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- W2783190507 abstract "Abstract SALM5, a synaptic adhesion molecule implicated in autism, induces presynaptic differentiation through binding to the LAR family receptor protein tyrosine phosphatases (LAR-RPTPs) that have been highlighted as presynaptic hubs for synapse formation. The mechanisms underlying SALM5/LAR-RPTP interaction remain unsolved. Here we report crystal structures of human SALM5 LRR-Ig alone and in complex with human PTPδ Ig1–3 (MeA − ). Distinct from other LAR-RPTP ligands, SALM5 mainly exists as a dimer with LRR domains from two protomers packed in an antiparallel fashion. In the 2:2 heterotetrameric SALM5/PTPδ complex, a SALM5 dimer bridges two separate PTPδ molecules. Structure-guided mutations and heterologous synapse formation assays demonstrate that dimerization of SALM5 is prerequisite for its functionality in inducing synaptic differentiation. This study presents a structural template for the SALM family and reveals a mechanism for how a synaptic adhesion molecule directly induces cis -dimerization of LAR-RPTPs into higher-order signaling assembly." @default.
- W2783190507 created "2018-01-26" @default.
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- W2783190507 date "2018-01-18" @default.
- W2783190507 modified "2023-10-13" @default.
- W2783190507 title "Structural basis of SALM5-induced PTPδ dimerization for synaptic differentiation" @default.
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- W2783190507 doi "https://doi.org/10.1038/s41467-017-02414-2" @default.
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