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Senthil K. Muthuswamy

Adjunct Associate Professor
Ph.D., McMaster University, 1995


Contact
muthuswa@cshl.edu
(516) 367-6975 (p)
 
 
Changes in tissue architecture and cell differentiation are often the early signs of cancer, but little is known about the pathways that regulate them. Senthil Muthuswamy has developed a novel paradigm for thinking about this aspect of cancer biology. Using sophisticated model systems such as three-dimensional cell culture platforms and transgenic mice, his team found that proteins which regulate cell polarity are involved in both initiation and progression of cancer. Because cell polarity is found to be altered in multiple human cancers, understanding the pathways regulated by them can identify novel molecules and pathways that can be used either as drug targets or as biomarkers for cancer. In addition, Muthuswamy’s lab collaborates actively with multiple research teams at CSHL. For example, lab members collaborated with the Mills lab to demonstrate a role for p63 protein in stem cells of the skin and with the Krainer lab to investigate the role that the splicing factor SF2 has in breast cancer. Muthuswamy’s lab has ongoing collaborations with the Tonks lab to investigate and identify novel opportunities for targeting tyrosine phosphatases in HER2-positive breast cancers and with the Spector lab to study the role noncoding RNAs have in breast cancer.

Aranda, V., Haire, T., Nolan, M.E., Calarco, J.P., Rosenberg, A.Z., Fawcett, J.P., Pawson, T., and Muthuswamy, S.K. 2006. Par6-aPKC uncouples ErbB2 induced disruption of polarized epithelial organization from proliferation control. Nat. Cell Biol. 8: 1235–1245. Wang, S.E., Narasanna, A., Perez-Torres, M., Xiang, B., Wu, F.Y., Yang, S., Carpenter, G., Gazdar, A.F., Muthuswamy, S.K., and Arteaga, C.L. 2006. HER2 kinase domain mutation results in constitutive phosphorylation and activation of HER2 and EGFR and resistance to EGFR tyrosine kinase inhibitors. Cancer Cell 10: 25–38.

Zhan, L., Xiang, B., and Muthuswamy, S.K. 2006. Controlled activation of ErbB1/ErbB2 heterodimers promote invasion of three-dimensional organized epithelia in an ErbB1-dependent manner: implications for progression of ErbB2-overexpressing tumors. Cancer Res. 66: 5201–5208.

Xiang, B., and Muthuswamy, S.K. 2006. Using three-dimensional acinar structures for molecular and cell biological assays. Methods Enzymol. 406: 692–701.

Archived Publications