Two papers in this issue of The Journal of Cell Biology uncover a possible new connection between the actin-nucleating complex of proteins, the Arp2/3 complex, and the type I myosin motors. In this issue, Lechler et al. 2000 and Evangelista et al. 2000 show a direct interaction of the S. cerevisiae myosin I motors (Myo3p and Myo5p) with the Arp2/3 complex through an acidic COOH-terminal sequence motif. The data suggest that a large complex containing both myosin motors and actin nucleating proteins may be a functional unit for signal-induced actin assembly. Furthermore, both studies provide evidence that myosin I function is essential for assembly and maintenance of filamentous actin structures in cells. This is exciting and raises some controversy, given the recent discovery that intracellular pathogens such as Shigella flexnerii and Listeria monocytogenes do not use myosin motors...
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24 January 2000
Review|
January 24 2000
The Tails of Two Myosins
Laura M. Machesky
Laura M. Machesky
aSchool of Biosciences, Division of Molecular and Cell Biology, University of Birmingham, Birmingham B15 2TT United Kingdom
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Laura M. Machesky
aSchool of Biosciences, Division of Molecular and Cell Biology, University of Birmingham, Birmingham B15 2TT United Kingdom
Received:
December 29 1999
Accepted:
January 03 2000
Online ISSN: 1540-8140
Print ISSN: 0021-9525
© 2000 The Rockefeller University Press
2000
The Rockefeller University Press
J Cell Biol (2000) 148 (2): 219–222.
Article history
Received:
December 29 1999
Accepted:
January 03 2000
Citation
Laura M. Machesky; The Tails of Two Myosins. J Cell Biol 24 January 2000; 148 (2): 219–222. doi: https://doi.org/10.1083/jcb.148.2.219
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