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Comment
. 2000 Jan 24;148(2):219-21.
doi: 10.1083/jcb.148.2.219.

The tails of two myosins

L M Machesky  1
Affiliations
Comment

The tails of two myosins

L M Machesky. J Cell Biol. .
No abstract available

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Figures

Figure 1
Figure 1
Schematics of the sequences of Myo3p, Myo5p, WIP, verprolin, Bee1p/Las17p, and WASP. Molecules and sequence domains/motifs are drawn roughly to scale. Myo3p and Myo5p contain basic sequences (purple) that interact with negatively charged phospholipids, and SH3 domain (yellow) and an acidic tail sequence (green) which binds to the Arp2/3 complex. WIP and verprolin contain a WH2 (WASP homology 2 motif that binds to monomeric actin, red) and are mostly proline-rich (yellow). Bee1p/Las17p and WASP contain WH1 (WASP homology 1, white), proline-rich sequences (yellow), WH2 motifs (red) and acidic tail sequences that bind to Arp2/3 complex (green). WASP also contains a Cdc42-binding motif (blue) while Bee1p/Las17p does not.
Figure 2
Figure 2
Myosin I may transport Arp2/3 complex to sites of actin polymerization. (1 and 2) Arp2/3 complex (blue) dissociates from an older branchpoint, allowing cofilin (yellow circles) to accelerate the disassembly of older filaments. Cofilin binds to the sides of actin filaments (red lines) and to actin monomers (red circles). (3) Myosin I clusters could then bind to the free Arp2/3 complex via the myosin I acidic tail sequence. (4) Once attached to a filament, the myosin I cluster could transport Arp2/3 complex back to the plasma membrane. (5) When the myosin I cluster arrives at the leading edge of the cell, it could dock via its SH3 domains contacting WASP family protein polyproline sequences. This could provide activated Arp2/3 complex in zones of nucleation of new actin. Myosin I clusters could then hand the Arp2/3 complex over to a WASP family protein and dissociate, or remain bound in a large complex (see Discussion in Lechler et al. and Evangelista et al.). Although there are several potential binding sites on WASP family proteins and verprolin for myosin I, and myosin I must work in clusters to be processive, only one myosin I per Arp2/3 complex has been drawn here for simplicity.
See this image and copyright information in PMC

Comment on

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