The Diaphanous-related formin dDia2 is required for the formation and maintenance of filopodia. (Q46503087)

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12 January 2020

title

The Diaphanous-related formin dDia2 is required for the formation and maintenance of filopodia (English)

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12 January 2020

2

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12 January 2020

author name string

Antje Schirenbeck

1

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12 January 2020

Rajesh Arasada

3

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12 January 2020

Michael Schleicher

4

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12 January 2020

Jan Faix

5

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12 January 2020

publication date

22 May 2005

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12 January 2020

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12 January 2020

volume

7

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12 January 2020

page(s)

619-625

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12 January 2020

issue

6

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https://scigraph.springernature.com/pub.10.1038/ncb1266

12 January 2020

exact match

0 references

cites work

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Formin-induced nucleation of actin filaments

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

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

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

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p140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for 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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Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast

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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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The Rho family GTPase Rif induces filopodia through mDia2.

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Membrane tether formation from blebbing cells

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Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis

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Critical role of Ena/VASP proteins for filopodia formation in neurons and in function downstream of netrin-1.

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21 January 2018

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Formin binding proteins bear WWP/WW domains that bind proline-rich peptides and functionally resemble SH3 domains

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inferred from DOI database lookup

7 January 2021

based on heuristic

An actin nucleation mechanism mediated by Bni1 and profilin

1 reference

inferred from DOI database lookup

7 January 2021

based on heuristic

Characterization of actin- and lipid-binding domains in severin, a Ca(2+)-dependent F-actin fragmenting protein

1 reference