Marija Zanic
Vanderbilt University, TN·Biophysics
Inside every cell is a scaffolding of hollow protein tubes called microtubules that must constantly be torn down and rebuilt so the cell can divide, crawl, or specialize. Individual microtubules do this by flipping unpredictably between growing and rapidly falling apart, a behavior known as dynamic instability.
- Fields
Biophysics
Biology
Biochemistry
- Topics
microtubules
dynamic instability
catastrophe
- Grants
- 1 known grant, through Dec 2026
What they work on
- Test whether the conditions a microtubule experiences during growth have long-term effects on its later catastrophe, shrinkage and rescue, using in vitro reconstitution with purified tubulin, microfluidics to switch conditions, and high-resolution light microscopy.
- Compare how distinct growth conditions at the plus and minus ends of a microtubule give rise to their different dynamic behaviors, focusing on regulators that bind both soluble tubulin and the polymer.
- Determine why the TOG-domain proteins XMAP215 and CLASP, despite similar architecture, have different effects on plus-end dynamics, by dissecting their individual and combined mechanisms.
- Dissect the interplay at the minus end between the stabilizing motor Kinesin-14 HSET and destabilizing factors, the tubulin-sequestering protein Op18/Stathmin and the severing enzyme Fidgetin.
- Develop mathematical and computational models that reconcile dynamics at both microtubule ends and the collective effects of multiple regulators, then test their predictions with fast quantitative super-resolution live-cell imaging.
- Examine the role of CLASP in cell migration and neuronal development in cells, using the resulting observations to generate new hypotheses for controlled in vitro and in silico experiments.
More about the research
The switch from growth to shrinkage (catastrophe) and the reverse rescue of a shrinking tube were described decades ago, but what actually triggers them, and how dozens of regulatory proteins acting together tune them, remain open. This project aims to pin down those mechanisms, working from the central hypothesis that the conditions a microtubule experiences while it grows leave a lasting imprint that shapes how and when it later undergoes catastrophe, shrinkage and rescue.
Why it matters
Microtubules are the target of widely used chemotherapy drugs, and every regulator examined here has been implicated in human disease, particularly cancers and neurodevelopmental disorders. Understanding at a molecular level what makes microtubules switch between growth and collapse, and how proteins such as CLASP, HSET, Stathmin and Fidgetin tune that switch, could clarify how such drugs work and how mutations in these proteins disrupt cell division, cell migration and neuronal development.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Tarun M. Kapoor
Rockefeller University, NY·Biochemistry
Determine the functions of different AAA mechanoenzymes (force-generating proteins powered by ATP) during human cell division and how they are regulated, by rapidly switching them off with chemical inhibitors and imaging the effects with lattice light-sheet microscopy.
Comert Kural
Ohio State University, OH·Biophysics
Build and iteratively optimize a 3D TIRF-SIM microscope, combining surface-limited illumination, patterned-light super-resolution and evanescent field nanometry, for the best spatial and temporal resolution.
Naomi Courtemanche
University of Minnesota, MN·Biochemistry
Determine the mechanism that lets formins, proteins that both start and lengthen actin filaments, adjust their polymerization activity across isoforms, using biophysical measurements.
The school
Vanderbilt University: 22 labs on PI Pages, $1.3B a year on research, 494 research doctorates a year.
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