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PDBsum entry 4yc7
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Signaling protein
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PDB id
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4yc7
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References listed in PDB file
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Key reference
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Title
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The structure of fmnl2-Cdc42 yields insights into the mechanism of lamellipodia and filopodia formation.
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Authors
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S.Kühn,
C.Erdmann,
F.Kage,
J.Block,
L.Schwenkmezger,
A.Steffen,
K.Rottner,
M.Geyer.
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Ref.
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Nat Commun, 2015,
6,
7088.
[DOI no: ]
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PubMed id
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Abstract
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Formins are actin polymerization factors that elongate unbranched actin
filaments at the barbed end. Rho family GTPases activate Diaphanous-related
formins through the relief of an autoregulatory interaction. The crystal
structures of the N-terminal domains of human FMNL1 and FMNL2 in complex with
active Cdc42 show that Cdc42 mediates contacts with all five armadillo repeats
of the formin with specific interactions formed by the Rho-GTPase insert helix.
Mutation of three residues within Rac1 results in a gain-of-function mutation
for FMNL2 binding and reconstitution of the Cdc42 phenotype in vivo.
Dimerization of FMNL1 through a parallel coiled coil segment leads to formation
of an umbrella-shaped structure that-together with Cdc42-spans more than 15 nm
in diameter. The two interacting FMNL-Cdc42 heterodimers expose six membrane
interaction motifs on a convex protein surface, the assembly of which may
facilitate actin filament elongation at the leading edge of lamellipodia and
filopodia.
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