T. Chris Gamblin

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.


Teaching Interests

  • Biochemistry
  • Neurobiology
  • Cell biology

Research Interests

  • Neurodegeneration
  • Alzheimer's disease
  • Biochemistry

Selected Publications

Bardai, F H, L Wang, Y Mutreja, M Yenjerla, T C Gamblin, and M B Feany. “A Conserved Cytoskeletal Signaling Cascade Mediates Neurotoxicity of FTDP-17 Tau Mutations In Vivo.” Journal Articles. The Journal of Neuroscience : The Official Journal of the Society for Neuroscience 38, no. 1 (January 3, 2018): 108–19. https://doi.org/10.1523/JNEUROSCI.1550-17.2017.
Mutreja, Y, and T C Gamblin. “Optimization of in Vitro Conditions to Study the Arachidonic Acid Induction of 4R Isoforms of the Microtubule-Associated Protein Tau.” Journal Articles. Methods in Cell Biology 141 (June 14, 2017): 65–88. https://doi.org/10.1016/bs.mcb.2017.06.007.
Paranjape, S R, A P Riley, A D Somoza, C E Oakley, C C Wang, T E Prisinzano, B R Oakley, and T C Gamblin. “Azaphilones Inhibit Tau Aggregation and Dissolve Tau Aggregates in Vitro.” Journal Articles. ACS Chemical Neuroscience, April 15, 2015. https://doi.org/10.1021/acschemneuro.5b00013.
Paranjape, S R, Y M Chiang, J F Sanchez, R Entwistle, C C Wang, B R Oakley, and T C Gamblin. “Inhibition of Tau Aggregation by Three Aspergillus Nidulans Secondary Metabolites: 2,ω-Dihydroxyemodin, Asperthecin, and Asperbenzaldehyde.” Journal Articles. Planta Medica 80, no. 1 (January 1, 2014): 77–85. https://doi.org/10.1055/s-0033-1360180.
Combs, B., and T. C. Gamblin. “FTDP-17 Tau Mutations Induce Distinct Effects on Tau Aggregation and Microtubule Interactions.” Journal Articles. Biochemistry 51, no. 43 (2012): 8597–8607. https://doi.org/10.1021/bi3010818.
Voss, K., B. Combs, K. R. Patterson, L. I. Binder, and T. C. Gamblin. “Hsp70 Alters Tau Function and Aggregation in an Isoform Specific Manner.” Journal Articles. Biochemistry 51, no. 4 (2012): 888–98. https://doi.org/10.1021/bi2018078.
Moore, C. L., M. H. Huan, S. A. Robbennolt, K. R. Voss, B. Combs, T. C. Gamblin, and W. J. Goux. “Secondary Nucleating Sequences Affect Kinetics and Thermodynamics of Tau Aggregation.” Journal Articles. Biochemistry 50, no. 50 (November 20, 2011): 10876–86. https://doi.org/10.1021/bi2014745.
Patterson, K. R., S. M. Ward, B. Combs, K. Voss, N. M. Kanaan, G. Morfini, S. T. Brady, T. C. Gamblin, and L. I. Binder. “Heat Shock Protein 70 Prevents Both Tau Aggregation and the Inhibitory Effects of Preexisting Tau Aggregates on Fast Axonal Transport.” Journal Articles. Biochemistry 50, no. 47 (October 29, 2011): 10300–310. https://doi.org/10.1021/bi2009147.
Combs, B., K. Voss, and T. C. Gamblin. “Pseudohyperphosphorylation Has Differential Effects on Polymerization and Function of Tau Isoforms.” Journal Articles. Biochemistry 50, no. 44 (October 8, 2011): 9446–56. https://doi.org/10.1021/bi2010569.
Sun, Q., and T. C. Gamblin. “Pseudohyperphosphorylation Causing AD-like Changes in Tau Has Significant Effects on Its Polymerization.” Journal Articles. Biochemistry 48, no. 25 (May 30, 2009): 6002–11. https://doi.org/10.1021/bi900602h.
Voss, K., and T. C. Gamblin. “GSK-3β Phosphorylation of Functionally Distinct Tau Isoforms Has Differential, but Mild Effects.” Journal Articles. Molecular Neurodegeneration 4 (2, 2009): 18. https://doi.org/10.1186/1750-1326-4-18.
Rankin, C. A., and T. C. Gamblin. “Assessing the Toxicity of Tau Aggregation.” Journal Articles. Journal of Alzheimer’s Disease 14, no. 4 (July 2008): 411–16.
Rankin, C. A., Q. Sun, and T. C. Gamblin. “Pre-Assembled Tau Filaments Phosphorylated by GSK-3β Form Large Tangle-like Structures.” Journal Articles. Neurobiology of Disease 31, no. 3 (2008): 368–77.
Carlson, S. W., M. Branden, K. Voss, Q. Sun, C. A. Rankin, and T. C. Gamblin. “A Complex Mechanism for Inducer Mediated Tau Polymerization.” Journal Articles. Biochemistry 46 (June 31, 2007): 8838–49.
Rankin, C. A., Q. Sun, and T. C. Gamblin. “Tau Phosphorylation by GSK3 Promotes Tangled Filament Morphology.” Journal Articles. Molecular Neurodegeneration 2 (May 28, 2007): 12.

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