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PDBsum entry 4yfg
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References listed in PDB file
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Key reference
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Title
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Mechanisms of splicing-Dependent trans-Synaptic adhesion by ptpδ-Il1rapl1/il-1racp for synaptic differentiation.
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Authors
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A.Yamagata,
T.Yoshida,
Y.Sato,
S.Goto-Ito,
T.Uemura,
A.Maeda,
T.Shiroshima,
S.Iwasawa-Okamoto,
H.Mori,
M.Mishina,
S.Fukai.
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Ref.
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Nat Commun, 2015,
6,
6926.
[DOI no: ]
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PubMed id
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Abstract
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Synapse formation is triggered through trans-synaptic interaction between pairs
of pre- and postsynaptic adhesion molecules, the specificity of which depends on
splice inserts known as 'splice-insert signaling codes'. Receptor protein
tyrosine phosphatase δ (PTPδ) can bidirectionally induce pre- and postsynaptic
differentiation of neurons by trans-synaptically binding to interleukin-1
receptor accessory protein (IL-1RAcP) and IL-1RAcP-like-1 (IL1RAPL1) in a
splicing-dependent manner. Here, we report crystal structures of PTPδ in
complex with IL1RAPL1 and IL-1RAcP. The first immunoglobulin-like (Ig) domain of
IL1RAPL1 directly recognizes the first splice insert, which is critical for
binding to IL1RAPL1. The second splice insert functions as an adjustable linker
that positions the Ig2 and Ig3 domains of PTPδ for simultaneously interacting
with the Ig1 domain of IL1RAPL1 or IL-1RAcP. We further identified the
IL1RAPL1-specific interaction, which appears coupled to the
first-splice-insert-mediated interaction. Our results thus reveal the decoding
mechanism of splice-insert signaling codes for synaptic differentiation induced
by trans-synaptic adhesion between PTPδ and IL1RAPL1/IL-1RAcP.
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