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Published 28 October 2002. doi:10.1083/jcb.200205062
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© The Rockefeller University Press, 0021-9525/2002/10/279 $5.00
The Journal of Cell Biology, Volume 159, Number 2, 279-290

Article

Myosin Va binding to neurofilaments is essential for correct myosin Va distribution and transport and neurofilament density



Mala V. Rao1,2, Linda J. Engle4, Panaiyur S. Mohan1,2, Aidong Yuan1,2, Dike Qiu1, Anne Cataldo1,5, Linda Hassinger5, Stephen Jacobsen1, Virginia M-Y. Lee6, Athena Andreadis7, Jean-Pierre Julien8, Paul C. Bridgman9 and Ralph A. Nixon1,2,3

1 Center for Dementia Research, Nathan Kline Institute, Orangeburg, NY 10962
2 Department of Psychiatry, New York University School of Medicine, New York, NY 10016
3 Department of Cell Biology, New York University School of Medicine, New York, NY 10016
4 Department of Neurobiology, Harvard Medical School, Boston, MA 02115
5 McLean Hospital, Belmont, MA 02178
6 Department of Pathology and Laboratory Medicine, University of Pennsylvania School of Medicine, Philadelphia, PA 19104
7 Department of Biomedical Sciences, E.K. Center for Mental Retardation, Waltham, Massachusetts 02254
8 McGill University, Montreal General Hospital, Research Institute, Center for Research in Neurosciences, Montreal, H3G 1A4, Canada
9 Department of Anatomy and Neurobiology, Washington University in St. Louis, St. Louis, MO 63110

Address correspondence to Ralph Nixon, Nathan Kline Institute, New York University School of Medicine, 140 Old Orangeburg Rd., Orangeburg, NY 10962. Tel.: (845) 398-5423. Fax: (845) 398-5422. E-mail: nixon{at}nki.rfmh.org

The identification of molecular motors that modulate the neuronal cytoskeleton has been elusive. Here, we show that a molecular motor protein, myosin Va, is present in high proportions in the cytoskeleton of mouse CNS and peripheral nerves. Immunoelectron microscopy, coimmunoprecipitation, and blot overlay analyses demonstrate that myosin Va in axons associates with neurofilaments, and that the NF-L subunit is its major ligand. A physiological association is indicated by observations that the level of myosin Va is reduced in axons of NF-L–null mice lacking neurofilaments and increased in mice overexpressing NF-L, but unchanged in NF-H–null mice. In vivo pulse-labeled myosin Va advances along axons at slow transport rates overlapping with those of neurofilament proteins and actin, both of which coimmunoprecipitate with myosin Va. Eliminating neurofilaments from mice selectively accelerates myosin Va translocation and redistributes myosin Va to the actin-rich subaxolemma and membranous organelles. Finally, peripheral axons of dilute-lethal mice, lacking functional myosin Va, display selectively increased neurofilament number and levels of neurofilament proteins without altering axon caliber. These results identify myosin Va as a neurofilament-associated protein, and show that this association is essential to establish the normal distribution, axonal transport, and content of myosin Va, and the proper numbers of neurofilaments in axons.

Key Words: myosin Va; dilute; neurofilaments; NF-associated proteins; axonal transport


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