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lüll P62 and the sequestosome, a novel mechanism for protein metabolism Shin JArch Pharm Res 1998[Dec]; 21 (6): 629-33In 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.|Adenosine Triphosphatases/metabolism[MESH]|Animals[MESH]|Cysteine Endopeptidases/metabolism[MESH]|Humans[MESH]|Multienzyme Complexes/metabolism[MESH]|Proteasome Endopeptidase Complex[MESH]|Protein Binding[MESH]|Protein Kinases/metabolism[MESH]|Proteins/*metabolism[MESH]|Proto-Oncogene Proteins c-myc/genetics/metabolism/*physiology[MESH]|Ubiquitins/*metabolism[MESH] |