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The Clusterin functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins (By similarity).When secreted, protects cells against apoptosis and against cytolysis by complement. Intracellular forms interact with ubiquitin and SCF E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Modulates NF-kappa-B transcriptional activity. Following stress, promotes apoptosis . Inhibits apoptosis when associated with the mitochondrial membrane by interference with BAX-dependent release of cytochrome c into the cytoplasm. Plays a role in the regulation of cell proliferation. Following ER stress, suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5. When secreted, does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity. When secreted, acts as an important modulator during neuronal differentiation through interaction with STMN3. Plays a role in the clearance of immune complexes that arise during cell injury.