A
correction
to this article has been published: Powell, J. Cell Biol. 177 (5) 941
Published online
doi:10.1083/jcb.1774iti5
The Journal of Cell Biology, Vol. 177, No. 4, 567b-
The Rockefeller University Press, 0021-9525 $30.00
© Powell
Motoring microvillar membrane
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Brush border apical membrane (red) accumulates at the tips of actin bundles (green) upon addition of ATP (right) and myosin-1a activation.
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Just as intestines constantly shed gut cells, so too may gut cells shed their brush border membranes. On page 671, McConnell and Tyska show that microvillar myosin-1a pulls membrane for shedding along the core actin bundle.
Myosin-1a was first seen in micrographs 30 years ago bridging the actin bundle and the overlying membrane in microvilli. But it was not until 1989 that myosin-1a was characterized as an actin plus enddirected motor. Its potential as an active motor in the microvillus, rather than mere structural element, was overlooked until now.
A motor is useful in isolated brush borders, which dramatically shear off their membranes from the base to the tip of the microvillar stalks when fed ATP. McConnell and Tyska find that this actin plus enddirected shearing results in vesicles' being shed from the microvilli tips. The ATP activated shedding by turning on myosin-1a: brush borders from myosin-1a knock-out mice shed membrane at only five percent of the wild-type level.
How myosin-1a gains traction on the membrane surface is an open question. But the discovery promotes the brush border from merely a static scaffold of boosted surface area for nutrient breakdown to an active zone for shedding vesiclestiny packets that may speed nutrient breakdown, shed invading microbes, send messages, and improve membrane remodeling.
Kendall Powell
kendall2{at}nasw.org

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Myosin-1a powers the sliding of apical membrane along microvillar actin bundles
- Russell E. McConnell and Matthew J. Tyska
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