Dr. Rice received his undergraduate degree from Yale, with a double major in Physics and in American Studies. For two years after that he worked as a scientific programmer in Axel Brunger’s lab at Yale, improving the performance of crystallographic refinement by adopting an algorithm from engineering disciplines that allowed more effective conformational sampling.
Dr. Rice stayed at Yale for his graduate studies in the Department of Molecular Biophysics and Biochemistry, continuing to work with Axel Brunger. His graduate work was mostly focused on biophysical and structural studies of yeast vesicular transport proteins (SNAREs and α-SNAP).
During his postdoctoral work with David Agard at UC San Francisco, Dr. Rice determined atomic structures of γ-tubulin, a specialized tubulin that catalyzes microtubule initiation in vivo. These and other experiments provided new insights into the mechanism of microtubule assembly because they showed, contrary to expectation, that the conformation of tubulins did not change as a function the nucleotide bound.
Dr. Rice joined the faculty of UT Southwestern in the fall of 2007. His lab is broadly focused on developing a comprehensive understanding of microtubule dynamics that connects the properties of individual molecules to the complex polymerization dynamics that emerge - at different length and time scales - from collective interactions among these molecules. A wide range of techniques is being used: X-ray crystallography, time-lapse microscopy, in vitro reconstitution, yeast genetics, biochemisty, computational modeling, and more.
Microtubules are essential, dynamic polymers of αβ-tubulin that are responsible for chromosome segregation, that have key roles in organizing the interior of eukaryotic cells, and that are the direct targets of anti-cancer therapeutics.
We are interested in discovering the connections between biochemical and structural properties of αβ-tubulin and the complex behavior that emerges from their collective interactions. This is a fascinating frontier problem that challenges our ability to integrate 'one molecule at a time' views of biochemistry and structure with lower resolution measurements of collective behavior spanning different length and time scales.
Our studies combine structure, biochemistry, imaging, and computation, and they take advantage of our ability to create and purify mechanistically defining mutants of αβ-tubulin.
- Graduate School
- Yale University (2000), Biochemistry
- Computational modeling
- Microtubule dynamics
- Structural Biology
- X-ray crystallography
- GDP to GTP exchange on the microtubule end can contribute to the frequency of catastrophe.
- Piedra FA, Kim T, Garza ES, Geyer EA, Burns A, Ye X, Rice LM Mol. Biol. Cell 2016 May
- A mutation uncouples the tubulin conformational and GTPase cycles, revealing allosteric control of microtubule dynamics.
- Geyer EA, Burns A, Lalonde BA, Ye X, Piedra FA, Huffaker TC, Rice LM Elife 2015 Oct 4
- A tethered delivery mechanism explains the catalytic action of a microtubule polymerase.
- Ayaz P, Munyoki S, Geyer EA, Piedra FA, Vu ES, Bromberg R, Otwinowski Z, Grishin NV, Brautigam CA, Rice LM Elife 2014 Aug e03069
- A TOG:aß-tubulin Complex Structure Reveals Conformation-Based Mechanisms for a Microtubule Polymerase.
- Ayaz P, Ye X, Huddleston P, Brautigam CA, Rice LM Science 2012 Aug 337 6096 857-60
- Design, overexpression, and purification of polymerization-blocked yeast aß-tubulin mutants.
- Johnson V, Ayaz P, Huddleston P, Rice LM Biochemistry 2011 Oct 50 40 8636-44
- The contribution of aß-tubulin curvature to microtubule dynamics.
- Brouhard GJ, Rice LM J. Cell Biol. 2014 Nov 207 3 323-334
- Regulation of microtubule motors by tubulin isotypes and post-translational modifications.
- Sirajuddin M, Rice LM, Vale RD Nat. Cell Biol. 2014 Apr 16 4 335-44
- The lattice as allosteric effector: structural studies of alphabeta- and gamma-tubulin clarify the role of GTP in microtubule assembly.
- Rice LM, Montabana EA, Agard DA Proc. Natl. Acad. Sci. U.S.A. 2008 Apr 105 14 5378-83
- Insights into microtubule nucleation from the crystal structure of human gamma-tubulin.
- Aldaz H, Rice LM, Stearns T, Agard DA Nature 2005 May 435 7041 523-7