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Walking proteins need to rock and roll, new study finds

The inside of a living cell has been compared to a train station at rush hour, with enzymes, chromosomes and other internal components constantly being shuttled along tiny fibrous tracks called microtubules.

Unlike a congested city commute, cellular traffic is efficient and highly regulated - thanks in part to a group of proteins known as motor molecules that use microtubules to haul vital cargo through the cell.

In 1985, biologists identified a molecular motor called kinesin that has turned out to be responsible for a variety of critical hauling jobs, such as separating chromosomes during cell division and ferrying neurotransmitters inside nerve cells.

Studies have shown that while one end of a kinesin molecule holds onto its cargo, the other end uses a remarkable two-headed structure to grab the microtubule and pull the cargo forward - a process called "kinesin walking" (see web animations at http://www.scripps.edu/milligan/projects and http://mc11.mcri.ac.uk/wrongtrousers.html).

Researchers are interested in unraveling the mystery of how kinesins walk along microtubules, and whether defective walking contributes to a variety of human ailments - including spontaneous abortion, tumor growth, infertility and neurodegenerative diseases such as Alzheimer's and retinitis pigmentosa.

A study featured on the cover of the June issue of the journal Nature Structural Biology adds an important piece to the puzzle.

"There is a lot of interest in kinesin and how it works as a motor," says Stanford chemistry Professor W. E. Moerner, co-author of the June study. "Measurements have been made of the forces kinesin produces as it walks, but we'd like to know how it is oriented when it moves as well."

HEAD OVER HEAD

Kinesin walking is controlled by the breakdown of ATP - a molecule that pr
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Contact: Mark Shwartz
mshwartz@stanford.edu
650-723-9296
Stanford University
27-Jun-2001


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