All cells have the capacity to selectively degrade misfoldedintracellular proteins, which, if they accumulated, could interferewith normal function and could be toxic. Such proteins may ariseby mutation, errors in gene expression, failure to fold correctly,spontaneous denaturation, or postsynthetic damage (for example,by oxygen radicals). How often such events occur in cells isuncertain, largely because the ubiquitin–proteasome pathwayrapidly degrades such aberrant proteins, including those thatcause various inherited diseases, such as cystic fibrosis andcertain hemoglobinopathies.1
This pathway also protects against neurodegenerative diseases.1,2The hallmarks of amyotrophic lateral sclerosis, Parkinson'sdisease, Lewy-body dementia, Huntington's disease, . . . [Full Text of this Article]
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From the Department of Cell Biology, Harvard Medical School, Boston.
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[Abstract][Full Text]
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