| Title | Aggresome-like structure induced by isothiocyanates is novel proteasome-dependent degradation machinery. | | Author(s) | Mi L, Gan N, Chung FL | | Institution | Department of Oncology, Lombardi Comprehensive Cancer Center, Georgetown University, Washington, DC 20057. | | Source | Biochem Biophys Res Commun 2009 Aug 11. | | Abstract | Unwanted or misfolded proteins are either refolded by chaperones or degraded by the ubiquitin-proteasome system (UPS). When UPS is impaired, misfolded proteins form aggregates, which are transported along microtubules by motor protein dynein towards the juxta-nuclear microtubule organizing center to form aggresome, a single cellular garbage disposal complex. Because aggresome formation results from proteasome failure, aggresome components are degraded through the autophagy/lysosome pathway. Here we report that small molecule isothiocyanates (ITCs) can induce formation of aggresome-like structure (ALS) through covalent modification of cytoplasmic alpha- and beta- tubulin. The formation of ALS is related to neither proteasome inhibition nor oxidative stress. ITC-induced ALS is a proteasome-dependent assembly for emergent removal of misfolded proteins, suggesting that the cell may have a previously unknown strategy to cope with misfolded proteins. | | Language | ENG | | Pub Type(s) | JOURNAL ARTICLE
| | PubMed ID | 19682429 |
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