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Sci. STKE, 29 May 2001
Vol. 2001, Issue 84, p. tw3
[DOI: 10.1126/stke.2001.84.tw3]

EDITORS' CHOICE

Cell Biology Protein Aggregation and Degradation

Many neurodegenerative disorders are characterized by the prevalence of protein aggregates in the brain. These aggregates are often composed of proteins that have been modified by the addition of ubiquitin, a marker that should lead to degradation of the offending protein by a cytosolic proteolytic complex known as the proteasome. But are the aggregates a cause or a consequence of the disease process? Bence et al. (see the news story by Helmuth) now show that protein aggregation per se appears to inhibit the proteasomal protein degradation system.

N. F. Bence, R. M. Sampat, R. K. Kopito, Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292, 1552-1555 (2001). [Abstract] [Full Text]

L. Helmuth, Protein clumps hijack cell's clearance system. Science 292, 1467-1468 (2001). [Full Text]

Citation: Protein Aggregation and Degradation. Sci. STKE 2001, tw3 (2001).


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