Jameson David M.

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David M. Jameson


Professor, Department of Cell and Molecular Biology John A. Burns School of Medicine University of Hawaii

Our laboratory utilizes fluorescence methodologies to elucidate dynamic aspects of biomolecules. We are currently studying dynamin, a large (98kDa) GTPase which functions to “pinch-off” membrane vesicles in pathways such as receptor mediated endocytosis and synaptic vesicle recycling. We carry out both in vitro and in vivo studies on the self-association modes of dynamin as well as its interaction with membranes and other proteins such as endophilin and Arc/Arg3.1. We have also been studying dynamins with mutations that cause motor disorders, specifically Centronuclear Myopathy and Charcot-Marie-Tooth disease. These studies, both in vitro and in living cells, are aimed at understanding the molecular basis for dynamin’s involvement in these disorders. We also have a project on Botulinum Neurotoxin which involves biophysical studies on proteins forming the neurotoxin complex as well as development of in vitro and in vivo toxin assays based on Fluorescence Fluctuation Spectroscopy. Recently we have been developing the application of the phasor method, a visual approach to treatment of time-resolved fluorescence data, to in vitro systems such as intrinsic protein fluorescence and membrane systems.

Recent Publications

1. Jameson, D.M. and Ross, J.A. (2010) Chem. Rev. 110:2685-2708. Fluorescence Polarization/Anisotropy in Clinical Diagnostics and Imaging.[1]

2. Wang, L., Barylko, B., Byers, C., Ross, J.A., Jameson, D.M, and Albanesi, J.P. (2010) J. Biol. Chem. 285:22753-22757. Dynamin 2 mutants linked to centronuclear myopathies form abnormally stable polymers.[2]

3. Barylko, B., Wang, L., Binns, D.D., Ross, J.A., Tassin, T., Collins, K., Jameson, D.M. and Albanesi, J.P. (2010) Biochemistry 49:10592-10594. The Proline-Arginine Rich Domain (PRD) is a Major Determinant of Dynamin Self-Activation.[3]

4. Stefl, M., James, N.G., Ross, J.A. and Jameson, D.M. (2011) Anal. Biochem. 410:62-69. Application of Phasor Plots to In Vitro Time-Resolved Fluorescence Measurements.[4]

5. James, N.G., Ross, J.A., Stefl, M. and Jameson, D.M. (2011) Anal. Biochem. 410:70-76. Application of Phasor Plots to In Vitro Protein Studies.[5]

6. Ross, J.A., Digman, M.A., Gratton, E., Albanesi, J.P. and Jameson, D.M. (2011) Biophysical. J. 100:L15-17. Oligomerization State of Dynamin 2 in Cell Membranes Using TIRF and Number and Brightness Analysis.[6]

7. Ross, J.A., Chen, Y., Mueller, J., Barylko, B., Wang, L., Banks, H.B., Albanesi, J.P. and Jameson, D.M. (2011) Biophysical J. 100:729-37. Dimeric Endophilin A2 Stimulates Assembly and GTPase Activity of Dynamin 2.[7]

8. Ross, J.A., Gilmore, M.A., Williams, D., Aoki, K.R., Steward, L.E. and Jameson, D.M. (2011) Anal. Biochem. 413: 43-49. Characterization of Förster resonance energy transfer in a botulinum neurotoxin protease assay.[8]

9. Gilmore, M.A., Williams, D., Okawa, Y., Holguin, B., James, N.G., Ross, J.A., Aoki, R.K., Jameson, D.M. and Steward, L.E. (2011) Anal. Biochem. 413:36-42. Depolarization after resonance energy transfer (DARET): A sensitive fluorescence-based assay for botulinum neurotoxin protease activity.[9]

10. Zakharov, M.N., Ulloor, J., Bhasin, S., Ross, J.A., Narula, N.S., Bakhit, M., Pillai, B.K., Kumar, R., Jameson, D.M. and Jasuja, R. (2011) Anal. Biochem. 416:126-128. Guanidinium chloride-induced spectral perturbations of 4,4'-dianilino-1,1'-binaphthyl-5,5'-disulfonic acid confound interpretation of data on molten globule states.[10]

11. Buscaglia, R., Jameson, D.M. and Chaires, J.B. (2012) Nucleic Acids Res. 40:4203-4215. G-Quadruplex structure and stability illuminated by 2-aminopurine phasor plots.[11]

12. Montecinos-Franjola, F., Ross, J.A., Sanchez, S., Brunet, J.E., Lagos, R , Jameson, D.M. and Monasterio, O. (2012) Biophysical J. 102:2176-2185. Spontaneous Dissociation and Unfolding of E. Coli FtsZ Supports the Dimer Nucleus Polymerization Model.[12]

13. James, N.G. Digman, M.A., Gratton, E., Barylko, B., Ding, X., Albanesi, J.P., Goldberg, M.S. and Jameson, D.M. (2012) Biophys J.102:L41-3. Number and Brightness Analysis of LRRK Oligomerization in Live Cells.[13]

14. Jameson, D.M., James, N.G. and Albanesi, J.P. (2013) Methods Enzymol. 519:87-113. Fluorescence Fluctuation Analysis Approaches to the Study of Receptors in Live Cells.

