Hsc70-interacting protein also known as suppression of tumorigenicity 13 (ST13) is a protein that in humans is encoded by the ST13gene.[1][2][3]
Function
The protein encoded by this gene is an adaptor protein that mediates the association of the heat shock proteins HSP70 and HSP90. This protein has been shown to be involved in the assembly process of glucocorticoid receptor, which requires the assistance of multiple molecular chaperones. The expression of this gene is reported to be downregulated in colorectal carcinoma tissue suggesting that is a candidate tumor suppressor gene.[3]
References
↑Zhang Y, Cai X, Schlegelberger B, Zheng S (Mar 1999). "Assignment1 of human putative tumor suppressor genes ST13 (alias SNC6) and ST14 (alias SNC19) to human chromosome bands 22q13 and 11q24→q25 by in situ hybridization". Cytogenet Cell Genet. 83 (1–2): 56–7. doi:10.1159/000015125. PMID9925927.
↑Prapapanich V, Chen S, Nair SC, Rimerman RA, Smith DF (Oct 1996). "Molecular cloning of human p48, a transient component of progesterone receptor complexes and an Hsp70-binding protein". Mol Endocrinol. 10 (4): 420–31. doi:10.1210/me.10.4.420. PMID8721986.
Cao J, Cai X, Zheng L, et al. (1997). "Characterization of colorectal-cancer-related cDNA clones obtained by subtractive hybridization screening". J. Cancer Res. Clin. Oncol. 123 (8): 447–51. doi:10.1007/BF01372549. PMID9292708.
Mo Y, Zheng S, Shen D (1998). "[Differential expression of HSU17714 gene in colorectal cancer and normal colonic mucosa]". Zhonghua Zhong Liu Za Zhi. 18 (4): 241–3. PMID9387309.
Johnson BD, Schumacher RJ, Ross ED, Toft DO (1998). "Hop modulates Hsp70/Hsp90 interactions in protein folding". J. Biol. Chem. 273 (6): 3679–86. doi:10.1074/jbc.273.6.3679. PMID9452498.
Zheng S, Cai X, Cao J, et al. (1998). "Screening and identification of down-regulated genes in colorectal carcinoma by subtractive hybridization: a method to identify putative tumor suppressor genes". Chin. Med. J. 110 (7): 543–7. PMID9594214.
Chen S, Smith DF (1999). "Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery". J. Biol. Chem. 273 (52): 35194–200. doi:10.1074/jbc.273.52.35194. PMID9857057.
Dunham I, Shimizu N, Roe BA, et al. (1999). "The DNA sequence of human chromosome 22". Nature. 402 (6761): 489–95. doi:10.1038/990031. PMID10591208.
Morishima Y, Kanelakis KC, Silverstein AM, et al. (2000). "The Hsp organizer protein hop enhances the rate of but is not essential for glucocorticoid receptor folding by the multiprotein Hsp90-based chaperone system". J. Biol. Chem. 275 (10): 6894–900. doi:10.1074/jbc.275.10.6894. PMID10702249.
Rajapandi T, Greene LE, Eisenberg E (2000). "The molecular chaperones Hsp90 and Hsc70 are both necessary and sufficient to activate hormone binding by glucocorticoid receptor". J. Biol. Chem. 275 (29): 22597–604. doi:10.1074/jbc.M002035200. PMID10781595.
Agarraberes FA, Dice JF (2002). "A molecular chaperone complex at the lysosomal membrane is required for protein translocation". J. Cell Sci. 114 (Pt 13): 2491–9. PMID11559757.
Velten M, Gomez-Vrielynck N, Chaffotte A, Ladjimi MM (2002). "Domain structure of the HSC70 cochaperone, HIP". J. Biol. Chem. 277 (1): 259–66. doi:10.1074/jbc.M106881200. PMID11687574.
Nelson GM, Prapapanich V, Carrigan PE, et al. (2005). "The heat shock protein 70 cochaperone hip enhances functional maturation of glucocorticoid receptor". Mol. Endocrinol. 18 (7): 1620–30. doi:10.1210/me.2004-0054. PMID15071092.
