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Tatyana Igumenova

Igumenova, Tatyana
Tatyana Igumenova
Associate Professor and Director of the Biomolecular NMR Facility
NMR / Room N118A
Graduate Education
Ph.D. Columbia University, 2003
Postdoc. University of Pennsylvania, 2003-2005
Postdoc. Columbia University, 2005-2007
Joined Texas A&M in 2008
NSF CAREER Award 2012
Ralph E. Powe Junior Faculty Award 2010

Structural biology of peripheral membrane proteins involved in signal transduction

My laboratory is broadly interested in understanding the structural basis of signal transduction events that occur at the membrane surface. These events are mediated by signaling proteins that reversibly associate with membranes in response to binding second messengers, such as Ca2+ ions, diacylglycerol, and phosphoinositides. One of the key kinases regulating these signal transduction pathways is the Protein Kinase C (PKC) family. Aberrant levels of PKC expression or activity have been implicated in a large number of human diseases, such as cancer, cardiac failure, Alzheimer’s disease, and diabetes. Despite the significance of PKC in signal transduction and human health, the structural and dynamical basis of its activation upon binding to lipid membranes remains elusive.


The ultimate objective of our studies is to understand how PKCs function at the atomic level. Our experimental approach is multi-faceted. We primarily rely on advanced Nuclear Magnetic Resonance (NMR) spectroscopy techniques, but also use fluorescence spectroscopy, X-ray crystallography, and computational methods to gain insight into various aspects of structure, dynamics, and function of PKC. We anticipate that our studies will inform and facilitate the design of agents that modulate the PKC activity for both therapeutic and research purposes. A related area of interest is the fundamental biophysics of peripheral lipid-binding domains that target their host proteins to membranes.

Recent Publications

  1. Katti, S, Nyenhuis, SB, Her, B, Cafiso, DS, Igumenova, TI. Partial Metal Ion Saturation of C2 Domains Primes Synaptotagmin 1-Membrane Interactions. Biophys. J. 2020;118 (6):1409-1423.
    doi: 10.1016/j.bpj.2020.01.032. PubMed PMID:32075747. PubMed Central PMC7091512.

  2. Katti, S, Igumenova, TI. Interference of pH buffer with Pb2+-peripheral domain interactions: obstacle or opportunity? Metallomics. 2020;12 (2):164-172.
    doi: 10.1039/d0mt00002g. PubMed PMID:32051983. .

  3. Cole, TR, Erickson, SG, Morales, KA, Sung, M, Holzenburg, A, Igumenova, TI et al.. Cd(II)- and Pb(II)-Induced Self-Assembly of Peripheral Membrane Domains from Protein Kinase C. Biochemistry. 2019;58 (6):509-513.
    doi: 10.1021/acs.biochem.8b01235. PubMed PMID:30584764. .

  4. Katti, S, Her, B, Srivastava, AK, Taylor, AB, Lockless, SW, Igumenova, TI et al.. High affinity interactions of Pb2+ with synaptotagmin I. Metallomics. 2018;10 (9):1211-1222.
    doi: 10.1039/c8mt00135a. PubMed PMID:30063057. PubMed Central PMC6146066.

  5. Yang, Y, Shu, C, Li, P, Igumenova, TI. Structural Basis of Protein Kinase Cα Regulation by the C-Terminal Tail. Biophys. J. 2018;114 (7):1590-1603.
    doi: 10.1016/j.bpj.2017.12.030. PubMed PMID:29642029. PubMed Central PMC5954273.

  6. Katti, S, Nyenhuis, SB, Her, B, Srivastava, AK, Taylor, AB, Hart, PJ et al.. Non-Native Metal Ion Reveals the Role of Electrostatics in Synaptotagmin 1-Membrane Interactions. Biochemistry. 2017;56 (25):3283-3295.
    doi: 10.1021/acs.biochem.7b00188. PubMed PMID:28574251. PubMed Central PMC5600830.

  7. Stewart, MD, Igumenova, TI. Toggling of Diacylglycerol Affinity Correlates with Conformational Plasticity in C1 Domains. Biochemistry. 2017;56 (21):2637-2640.
    doi: 10.1021/acs.biochem.7b00228. PubMed PMID:28505428. PubMed Central PMC5600822.

  8. Morales, KA, Yang, Y, Cole, TR, Igumenova, TI. Dynamic Response of the C2 Domain of Protein Kinase Cα to Ca2+ Binding. Biophys. J. 2016;111 (8):1655-1667.
    doi: 10.1016/j.bpj.2016.09.008. PubMed PMID:27760353. PubMed Central PMC5071625.

  9. Igumenova, TI. Dynamics and Membrane Interactions of Protein Kinase C. Biochemistry. 2015;54 (32):4953-68.
    doi: 10.1021/acs.biochem.5b00565. PubMed PMID:26214365. PubMed Central PMC4979571.

  10. Ghosh, R, de Campos, MK, Huang, J, Huh, SK, Orlowski, A, Yang, Y et al.. Sec14-nodulin proteins and the patterning of phosphoinositide landmarks for developmental control of membrane morphogenesis. Mol. Biol. Cell. 2015;26 (9):1764-81.
    doi: 10.1091/mbc.E14-10-1475. PubMed PMID:25739452. PubMed Central PMC4436786.

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