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Research Article |
Department of Cell and Molecular Physiology, Medical Science Research Building, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA
* Author for correspondence (e-mail: cheneyr{at}med.unc.edu )
Accepted 3 December 2001
Class V myosins are one of the most ancient and widely distributed groups
of the myosin superfamily and are hypothesized to function as motors for
actin-dependent organelle transport. We report the discovery and initial
characterization of a novel member of this family, human myosin-Vc (Myo5c).
The Myo5c protein sequence shares 
50% overall identity with the two other
class V myosins in vertebrates, myosin-Va (Myo5a) and myosin-Vb (Myo5b).
Systematic analysis of the mRNA and protein distribution of these myosins
indicates that Myo5a is most abundant in brain, whereas Myo5b and Myo5c are
expressed chiefly in non-neuronal tissues. Myo5c is particularly abundant in
epithelial and glandular tissues including pancreas, prostate, mammary,
stomach, colon and lung. Immunolocalization in colon and exocrine pancreas
indicates that Myo5c is expressed chiefly in epithelial cells. A dominant
negative approach using a GFP-Myo5c tail construct in HeLa cells reveals that
the Myo5c tail selectively colocalizes with and perturbs a membrane
compartment containing the transferrin receptor and rab8. Transferrin also
accumulates in this compartment, suggesting that Myo5c is involved in
transferrin trafficking. As a class V myosin of epithelial cells, Myo5c is
likely to power actin-based membrane trafficking in many physiologically
crucial tissues of the human body.
Key words: Myosin-V, Organelle transport, Membrane trafficking, Transferrin receptor, rab8
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