Type I myosins are highly conserved actin-based molecular motors that localize to the actin-rich cortex and participate in motility functions such as endocytosis, polarized morphogenesis, and cell migration. The COOH-terminal tail of yeast myosin-I proteins, Myo3p and Myo5p, contains an Src homology domain 3 (SH3) followed by an acidic domain. The myosin-I SH3 domain interacted with both Bee1p and Vrp1p, yeast homologues of human WASP and WIP, adapter proteins that link actin assembly and signaling molecules. The myosin-I acidic domain interacted with Arp2/3 complex subunits, Arc40p and Arc19p, and showed both sequence similarity and genetic redundancy with the COOH-terminal acidic domain of Bee1p (Las17p), which controls Arp2/3-mediated actin nucleation. These findings suggest that myosin-I proteins may participate in a diverse set of motility functions through a role in actin assembly.
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24 January 2000
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January 24 2000
A Role for Myosin-I in Actin Assembly through Interactions with Vrp1p, Bee1p, and the Arp2/3 Complex
Marie Evangelista,
Marie Evangelista
aDepartment of Biology, Queen's University, Kingston, Ontario, K7L 3N6, Canada
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Bert M. Klebl,
Bert M. Klebl
bGenetics Division, Institut de Recherche en Biotechnologie, 6100, Avenue Royalmount, Montreal, Quebec, H4P 2R2, Canada
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Amy H.Y. Tong,
Amy H.Y. Tong
aDepartment of Biology, Queen's University, Kingston, Ontario, K7L 3N6, Canada
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Bradley A. Webb,
Bradley A. Webb
aDepartment of Biology, Queen's University, Kingston, Ontario, K7L 3N6, Canada
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Thomas Leeuw,
Thomas Leeuw
bGenetics Division, Institut de Recherche en Biotechnologie, 6100, Avenue Royalmount, Montreal, Quebec, H4P 2R2, Canada
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Ekkehard Leberer,
Ekkehard Leberer
bGenetics Division, Institut de Recherche en Biotechnologie, 6100, Avenue Royalmount, Montreal, Quebec, H4P 2R2, Canada
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Malcolm Whiteway,
Malcolm Whiteway
bGenetics Division, Institut de Recherche en Biotechnologie, 6100, Avenue Royalmount, Montreal, Quebec, H4P 2R2, Canada
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David Y. Thomas,
David Y. Thomas
bGenetics Division, Institut de Recherche en Biotechnologie, 6100, Avenue Royalmount, Montreal, Quebec, H4P 2R2, Canada
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Charles Boone
Charles Boone
aDepartment of Biology, Queen's University, Kingston, Ontario, K7L 3N6, Canada
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Marie Evangelista
aDepartment of Biology, Queen's University, Kingston, Ontario, K7L 3N6, Canada
Bert M. Klebl
bGenetics Division, Institut de Recherche en Biotechnologie, 6100, Avenue Royalmount, Montreal, Quebec, H4P 2R2, Canada
Amy H.Y. Tong
aDepartment of Biology, Queen's University, Kingston, Ontario, K7L 3N6, Canada
Bradley A. Webb
aDepartment of Biology, Queen's University, Kingston, Ontario, K7L 3N6, Canada
Thomas Leeuw
bGenetics Division, Institut de Recherche en Biotechnologie, 6100, Avenue Royalmount, Montreal, Quebec, H4P 2R2, Canada
Ekkehard Leberer
bGenetics Division, Institut de Recherche en Biotechnologie, 6100, Avenue Royalmount, Montreal, Quebec, H4P 2R2, Canada
Malcolm Whiteway
bGenetics Division, Institut de Recherche en Biotechnologie, 6100, Avenue Royalmount, Montreal, Quebec, H4P 2R2, Canada
David Y. Thomas
bGenetics Division, Institut de Recherche en Biotechnologie, 6100, Avenue Royalmount, Montreal, Quebec, H4P 2R2, Canada
Charles Boone
aDepartment of Biology, Queen's University, Kingston, Ontario, K7L 3N6, Canada
Abbreviations used in this paper: AD, acidic domain; DIC, differential interference contrast; GFP, green fluorescent protein; GST, glutathione-S-transferase; HA, hemagglutinin; MBP, maltose binding protein; SH3, Src homology domain 3; WH2, WASP homology domain 2.
Received:
October 20 1999
Revision Requested:
December 10 1999
Accepted:
December 13 1999
Online ISSN: 1540-8140
Print ISSN: 0021-9525
© 2000 The Rockefeller University Press
2000
The Rockefeller University Press
J Cell Biol (2000) 148 (2): 353–362.
Article history
Received:
October 20 1999
Revision Requested:
December 10 1999
Accepted:
December 13 1999
Connected Content
Citation
Marie Evangelista, Bert M. Klebl, Amy H.Y. Tong, Bradley A. Webb, Thomas Leeuw, Ekkehard Leberer, Malcolm Whiteway, David Y. Thomas, Charles Boone; A Role for Myosin-I in Actin Assembly through Interactions with Vrp1p, Bee1p, and the Arp2/3 Complex. J Cell Biol 24 January 2000; 148 (2): 353–362. doi: https://doi.org/10.1083/jcb.148.2.353
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