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PDBsum entry 4v2d
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Signaling protein
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PDB id
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4v2d
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References listed in PDB file
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Key reference
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Title
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Flrt structure: balancing repulsion and cell adhesion in cortical and vascular development.
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Authors
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E.Seiradake,
D.Del toro,
D.Nagel,
F.Cop,
R.Härtl,
T.Ruff,
G.Seyit-Bremer,
K.Harlos,
E.C.Border,
A.Acker-Palmer,
E.Y.Jones,
R.Klein.
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Ref.
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Neuron, 2014,
84,
370-385.
[DOI no: ]
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PubMed id
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Abstract
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FLRTs are broadly expressed proteins with the unique property of acting as
homophilic cell adhesion molecules and as heterophilic repulsive ligands of
Unc5/Netrin receptors. How these functions direct cell behavior and the
molecular mechanisms involved remain largely unclear. Here we use X-ray
crystallography to reveal the distinct structural bases for FLRT-mediated cell
adhesion and repulsion in neurons. We apply this knowledge to elucidate FLRT
functions during cortical development. We show that FLRTs regulate both the
radial migration of pyramidal neurons, as well as their tangential spread.
Mechanistically, radial migration is controlled by repulsive FLRT2-Unc5D
interactions, while spatial organization in the tangential axis involves
adhesive FLRT-FLRT interactions. Further, we show that the fundamental
mechanisms of FLRT adhesion and repulsion are conserved between neurons and
vascular endothelial cells. Our results reveal FLRTs as powerful guidance
factors with structurally encoded repulsive and adhesive surfaces.
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