The Journal of Cell Biology, Vol 103, 1539-1545, Copyright © 1986 by The Rockefeller University Press

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A novel microtubule-associated protein from mammalian nerve shows ATP- sensitive binding to microtubules

PJ Hollenbeck and K Chapman

We report the isolation of a protein from mammalian nerve which shows ATP-sensitive binding to microtubules and ATPase activity. This protein, which we have designated HMW4, was prepared from bovine spinal nerve roots by microtubule affinity and ATP-induced release, and was further purified by sucrose density gradient centrifugation. It is a high molecular weight protein with a denatured Mr of 315,000, a Stokes radius of 90 A, and a sedimentation value of approximately 19S. It can be resolved electrophoretically from the well-characterized bovine brain microtubule-associated proteins (MAPs) and also appears to be distinct from MAP 1C. HMW4 has a vanadate-sensitive and azide- insensitive ATPase activity which averages 20 nmol Pi/min per mg protein and is different from dynein and myosin ATPases. HMW4 prepared on sucrose gradients exhibits binding to MAP-free microtubules in the absence of ATP which is reduced by ATP addition. Assayed by darkfield microscopy, HMW4 causes bundling of MAP-free microtubules which is reversed by ATP addition.
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This article has been cited by other articles:

• Lee, K.-D., Hollenbeck, P. J. (1995). Phosphorylation of Kinesin inVivo Correlates with Organelle Association and Neurite Outgrowth. J. Biol. Chem. 270: 5600-5605 [Abstract] [Full Text]  

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