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Vol. LXVI, No. 22
October 24, 2014
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Cell Biologist Vale To Discuss Motor Proteins in Stetten Lecture

Dr. Ron Vale of UCSF

Dr. Ron Vale of UCSF

The interior of our cells teems with purposeful motion akin to the flow of traffic in a major metropolis. Powering this movement are dozens of molecular motors—biological internal combustion engines found in all eukaryotic cells.

This year’s DeWitt Stetten Jr. lecturer, Dr. Ron Vale of the University of California, San Francisco, has long been a leader in devising and integrating biochemical, structural and microscopy-based methods to reveal the inner workings of the motors that drive intracellular movement. He will discuss his innovative research in a talk titled “The Mechanisms of Cytoskeletal Motor Proteins.” Part of the NIH Director’s Wednesday Afternoon Lecture Series and sponsored by NIGMS, the lecture will be held on Wednesday, Oct. 29 at 3 p.m. in Masur Auditorium, Bldg. 10.

Cytoskeletal motor proteins use chemical energy stored in adenosine triphosphate (ATP) to power unidirectional motion along tracks made of actin filaments or microtubules. The proteins perform tasks such as transporting membrane-enclosed organelles to their proper locations in the cell and ensuring the equal partitioning of genetic material during cell division. Vale’s focus is on understanding and manipulating the motor proteins that move along microtubules, which are the heavy lifters of the cytoskeleton.

Research by Vale and others has shown that each cytoskeletal motor protein consists of a region called the motor domain, which catalyzes the breakdown of ATP and moves the protein along its track, and a tail domain that docks the motor onto a particular cargo in the cell.

In 1985, by observing the movement of organelles along microtubule filaments in the squid giant axon (nerve fiber), Vale discovered kinesin, the smallest known molecular motor. In 1996, in collaboration with Robert Fletterick’s UCSF lab, Vale and his colleagues determined the structure of the kinesin motor domain at atomic-resolution detail and discovered, quite unexpectedly, that it is similar to myosin, the actin-based, prototypical molecular motor.

More recently, Vale has shifted his attention to understanding the mechanisms by which motor proteins in the dynein family—the largest known molecular motors—power the beating of hairlike cilia and flagella, transport molecular cargoes and help form the mitotic spindle. As part of this effort, in 2011, he and colleagues obtained the crystal structure of the dynein motor domain, a major technical achievement.

Vale is a professor and vice-chair of the department of cellular and molecular pharmacology at UCSF, where he has been on the faculty since 1987. He is also a Howard Hughes Medical Institute investigator and holds an adjunct senior scientist appointment with the Marine Biological Laboratory in Woods Hole, Mass. Vale earned a B.A. in biology and chemistry from the University of California, Santa Barbara, in 1980 and a Ph.D. in neuroscience from Stanford University in 1985.

Among Vale’s many honors are the Wiley Prize in Biomedical Sciences and the Albert Lasker Basic Medical Research Award. He was elected to the National Academy of Sciences in 2001 and to the American Academy of Arts and Sciences in 2002.—Elia Ben-Ari


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