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Clusterin

Definition:

[Isoform 1]: Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). 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. 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. A mitochondrial form suppresses BAX-dependent release of cytochrome c into the cytoplasm and inhibit apoptosis. Plays a role in the regulation of cell proliferation. An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5. Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity. Secreted form act 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 (By similarity).; [Isoform 6]: Does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity.; [Isoform 4]: Does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity. Promotes cell death through interaction with BCL2L1 that releases and activates BAX.

References:

[1]. D E Jenne, et al. Molecular structure and functional characterization of a human complement cytolysis inhibitor found in blood and seminal plasma: identity to sulfated glycoprotein 2, a constituent of rat testis fluid. Proc Natl Acad Sci U S A. 1989 Sep;86(18):7123-7. [Content Brief]

[2]. Honglai Zhang, et al. Clusterin inhibits apoptosis by interacting with activated Bax. Nat Cell Biol. 2005 Sep;7(9):909-15. [Content Brief]

[3]. Stephen Poon, et al. Mildly acidic pH activates the extracellular molecular chaperone clusterin. J Biol Chem. 2002 Oct 18;277(42):39532-40. [Content Brief]

[4]. Amy R Wyatt, et al. Clusterin facilitates in vivo clearance of extracellular misfolded proteins. Cell Mol Life Sci. 2011 Dec;68(23):3919-31. [Content Brief]

[5]. Amy R Wyatt, et al. Structural characterization of clusterin-chaperone client protein complexes. J Biol Chem. 2009 Aug 14;284(33):21920-21927. [Content Brief]

[6]. Melissa K Ranney, et al. Multiple pathways regulating the anti-apoptotic protein clusterin in breast cancer. Biochim Biophys Acta. 2007 Sep;1772(9):1103-11. [Content Brief]

[7]. Danny M Hatters, et al. Suppression of apolipoprotein C-II amyloid formation by the extracellular chaperone, clusterin. Eur J Biochem. 2002 Jun;269(11):2789-94. [Content Brief]

[8]. Elise M Stewart, et al. Effects of glycosylation on the structure and function of the extracellular chaperone clusterin. Biochemistry. 2007 Feb 6;46(5):1412-22. [Content Brief]

[9]. Amy R Wyatt, et al. Identification of human plasma proteins as major clients for the extracellular chaperone clusterin. J Biol Chem. 2010 Feb 5;285(6):3532-3539. [Content Brief]

[10]. Nayoung Kim, et al. Human nuclear clusterin mediates apoptosis by interacting with Bcl-XL through C-terminal coiled coil domain. J Cell Physiol. 2012 Mar;227(3):1157-67. [Content Brief]

[11]. Amina Zoubeidi, et al. Clusterin facilitates COMMD1 and I-kappaB degradation to enhance NF-kappaB activity in prostate cancer cells. Mol Cancer Res. 2010 Jan;8(1):119-30. [Content Brief]

[12]. Federica Rizzi, et al. Clusterin is a short half-life, poly-ubiquitinated protein, which controls the fate of prostate cancer cells. J Cell Physiol. 2009 May;219(2):314-23. [Content Brief]

[13]. N Li, et al. GRP78 regulates clusterin stability, retrotranslocation and mitochondrial localization under ER stress in prostate cancer. Oncogene. 2013 Apr 11;32(15):1933-42. [Content Brief]

[14]. Justin J Yerbury, et al. The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures. FASEB J. 2007 Aug;21(10):2312-22. [Content Brief]

[15]. Giorgia Santilli, et al. Essential requirement of apolipoprotein J (clusterin) signaling for IkappaB expression and regulation of NF-kappaB activity. J Biol Chem. 2003 Oct 3;278(40):38214-9. [Content Brief]

[16]. Janet R Kumita, et al. The extracellular chaperone clusterin potently inhibits human lysozyme amyloid formation by interacting with prefibrillar species. J Mol Biol. 2007 May 25;369(1):157-67. [Content Brief]

[17]. S Poon, et al. Clusterin is an ATP-independent chaperone with very broad substrate specificity that stabilizes stressed proteins in a folding-competent state. Biochemistry. 2000 Dec 26;39(51):15953-60. [Content Brief]

[18]. Hans Prochnow, et al. Non-secreted clusterin isoforms are translated in rare amounts from distinct human mRNA variants and do not affect Bax-mediated apoptosis or the NF-κB signaling pathway. PLoS One. 2013 Sep 20;8(9):e75303. [Content Brief]

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