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PDBsum entry 4mt6
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Protein binding
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PDB id
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4mt6
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References listed in PDB file
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Key reference
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Title
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A conformational switch in collybistin determines the differentiation of inhibitory postsynapses.
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Authors
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T.Soykan,
D.Schneeberger,
G.Tria,
C.Buechner,
N.Bader,
D.Svergun,
I.Tessmer,
A.Poulopoulos,
T.Papadopoulos,
F.Varoqueaux,
H.Schindelin,
N.Brose.
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Ref.
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Embo J, 2014,
33,
2113-2133.
[DOI no: ]
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PubMed id
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Abstract
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The formation of neuronal synapses and the dynamic regulation of their efficacy
depend on the assembly of the postsynaptic neurotransmitter receptor apparatus.
Receptor recruitment to inhibitory GABAergic and glycinergic synapses is
controlled by the scaffold protein gephyrin and the adaptor protein collybistin.
We derived new insights into the structure of collybistin and used these to
design biochemical, cell biological, and genetic analyses of collybistin
function. Our data define a collybistin-based protein interaction network that
controls the gephyrin content of inhibitory postsynapses. Within this network,
collybistin can adopt open/active and closed/inactive conformations to act as a
switchable adaptor that links gephyrin to plasma membrane phosphoinositides.
This function of collybistin is regulated by binding of the adhesion protein
neuroligin-2, which stabilizes the open/active conformation of collybistin at
the postsynaptic plasma membrane by competing with an intramolecular interaction
in collybistin that favors the closed/inactive conformation. By linking
trans-synaptic neuroligin-dependent adhesion and phosphoinositide signaling with
gephyrin recruitment, the collybistin-based regulatory switch mechanism
represents an integrating regulatory node in the formation and function of
inhibitory postsynapses.
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