Associate, Department of Biochemistry
Quantifying Immune Function Networks.
The goal of my research is to understand how the Immune system responds to infections and cancers. Currently, I am focusing on developing new technology to characterize and quantify the surface characteristics of human cells using antibodies that recognize particular heparan sulfate structures. These ubiquitous polysaccharides are often described as the most complex molecules in nature. They have the potential to provide each cell type with a unique surface signature. The ability to discriminate functionally distinct cell types and purify them by their surface characteristics has fundamental and far-reaching importance to biomedical research. This technology could provide the ability to identify unique cellular phenotypes and follow phenotypic dynamics with unprecedented precision.
Decyphering the Heparan sulfate Code.
As stated above, Heparan sulfates (HS) are often described as the most complex families of molecules found in nature. How this complexity arises and functions in human health are one of the main focuses of my research program. HSs are complex and heterogeneous polysaccharides found on the surfaces of virtually all animal cells. The complexity arises from modification by de-acetylation, epimerization and sulfation reactions that are catalyzed by an evolutionarily conserved network of enzymes. These modification patterns can be cell and tissue specific. How the heterogeneity of HS arises has not been fully explained but is thought to result because the biosynthesis of HS is non-templated, as well as some inherently stochastic aspect of the modification processes.
Visualizing intercellular communication during neural circuit formation.
The form and function of neurons within the nervous system is governed by their surface characteristics and arises as a result of intercellular signaling networks. One important structural unit of a neuron is the ‘tree like’ region termed the Dendritic Arbor. We have undertaken a physical and biochemical analysis of a novel conserved, tri-molecular complex that is necessary for proper formation of dendritic arbors during sensory innervation of the skin.
10. Townley RA and Bülow HE. Genetic analysis of the heparan modification network in Caenorhabditis elegans. J Biol Chem. 2011 May 13;286(19):16824-31. 21454666
9. Bhattacharya R, Townley RA, Berry K, Bülow HE. The PAPS Transporter PST-1 is required for Heparan sulfation and is essential for viability and neural development. J. Cell Sci. 2009 Dec 15;122 (Pt 24):4492-504. 19920077
8. Bülow HE, Tjoe N, Townley RA, Didiano D, van Kuppevelt TH, Hobert O. Extracellular sugar modifications provide instructive and cell-specific information for axon-guidance choices. Curr Biol. 2008 Dec 23;18(24): 1978-85. 19062279
7. Jin X, Townley R, Shapiro L. Structural insight into AMPK regulation: ADP comes into play. Structure. 2007 Oct; 15(10): 1285-95. 17937917
6. Townley R and Shapiro L. Crystal Structures of the Adenylate Sensor from Fission Yeast AMP-Activated Protein Kinase. Science. 2007 Mar 23;315 (5819): 1726-9 . 17289942
5. Hedbacker K, Townley R, Carlson M. Cyclic AMP-dependent protein kinase regulates the subcellular localization of Snf1-Sip1 protein kinase. Mol Cell Biol. 2004 Mar; 24(5): 1836-43. 14966266
4. Vincent O, Kuchin S, Hong SP, Townley R, Vyas VK, Carlson M. Interaction of the Srb10 kinase with Sip4, a transcriptional activator of gluconeogenic genes in Saccharomyces cerevisiae. Mol Cell Biol. 2001 Sep; 21(17): 5790-6. 11331606
3. Vincent O, Townley R, Kuchin S, Carlson M. Subcellular localization of the Snf1 kinase is regulated by specific beta subunits and a novel glucose signaling mechanism. Genes Dev. 2001 May 1; 15(9): 1104-14. 11486018
2. Tirabassi RS, Townley RA, Eldridge MG, Enquist LW. Characterization of pseudorabies virus mutants expressing carboxy-terminal truncations of gE: evidence for envelope incorporation, virulence, neurotropism domains. J Virol. 1997 Sep; 71(9): 6455-64. 9261363
1. Brough DE, Hofmann TJ, Ellwood KB, Townley RA, Cole MD. An essential domain of the c-myc protein interacts with a nuclear factor that is also required for E1A-mediated transformation. Mol Cell Biol. 1995 Mar; 15(3): 1536-44. 7862146
Material in this section is provided by individual faculty members who are solely responsible for its accuracy and content.
Albert Einstein College of Medicine
Michael F. Price Center
1301 Morris Park Avenue , Room 313
Bronx, NY 10461