15. Jameson, D.M., Vetromile, C.M. and James, N.G. (2013) Methods 59:278-286. Investigations of protein-protein interactions using time-resolved fluorescence and phasors.[14]

16. James, N.G., Digman, M.A., Ross, J.A., Barylko, B., Wang, L., Li, J., Chen, Y., Mueller, J.D., Gratton, E., Albanesi, J.P. and Jameson, D.M. (2014) Biochim Biophys Acta. 1840:315-321. A mutation associated with centronuclear myopathy enhances the size and stability of dynamin 2 complexes in cells.[15]

17. James, N.G. and Jameson, D.M. (2014) Methods Mol Biol. 1076:29-42. Steady-state fluorescence polarization/anisotropy for the study of protein interactions.[16]

18. Vetromile, C.M. and Jameson, D.M. (2014) Methods Mol Biol. 1076:77-95. Frequency domain fluorometry: theory and application.[17]

19. Montecinos-Franjola, F., James, N.G., Concha-Marambio, L., Brunet, J.E., Lagos, R., Monasterio, O., Jameson, D.M. (2014) Biochim Biophys Acta. 1844(7):1193-200. Single tryptophan mutants of FtsZ: Nucleotide binding/exchange and conformational transitions.[18]

20. Reilly, S.M., Lyons, D.F., Wingate, S.E., Wright, R.T., Correia, J.J., Jameson, D.M. and Wadkins, R.M. (2014) Biophys J. 107(7):1703-11. Folding and hydrodynamics of a DNA i-motif from the c-MYC promoter determined by fluorescent cytidine analogs.[19]

21. Ranjit, S., Dvornikov, A., Holland, D.A., Reinhart, G.D., Jameson, D.M. and Gratton, E. (2014) J Phys Chem B. 118(50):14627-31. Application of three-photon excitation FCS to the study of protein oligomerization.[20]

22. Lopes, J.L.S., Araujo, A.P.U., Beltramini, L.M. and Jameson, D.M. (2015) Investigation of the conformational flexibility of DGAT1 peptides using tryptophan fluorescence. Methods Appl. Fluore. 025003.[21]

23. Byers, C.E., Barylko, B., Ross, J.A., Southworth, D.R., James, N.G., Taylor IV, C.A., Wang, L., Collins, K.A., Estrada, A., Waung, M., Tassin, T.C., Huber, K.M., Jameson, D.M. and Albanesi, J.P. (2015) Enhancement of dynamin polymerization and GTPase activity by Arc/Arg3.1. Biochem. Biophys. Acta. 1850:1310-8.


24. Malacrida, L., Gratton, E. and Jameson, D.M. (2015) Model-free methods to study membrane environmental probes: A comparison of the spectral phasor and generalized polarization approaches. Methods Appl Fluores 3:047001.[23]

25. Lopes, J.L., Yoneda, J.S., Martins, J.M., DeMarco, R., Jameson, D.M., Castro, A.M., Bossolan, N.R., Wallace, B.A. and Araujo, A.P. (2016) Environmental Factors Modulating the Stability and Enzymatic Activity of the Petrotoga mobilis Esterase (PmEst). PLoS One. 11(6):e0158146[24]

26. Jameson, D.M. (2016) A Fluorescent Lifetime: Reminiscing About Gregorio Weber in Perspectives in Fluorescence: A Tribute to Gregorio Weber. Springer Series on Fluorescence, Springer International Publishing, Switzerland.



Fluorescent Biomolecules: Methodologies and Applications, (1989) D.M. Jameson and G.D. Reinhart, eds. Plenum Press, N.Y.

Perspectives on Fluorescence: A Tribute to Gregorio Weber (2016) D.M. Jameson, ed., Springer, Heidelberg, Germany


Wong, S.S. and Jameson, D.M. Chemistry of Protein and Nucleic Acid Cross-Linking and Conjugation, 2012, Taylor and Francis, New York, NY.

Jameson, D.M. Introduction to Fluorescence, 2014. Taylor and Francis, New York, NY.