Abstract
mDia1, a Rho effector, belongs to the Formin family of proteins, which shares the conserved tandem FH1-FH2 unit structure. Formins including mDia1 accelerate actin nucleation while interacting with actin filament fast-growing ends. Here our single-molecule imaging revealed fast directional movement of mDia1 FH1-FH2 for tens of microns in living cells. The movement of mDia1 FH1-FH2 was blocked by actin-perturbing drugs, and the speed of mDia1 FH1-FH2 movement appeared to correlate with actin elongation rates. In vitro, mDia1 FH1-FH2 associated persistently with the growing actin barbed end. mDia1 probably moves processively along the growing end of actin filaments in cells, and Formins may be a molecular motility machinery that is independent from motor proteins.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Actin Cytoskeleton / drug effects
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Actin Cytoskeleton / physiology*
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Actin Cytoskeleton / ultrastructure
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Actins / metabolism*
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Animals
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Biopolymers
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Bridged Bicyclo Compounds, Heterocyclic / metabolism
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Bridged Bicyclo Compounds, Heterocyclic / pharmacology
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Carrier Proteins / chemistry
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Carrier Proteins / metabolism
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Carrier Proteins / physiology*
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Cytochalasin D / metabolism
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Cytochalasin D / pharmacology
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Depsipeptides*
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Formins
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Mice
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Microtubules / drug effects
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Microtubules / physiology
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Movement
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Mutation
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Myosins / physiology
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Peptides, Cyclic / pharmacology
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / metabolism
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Thiazoles / metabolism
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Thiazoles / pharmacology
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Thiazolidines
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Xenopus
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rhoA GTP-Binding Protein / metabolism
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rhoA GTP-Binding Protein / pharmacology
Substances
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Actins
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Biopolymers
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Bridged Bicyclo Compounds, Heterocyclic
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Carrier Proteins
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Depsipeptides
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Diap1 protein, mouse
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Formins
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Peptides, Cyclic
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Recombinant Fusion Proteins
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Thiazoles
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Thiazolidines
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jasplakinolide
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Cytochalasin D
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Myosins
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rhoA GTP-Binding Protein
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latrunculin B