Antonina Roll-Mecak, Ph.D.

Senior Investigator

Cell Biology and Biophysics Section


Building 35, Room 3B203
35 Convent Drive
Bethesda, MD 20892-3700


Research Topics

In addition to providing structural support, microtubules form a complex and dynamic intracellular "highway" that delivers molecular cargo from one end of the cell to another -which in the case of neuronal cells can span several feet. Given the continually changing cell physiology, this delivery system undergoes constant remodeling as cargo is transported to different destinations with high temporal and spatial accuracy. Failures in this highly coordinated transport system lead to disease and mutations in genes that encode microtubule dynamics regulators have been implicated in neurodegeneration, cardiovascular disease, cancers and viral infections.

Not surprisingly, tubulin, the building block of the microtubule network is one of the most post-translationally modified proteins in the cell. My laboratory combines biophysical and cell biological approaches to understand the interplay between microtubules and their regulators and how the chemical complexity of microtubules tunes the behavior of motors and microtubule associated proteins. Despite the abundance and complexity of tubulin modifications, their effects on microtubule behavior are still poorly understood. Is the microtubule more than just a structural strut, or a naive roadway for cellular components to transit along? Is there a "tubulin code", written in the rich language of the post-translational modifications of tubulin that, much like a histone code, provides specificity and regulation to cellular dynamics and to the trafficking of motor proteins and their cargo on the cellular highway? How functional diversity is imparted to different microtubules is a central question in cell biology with important implications for human health.


Dr. Roll-Mecak received her undergraduate degree in chemical engineering from The Cooper Union for the Advancement of Science and Art in 1996. She pursued her graduate training in Stephen Burley's laboratory and received her Ph.D. in molecular biophysics from the Rockefeller University in 2002. Her structural and biochemical studies on translation GTPases helped elucidate the mechanism of assembly of translationally competent ribosomes. She conducted her postdoctoral training with Ron Vale at the University of California, San Francisco where she investigated the mechanism of macromolecular machines that regulate the microtubule cytoskeleton. Dr. Roll-Mecak joined NINDS and NHLBI as an investigator in 2010. Dr. Roll-Mecak received for her work a Searle Scholar Award, a Burroughs Wellcome Career Award in Biomedical Sciences, a L'Oreal for Women in Science Fellowship Award, a Pathway to Independence Award (K99), a Damon Runyon Cancer Research Postdoctoral Fellowship, a Hillblom Foundation Fellowship and was awarded the Henry W. Reddick Fund Prize and Medal for Mathematics. Her lab combines biophysical and cell biological approaches to understand the mechanism underlying intracellular organization and movement, with a focus on the microtubule cytoskeleton.

Selected Publications

  1. Garnham CP, Vemu A, Wilson-Kubalek EM, Yu I, Szyk A, Lander GC, Milligan RA, Roll-Mecak A. Multivalent Microtubule Recognition by Tubulin Tyrosine Ligase-like Family Glutamylases. Cell. 2015;161(5):1112-1123.

  2. Valenstein ML, Roll-Mecak A. Graded Control of Microtubule Severing by Tubulin Glutamylation. Cell. 2016;164(5):911-21.

  3. Vemu A, Atherton J, Spector JO, Szyk A, Moores CA, Roll-Mecak A. Structure and Dynamics of Single-isoform Recombinant Neuronal Human Tubulin. J Biol Chem. 2016;291(25):12907-15.

  4. Zehr E, Szyk A, Piszczek G, Szczesna E, Zuo X, Roll-Mecak A. Katanin spiral and ring structures shed light on power stroke for microtubule severing. Nat Struct Mol Biol. 2017;24(9):717-725.

  5. Vemu A, Szczesna E, Zehr EA, Spector JO, Grigorieff N, Deaconescu AM, Roll-Mecak A. Severing enzymes amplify microtubule arrays through lattice GTP-tubulin incorporation. Science. 2018;361(6404).

This page was last updated on March 1st, 2018