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Mark BowmanMark E. Bowen
Associate Professor

Ph.D. University of Illinois at Chicago, 1998

Basic Science Tower, T-5, Room 124
Stony Brook University
Stony Brook, NY, 11794-8661

Phone: (631) 444-2536
Fax: (631) 444-3432
Email: Mark.Bowen@stonybrook.edu


My lab studies the role of Intrinsically Disordered Proteins (IDPs)in glutamate signaling at the neuronal synapse. Glutamatergic synapses, those using glutamate as a neurotransmitter, are a critical component of the neuronal circuits governing higher brain functions like learning, memory and emotion. Dysfunctional glutamatergic synapses mediate or exacerbate numerous psychiatric diseases. A key to understanding how cells glutamate signals are processed is a description of how protein interactions change in response to synaptic activity. Many of these interactions involve IDPs, which are predicted to be unstructured. This presents a challenge to the current dogma that protein structure defines function.

Our primary approach uses flourescence microscopy to image at the level of single molecules. This allows us to follow the composition, structure and dynamics of individual proteins and complexes involving synaptic IDPs. Single molecule methodology is well suited to clarify the dynamic assembly of multiprotein complexes that govern the synapse. We are developing imaging methodology for protein structure determination to allow previously intractable complexes to be characterized. To complement our in vitro studies, we are turning our microscopes towards live cell imaging of genetically-encoded fluorescent proteins in cell lines and primary neurons which will allow the study of these proteins in vivo.


Salussolia, C. L., A. Corrales, I. Talukder, R. Kazi, G. Akgul, M. Bowen and L. P. Wollmuth (2011). "Interaction of the M4 segment with other transmembrane segments is required for surface expression of mammalian AMPA receptors." J Biol Chem. In press.

Choi, U.B., S. Xiao, Wollmuth, L.P., Bowen, M.E. "Effect of Src Kinase Phosphorylation on Disordered C-terminal Domain of N-Methyl-d-aspartic Acid (NMDA) Receptor Subunit GluN2B Protein." Journal of Biological Chemistry (2011) 286(34): 29904-29912.

McCann J., Zheng, L., Chiantia, S., Bowen, M.E.  “Domain Orientation in the Tandem PDZ Supramodule from PSD-95 is Maintained in the Full-Length Protein” Structure (2011) 19, 810-820

Choi, U.B., McCann J., Weninger, K., Bowen, M.E. “Beyond the random coil: stochastic conformational switching in intrinsically disordered proteins.”  Structure (2011) Apr 13;19(4):566-76. 

Choi, U.B., McCann J., Weninger, K., Bowen, M.E.  “Immobilization of Proteins for Single Molecule Fluorescence Resonance Energy Transfer Measurements of Conformation and Dynamics” in Methods in Molecular Biology: Intrinsically Disordered Proteins: Volume II. Experimental Techniques ed. Keith Dunker & Vladamir Uversky (Humana Press, 2011) In Press

McCann J., Zheng, L., Choi, U.B., Weninger, K., Bowen, M.E.  “Recovering Absolute FRET Efficiency from Immobilized Single Molecules:” Biophysical Journal (2010) Aug 4; 99(3):961-70.

Brunger A. T., Weninger K, Bowen M. E., and Chu S.  “Single molecule studies of the neuronal SNARE fusion machinery”  Annual Reviews of Biochemistry (2009); 78:903-28 

Weninger K., Bowen M.E., Choi U. B., Chu S. and Brunger A.T.; “Accessory proteins stabilize the acceptor complex for synaptobrevin, the 1 : 1 syntaxin/SNAP-25 complex” Structure (2008) Feb;16(2):308-20

Bowen M. and Brunger A.T. “Conformation of the Synaptobrevin Transmembrane Domain”  Proceedings of the National Academy of Sciences (2006) May 30; 103(22): 8378-83 

Dennison S.M., Bowen M., Brunger A.T. and Lentz B.R “Neuronal SNAREs Do Not Trigger Fusion between Synthetic Membranes but Do Promote PEG-Mediated Membrane Fusion.”  Biophysical Journal (2006) 90: 1661-1675