P62 and the sequestosome, a novel mechanism for protein metabolism
- 1 December 1998
- journal article
- review article
- Published by Springer Nature in Archives of Pharmacal Research
- Vol. 21 (6) , 629-633
- https://doi.org/10.1007/bf02976748
Abstract
In addition to selecting proteins for degradation by the 26S proteasome, ubiqitination appears to serve other regulatory functions, including for endosomal/lysosomal targeting, protein translocation, and enzyme modification. Currently, little is known how multiubiquitin chains are recognized by these cellular mechanisms. Within the 26S proteasome, one subunit (Mcb1/S5a) has been identified that has affinity for multiubiquitin chains and may function as a ubiquitin receptor. We recently found that a non-proteasomal protein p62 also preferentially binds multiubiquitin chains and forms a novel cytoplasmic structure “sequestosome” which serves as a storage place for ubiquitinated proteins. In the present manuscript, the role and regulation of p62 in relation to the sequestosomal function will be reviewed.Keywords
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