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Arch Pharm Res. 1998 Dec;21(6):629-33.

P62 and the sequestosome, a novel mechanism for protein metabolism.

Author information

1
Division of Tumor Virology, Dana-Farber Cancer Institute, Boston, MA 02115, USA.

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.

PMID:
9868528
DOI:
10.1007/bf02976748
[Indexed for MEDLINE]

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