Boston University Department of Biology

Faculty Profiles

Current Research

My research focuses on understanding the cellular and molecular mechanisms by which certain genes can transform normal cells into malignant cells, and the normal control of cellular growth by these genes. In particular, we have concentrated on the Rel/NF-kB family of transcription factors, whose activity is altered in a variety of human cancers, especially lymphoid cell cancers. In recent studies, we have found that the human c-rel gene, which is amplified and overexpressed in many human lymphomas, can also malignantly transform avian and human lymphoid cells in tissue culture. Currently, we are identifying target genes that are important for c-Rel transformation, and are developing further model systems to study oncogenesis induced by overexpressed c-Rel.

In collaborative studies with Dr. John Porco in the Chemistry Department at Boston University, we are also characterizing natural and synthetic inhibitors of Rel/NF-kB signaling. Many of these inhibitors are derivatives of fungal metabolites, and may have anti-cancer or anti-inflammatory activities.

Recently, we have been studying the evolutionary origins of the NF-kB pathway by characterizing NF-kB genes and proteins in simple marine organisms, such as the sea anemone Nematostella vectensis. This research may have relevance to the mechanisms by which simple marine organisms deal with the environmental stress that is currently impacting sensitive marine ecosystems. These studies are being carried out in collaboration with Drs. Les Kaufman and John Finnerty (Biology Department, Boston University).

Courses Taught

• BB522 Molecular Biology Laboratory

Selected Publications

• Chin M, Herscovitch M, Zhang N, Waxman DJ, Gilmore TD (2009). Overexpression of an activated version of the REL oncoprotein enhances the oncogenie properties of the human B-lymphoma BJAB cell line and alters its gene expression prolife. Oncogene, in press
• Leeman JR, Weniger MA, Barth TF, Gilmore TD. (2008). Deletion analysis and alternative splicing define a transactivation inhibitory domain in human oncoprotein REL. Oncogene 27, 6770-6781
• Leeman & TD Gilmore. (2008). Alternative splicing in the NF-kB signaling pathway. Gene, 423, 97-107
• Garbati MR & TD Gilmore. (2008). Ser484 and Ser494 in REL are the major sites of IKK phosphorylation in vitro: evidence that IKK does not directly enhance GAL4-REL transactivation. Gene Expression 14, 195-205
• Herscovitch M, Comb W, Ennis T, Coleman K, Yong S, Armstead B, Kalaitzidis D, Chandani S, Gilmore TD (2008). Intermolecular disulfide bond formation in the NEMO dimer requires Cys54 and Cys347. Biochemical and Biophysical Research Communications 367, 103-108
• Gilmore TD. (2007). Multiple myeloma: lusting for NF-kB. Cancer Cell 12, 95-97
• Starzynowski DT, Trautmann H, Pott C, Harder L, Arnold N, Africa JA, Leeman JR, Siebert R, Gilmore TD (2007). Mutation of an IKK phosphorylation site within the transactivation domain of REL in two patients with B-cell lymphoma enhances REL’s in vitro transforming activity. Oncogene 26, 2685-2694
• Sullivan JC, Kalaitzidis D, Gilmore TD, Finnerty JR (2007). Rel homology domain-containing transcription factors in the cnidarian Nematostella vectensis. Development Genes and Evolution 217, 63-72