1987 M.D Yaroslavl State Medical Institute, Yaroslavl, Russia

1992 Ph.D. All-Union Cancer Research Center (AUCRC), Moscow, Russia

Protein ubiquitination and degradation have emerged as important mechanisms in regulating cell growth and survival that play a key role in cancer. The long-term objective our laboratory is to identify the aberrations in ubiquitination of regulatory proteins that contribute to cell transformation and tumor progression and determine the usefulness of specific mediators of ubiquitination as potential targets for anti-cancer therapy. Our current focus is on the disregulated proteolysis of cytokine and hormone receptors in human malignant melanomas and breast cancers. For our studies, we employ various approaches and methods of molecular and cellular biology, biochemistry and mammalian genetics.

1. Spiegelman VS, Slaga TJ, Pagano M, Minamoto T, Ronai Z and Fuchs SY (2000) Wnt/ β-catenin signaling induces the expression and activity of βTrCP ubiquitin ligase receptor. Mol Cell, 5: 877-882.
2. Suresh Kumar K.G., Tang W, Ravindranath AR, Clark WA, Croze E and Fuchs SY (2003) SCF^HOS ubiquitin ligase mediates the ligand-induced down regulation of the interferon alpha receptor, EMBO J, 22: 5480-90.
3. Li Y, Suresh Kumar KG, Tang W, Spiegelman VS and Fuchs SY (2004) Negative regulation of prolactin receptor stability and signaling mediated by SCF^β-TrCP E3 ubiquitin ligase. Mol Cell Biol, 24: 4038-4048.
4. Suresh Kumar KG, Krolewski JJ and Fuchs SY (2004) Phosphorylation and specific ubiquitin-acceptor sites are required for ubiquitination and degradation of the IFNAR1 subunit of Type I interferon receptor. J Biol Chem, 279: 46614-46620.
5. Tang W, Li Y, Yu D, Thomas-Tikhonenko A, Spiegelman VS, and Fuchs SY (2005) Targeting β-TrCP E3 ubiquitin ligase augments the effects of anti-tumor drugs on breast cancer cells, Cancer Res, 65: 1905-1908.