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P62 and the sequestosome, a novel mechanism for protein metabolism

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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.

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Authors and Affiliations

  1. Division of Tumor Virology, Dana-Farber Cancer Institute and Harvard Medical School, 44 Binney Street, 02115, Boston, MA, U.S.A.

    Jaekyoon Shin

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  1. Jaekyoon Shin
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Shin, J. P62 and the sequestosome, a novel mechanism for protein metabolism. Arch. Pharm. Res. 21, 629–633 (1998). https://doi.org/10.1007/BF02976748

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  • DOI: https://doi.org/10.1007/BF02976748

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