cone/persons/resource/persons50098

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

Locator
There are no locators available
Fulltext (public)
There are no public fulltexts available
Supplementary Material (public)
There is no public supplementary material available
Citation

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.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-78BA-0
Abstract
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.