The Vizcarra group investigates how actin, the most abundant protein in many cells, is regulated to perform its impressive list of cellular roles. We employ biochemical techniques, spectroscopy, and high-resolution microscopy with three primary research goals: (1) understanding cytoskeletal regulators that are associated with inherited deafness, (2) developing small molecules that inhibit specific formin proteins and functions, and (3) studying how the metal binding protein metallothionein-3 modulates the actin cytoskeleton in response to lead exposure.
This work is funded by the Research Corporation for Science Advancement, the NIH National Institute on Deafness and Other Communication Disorders, and the NSF Divisions of Chemistry and Biological Infrastructure.
CHEM BC1003, Chemical Problem Solving
CHEM BC3282, Biological Chemistry I
CHEM BC3283, Biological Chemistry II
CHEM BC3348, Advanced Spectroscopy Laboratory
CHEM BC3355, Biochemistry Laboratory Techniques
Related to current research:
Silkworth WT, Kunes KL, Nickel GC, Phillips, ML, Quinlan ME, and Vizcarra CL. The neuron specific formin Delphilin nucleates but does not enhance actin filament elongation. Mol. Biol. Cell 2018, 29: 610.
Vizcarra CL, Quinlan ME. Actin filament assembly by bacterial factors VopL/F: Which end is up? J. Cell Biol. 2017 216: 1211–1213.
Metavinculin tunes the flexibility and the architecture of vinculin-induced bundles of actin filaments. Oztug Durer ZA, McGillivary RM, Kang H, Elam WA, Vizcarra CL, Hanein D, De La Cruz EM, Reisler E, Quinlan ME, J. Mol. Biol. 2015 427: 2782–2798.
The role of formin tails in actin nucleation, processive elongation, and filament bundling. Vizcarra CL, Bor B, and Quinlan ME, J. Biol. Chem. 2014 289: 30602–30613.
Interaction between microtubules and the Drosophila formin Cappuccino and its effect on actin assembly. Roth-Johnson EA, Vizcarra CL, Bois JS, and Quinlan ME, J. Biol. Chem. 2013, 289: 4395–4404.
Autoinhibition of the formin Cappuccino in the absence of canonical autoinhibitory domains. Bor B, Vizcarra CL, Phillips ML, and Quinlan ME, Mol. Biol. Cell 2012 23: 3801–3813.
Structure and function of the interacting domains of Spire and Fmn-family formins. Vizcarra CL*, Kreutz B*, Rodal AA, Toms AV, Lu J, Zheng W, Quinlan ME, and Eck MJ, Proc. Natl. Acad. Sci. USA 2011 108: 11884–11889. *equal contribution
Comparison of random mutagenesis and semi-rational designed libraries for improved cytochrome P450 BM3- catalyzed hydroxylation of small alkanes. Chen MM, Snow CD, Vizcarra CL, Mayo SL, and Arnold FH, Protein Eng. Des. Sel. 2012 25: 171–178.
An improved pairwise decomposable finite difference Poisson-Boltzmann method for computational protein design. Vizcarra CL, Zhang N, Marshall SA, Wingreen N, Zeng C, and Mayo SL, J. Comp. Chem. 2008 29: 1153–1162.
Computationally designed libraries of fluorescent proteins evaluated by preservation and diversity of function. Treynor TP, Vizcarra CL, Nedelcu D, and Mayo SL (2007). Proc Natl Acad Sci USA 2007 104: 48–53.
One- and two-body decomposable Poisson- Boltzmann methods for protein design calculations. Marshall SA, Vizcarra CL, and Mayo SL, Protein Sci 2005 14: 1293–1304.
Electrostatics in Computational Protein Design. Vizcarra CL and Mayo SL, Curr. Opin. Chem. Biol. 2005 9: 622–629.