(Q28248978)

6

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author name string

Judith E Gasteier

1

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Sebastian Schroeder

2

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Walter Muranyi

3

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Ricardo Madrid

Experimental Cell Research

4

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language of work or name

English

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publication date

15 May 2005

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published in

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volume

306

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page(s)

192-202

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issue

1

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cites work

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Formins: signaling effectors for assembly and polarization of actin filaments

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Formin family proteins in cytoskeletal control

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Crystal structures of a Formin Homology-2 domain reveal a tethered dimer architecture

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The core FH2 domain of diaphanous-related formins is an elongated actin binding protein that inhibits polymerization

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FH3, a domain found in formins, targets the fission yeast formin Fus1 to the projection tip during conjugation

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Identification of a carboxyl-terminal diaphanous-related formin homology protein autoregulatory domain

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Signal-regulated activation of serum response factor is mediated by changes in actin dynamics

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Role of formins in actin assembly: nucleation and barbed-end association

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A conserved mechanism for Bni1- and mDia1-induced actin assembly and dual regulation of Bni1 by Bud6 and profilin

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The fission yeast cytokinesis formin Cdc12p is a barbed end actin filament capping protein gated by profilin

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Mammalian formin-1 participates in adherens junctions and polymerization of linear actin cables

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Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast

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The mouse Formin mDia1 is a potent actin nucleation factor regulated by autoinhibition

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Actin dynamics control SRF activity by regulation of its coactivator MAL

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Bni1p, a yeast formin linking cdc42p and the actin cytoskeleton during polarized morphogenesis

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RhoD regulates endosome dynamics through Diaphanous-related Formin and Src tyrosine kinase

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Disruption of the Diaphanous-related formin Drf1 gene encoding mDia1 reveals a role for Drf3 as an effector for Cdc42

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FRL, a novel formin-related protein, binds to Rac and regulates cell motility and survival of macrophages

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Identification and characterization of a protein containing formin homology (FH1/FH2) domains

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Roles of the fission yeast formin for3p in cell polarity, actin cable formation and symmetric cell division

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The small GTPase Rho3 and the diaphanous/formin For3 function in polarized cell growth in fission yeast

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Bni1p and Bnr1p: downstream targets of the Rho family small G-proteins which interact with profilin and regulate actin cytoskeleton in Saccharomyces cerevisiae

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mDia mediates Rho-regulated formation and orientation of stable microtubules

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Coordination of microtubules and the actin cytoskeleton by the Rho effector mDia1.

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Activation of the Rac-binding partner FHOD1 induces actin stress fibers via a ROCK-dependent mechanism

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The formin/diaphanous-related protein, FHOS, interacts with Rac1 and activates transcription from the serum response element

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Rho proteins: linking signaling with membrane trafficking

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Rho and Rac take center stage

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The formin-homology-domain-containing protein FHOD1 enhances cell migration

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Fhos, a mammalian formin, directly binds to F-actin via a region N-terminal to the FH1 domain and forms a homotypic complex via the FH2 domain to promote actin fiber formation

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Activation of SRF-regulated chromosomal templates by Rho-family GTPases requires a signal that also induces H4 hyperacetylation

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Cytokinesis: rho and formins are the ringleaders

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ROCK and mDia1 antagonize in Rho-dependent Rac activation in Swiss 3T3 fibroblasts

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Actin and microtubules in cell motility: which one is in control?

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Conserved microtubule-actin interactions in cell movement and morphogenesis

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