Abstract
Today the mechanism of protein aggregation is an intensely investigated subject in cell biology. We know that protein aggregation can occur due to a variety of causes including mutations in proteins easily misfolded or disruption of components of protein homeostasis machinery such as chaperones or components of the ubiquitin⿿proteasome system. Moreover, these aggregates are known to increase with age and to be associated with a variety of neurodegenerative disease. But not long ago, our understanding of the fate and function of protein aggregates in cells remained a mystery. Seminal studies revealed that protein aggregates could be sequestered into inclusion bodies called aggresomes through a highly regulated process that relies on dynein-dependent retrograde transport on microtubules. In 2000, Ron R. Kopito from Stanford University described recent insights into the mechanisms of aggregate sequestration and proposed potential benefits of this sequestration for the cell [ 1 Kopito R.R. Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol. 2000; 10: 524-530 Abstract Full Text Full Text PDF PubMed Scopus (1599) Google Scholar ]. Dr Kopito shares his thoughts on where the field of protein aggregation has come since publication of this review and the outstanding questions that remain.
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