The lobster proteasome is primarily a cytosolic enzyme in crustacean striated muscles, although a small amount (<1 % of total)occurs in aggregates associated with invaginations of the cell membrane. The complex exists in vitro in three distinct catalytic states (basal, SDS-activated, and heat-activated forms)which have identical subunit compositions. This review summarizes recent results showing that the branched-chain amino acid-preferring (BrAAP) activity mediates the hydrolysis of myofibrillar proteins by the heat-activated proteasome; (a) only the BrAAP activity is stimulated by heat treatment; (b) the BrAAP activity is strongly inhibited by protein substrates, and(c) both the BrAAP and proteolytic activities show similar sensitivities to cations and protease inhibitors

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