Adrian Olivares

From WikidChem

Adrian is a graduate student in the De La Cruz Lab in the department of Molecular Biophysics & Biochemistry.

Contents 1 Education 2 Research 3 Publications 4 Memberships and Societies 5 Links 6 About Adrian

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Education

Yale University, Ph.D., Molecular Biophysics & Biochemistry, May 2008

Baylor University, B.S., Biochemistry, 2001

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Research

Steady state and transient kinetics of myosin motor proteins.

Background and Significance

Myosins compose a large and diverse superfamily of actin-based ATPase motor proteins. Every known myosin class shares the common characteristic of coupling the chemical energy from ATP hydrolysis with mechanical work on the actin cytoskeleton. Two myosin classes, myosin V and myosin VI, share the extra feature of processive motility on actin filaments. This feature is unique to the dimeric (not the monomeric) forms of myosin V and myosin VI and is believed to be important for their cellular function as organelle and vesicle transport motors. Since myosin motility is tightly coupled to ATPase activity, an understanding of the kinetic events that underlie the enzymatic processes of myosin V and myosin VI will help define their mechanisms of processivity.

Calcium Regulation of Full-length Myosin V

Excess calcium activates the ATPase activity and diminishes the in vitro motility of myosin V (isoform a). The effects appear to be more dramatic for full-length myosin V containing two motor subunits (“heads”) than recombinant two-headed myosin V missing its C-terminal cargo-binding “tail”, raising the possibility that the enzymatic properties differ between the two forms. Hydrodynamic and electron microscopic studies show a large conformational change of full-length myosin V in the presence of calcium from a folded (ATPase inhibited) state to an extended (ATPase activated) conformation. The inhibited state likely arises from an interaction of the C-terminal tail with the N-terminal head. Until now, it remained unclear as to what ATPase cycle events were inhibited in the folded conformation. I have helped define the calcium-regulated actin and nucleotide binding properties of full-length myosin V.

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Publications

J. K. Au*, A. O. Olivares*, A. Henn, W. Cao, D. Safer and E. M. De La Cruz. Widely distributed residues in thymosin beta-4 are critical for actin binding. Biochemistry in press (2008). *authors contributed equally

A. O. Olivares, W. Chang, M. S. Mooseker, D. D. Hackney and E. M. De La Cruz. The tail domain of myosin Va modulates actin binding to one head. J. Biol. Chem. 281, 31326-36 (2006).

A. O. Olivares and E. M. De La Cruz. Holding the reins on myosin V. Proc. Natl. Acad. Sci. U.S.A. 102, 13719-20 (2005).

D. E. Hannemann, W. X. Cao, A. O. Olivares, J. P. Robblee and E. M. De La Cruz. Magnesium, ADP, and actin binding linkage of myosin V: Evidence for multiple myosin V-ADP and actomyosin V-ADP states. Biochemistry 44, 8826-40 (2005).

J. P. Robblee*, A. O. Olivares* and E. M. De La Cruz. Mechanism of nucleotide binding to actomyosin VI - Evidence for allosteric head-head communication. J. Biol. Chem. 279, 38608-17 (2004). *authors contributed equally

S. Uemura, H. Higuchi, A. O. Olivares, E. M. De La Cruz and S. Ishiwata. Mechanochemical coupling of two substeps in a single myosin V motor. Nat. Struct. Mol. Biol. 11, 877-83 (2004).

M. B. Hadimani, J. Hua, M. D. Jonklaas, R. J. Kessler, Y. Sheng, A. Olivares, R. P. Tanpure, A. Weiser, J. Zhang, E. Edvardsen, R. R. Kane and K. G. Pinney. Synthesis, in vitro, and in vivo evaluation of phosphate ester derivatives of combretastatin A-4. Bioorg. Med. Chem. Lett. 13, 1505-08 (2003).

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Memberships and Societies

Biophysical Society
member, 2003-present

Society for the Advancement of Native Americans and Chicanos in Science (SACNAS)
member, 2002-present

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Links

• 5th Years and Beyond

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About Adrian

Adrian was born in McAllen, Texas near the border with Mexico. He spent much of his early childhood in Texas but later moved overseas with his family to various countries including Saudi Arabia, Korea, Malaysia, Italy and Kuwait. After receiving his high school diploma from the American School of Kuwait, Adrian returned to Texas to work on a Bachelor's degree at Baylor University. During the summer prior to his senior year, Adrian began work in the lab of Dr. Kevin G. Pinney in the Department of Chemistry and Biochemistry at Baylor. There he synthesized two alkyl derivatives of a disodium phosphate prodrug of combretastatin A-4, a known microtubule depolymerizing agent and potent anti-cancer, anti-tumor natural product analog. His interest in understanding how these synthetic natural product analogs affect biological processes led Adrian to pursue a Ph.D. at Yale.