Mouse Clusterin, CLU ELI

Functions as extracellular chaperone that prevents aggregation of non native proteins.

Prevents stress-induced aggregation of blood plasma proteins (By similarity).

Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro) (PubMed: 14741101).

Does not require ATP.

Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70.

Does not refold proteins by itself.

Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation.

When secreted, protects cells against apoptosis and against cytolysis by complement.

Intracellular forms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins.

Promotes proteasomal degradation of COMMD1 and IKBKB.

Modulates NF-kappa-B transcriptional activity (By similarity).

Following stress, promotes apoptosis (PubMed: 12551933).

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 (By similarity).

When secreted, acts as an important modulator during neuronal differentiation through interaction with STMN3 (By similarity).

Plays a role in the clearance of immune complexes that arise during cell injury (PubMed: 11865066).