T. Chris Gamblin

Associate Chair
Post doctoral fellow, Northwestern University, 1998-2002; Ph.D., Vanderbilt University School of Medicine, 1998
Primary office:
(785) 864-5065
5055 Haworth


Role of tau in Alzheimer's and other neurodegenerative disorders.

The presence of abnormal deposits of filamentous tau is thought to be a major part of the neurodegenerative process. For example, the location and amounts of tau pathology in specific regions of the brain correlates with the type and degree of observed dementia in patients. In addition, several mutations in the tau gene have been shown to be directly linked to increased tau pathology and neurodegeneration in familial cases of frontotemporal dementia.

Tau is a microtubule-associated protein that was originally discovered to associate with microtubules and provide stabilization for these structures. However, in the late 1980's, it was discovered that a "hyperphosphorylated" form of tau was the major component of several pathological structures in Alzheimer's disease known as neuropil threads, neurofibrillary tangles, and neuritic plaques. Further characterization of these structures revealed that the tau present in these structures had self-associated into filamentous structures known as straight filaments and paired-helical filaments. Since that time, numerous diseases have been identified as having significant tau pathology such as Pick's disease, progressive supranuclear palsy, and corticobasal degeneration.

The major goal of this laboratory is to understand the molecular mechanisms that lead to the polymerization of the microtubule-associated protein tau into pathological structures observed in Alzheimer's disease and other neurodegenerative disorders. The main thrust of research will involve the detailed investigation of the effects of tau phosphorylation on its ability to polymerize, bind microtubules, and stabilize microtubules. This research will be accomplished using several molecular biology and biochemical approaches, including site-directed mutagenesis, laser light scattering, electron microscopy, and in vitro binding assays.



Ph.D., Molecular Biology, Vanderbilt University

B.S., Recombinant Genetics, Western Kentucky University

Teaching Interests

  • Biochemistry
  • Neurobiology
  • Cell biology

Research Interests

  • Neurodegeneration
  • Alzheimer's disease
  • Biochemistry

Selected Publications

Bardai, F. H., Wang, L. Mutreja, Y. Yenjerla, M. Gamblin, T. C., & Feany, M. B. (2018). A Conserved Cytoskeletal Signaling Cascade Mediates Neurotoxicity of FTDP-17 Tau Mutations In Vivo. The Journal of neuroscience : the official journal of the Society for Neuroscience, 38(1), 108-119. DOI:10.1523/JNEUROSCI.1550-17.2017

Mutreja, Y. & Gamblin, T. C. (2017). Optimization of in vitro conditions to study the arachidonic acid induction of 4R isoforms of the microtubule-associated protein tau. Methods in cell biology, 141, 65-88. DOI:10.1016/bs.mcb.2017.06.007

Paranjape, S. R., Riley, A. P., Somoza, A. D., Oakley, C. E., Wang, C. C., Prisinzano, T. E., Oakley, B. R., & Gamblin, T. C. (2015). Azaphilones Inhibit Tau Aggregation and Dissolve Tau Aggregates in Vitro. ACS chemical neuroscience. DOI:10.1021/acschemneuro.5b00013

Paranjape, S. R., Chiang, Y. M., Sanchez, J. F., Entwistle, R. Wang, C. C., Oakley, B. R., & Gamblin, T. C. (2014). Inhibition of Tau aggregation by three Aspergillus nidulans secondary metabolites: 2,ω-dihydroxyemodin, asperthecin, and asperbenzaldehyde. Planta medica, 80(1), 77-85. DOI:10.1055/s-0033-1360180

Combs, B. & Gamblin, T. C. (2012). FTDP-17 tau mutations induce distinct effects on tau aggregation and microtubule interactions. Biochemistry, 51(43), 8597-8607. DOI:10.1021/bi3010818

Voss, K. Combs, B. Patterson, K. R., Binder, L. I., & Gamblin, T. C. (2012). Hsp70 alters tau function and aggregation in an isoform specific manner. Biochemistry, 51(4), 888-898. DOI:10.1021/bi2018078

Moore, C. L., Huan, M. H., Robbennolt, S. A., Voss, K. R., Combs, B. Gamblin, T. C., & Goux, W. J. (2011). Secondary nucleating sequences affect kinetics and thermodynamics of tau aggregation. Biochemistry, 50(50), 10876-10886. DOI:10.1021/bi2014745

Patterson, K. R., Ward, S. M., Combs, B. Voss, K. Kanaan, N. M., Morfini, G. Brady, S. T., Gamblin, T. C., & Binder, L. I. (2011). Heat shock protein 70 prevents both tau aggregation and the inhibitory effects of preexisting tau aggregates on fast axonal transport. Biochemistry, 50(47), 10300-10310. DOI:10.1021/bi2009147

Combs, B. Voss, K. & Gamblin, T. C. (2011). Pseudohyperphosphorylation has differential effects on polymerization and function of tau isoforms. Biochemistry, 50(44), 9446-9456. DOI:10.1021/bi2010569

Sun, Q. & Gamblin, T. C. (2009). Pseudohyperphosphorylation causing AD-like changes in tau has significant effects on its polymerization. Biochemistry, 48(25), 6002-6011. DOI:10.1021/bi900602h

Voss, K. & Gamblin, T. C. (2009). GSK-3β phosphorylation of functionally distinct tau isoforms has differential, but mild effects. Molecular Neurodegeneration, 4, 18. DOI:10.1186/1750-1326-4-18

Rankin, C. A., Sun, Q. & Gamblin, T. C. (2008). Pre-assembled tau filaments phosphorylated by GSK-3β form large tangle-like structures. Neurobiology of Disease, 31(3), 368-377.

Rankin, C. A., & Gamblin, T. C. (2008). Assessing the toxicity of tau aggregation. Journal of Alzheimer's Disease, 14(4), 411-416.

Carlson, S. W., Branden, M. Voss, K. Sun, Q. Rankin, C. A., & Gamblin, T. C. (2007). A complex mechanism for inducer mediated tau polymerization. Biochemistry, 46, 8838-8849.

Rankin, C. A., Sun, Q. & Gamblin, T. C. (2007). Tau phosphorylation by GSK3 promotes tangled filament morphology. Molecular Neurodegeneration, 2, 12.

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