Structural basis of SALM5-induced PTPδ dimerization for synaptic differentiation.

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Tytuł:: Structural basis of SALM5-induced PTPδ dimerization for synaptic differentiation.
Autorzy:: Lin Z; State Key Laboratory of Natural and Biomimetic Drugs & Department of Molecular and Cellular Pharmacology, School of Pharmaceutical Sciences, Peking University Health Science Center, 38 Xueyuan Road, Haidian District, Beijing, 100191, China.
Liu J; State Key Laboratory of Natural and Biomimetic Drugs & Department of Molecular and Cellular Pharmacology, School of Pharmaceutical Sciences, Peking University Health Science Center, 38 Xueyuan Road, Haidian District, Beijing, 100191, China.
Ding H; State Key Laboratory of Natural and Biomimetic Drugs & Department of Molecular and Cellular Pharmacology, School of Pharmaceutical Sciences, Peking University Health Science Center, 38 Xueyuan Road, Haidian District, Beijing, 100191, China.
Xu F; State Key Laboratory of Natural and Biomimetic Drugs & Department of Molecular and Cellular Pharmacology, School of Pharmaceutical Sciences, Peking University Health Science Center, 38 Xueyuan Road, Haidian District, Beijing, 100191, China.
Liu H; State Key Laboratory of Natural and Biomimetic Drugs & Department of Molecular and Cellular Pharmacology, School of Pharmaceutical Sciences, Peking University Health Science Center, 38 Xueyuan Road, Haidian District, Beijing, 100191, China. .
Źródło:: Nature communications [Nat Commun] 2018 Jan 18; Vol. 9 (1), pp. 268. Date of Electronic Publication: 2018 Jan 18.
Typ publikacji:: Journal Article; Research Support, Non-U.S. Gov't
Język:: English
Imprint Name(s):: Original Publication: [London] : Nature Pub. Group
MeSH Terms:: Cell Adhesion Molecules, Neuronal/*metabolism
Receptor-Like Protein Tyrosine Phosphatases, Class 2/*metabolism
Baculoviridae ; Dimerization ; HEK293 Cells ; Humans ; Immunoglobulin Domains ; Protein Structure, Quaternary
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Substance Nomenclature:: 0 (Cell Adhesion Molecules, Neuronal)
0 (LRFN5 protein, human)
EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases, Class 2)
Entry Date(s):: Date Created: 20180120 Date Completed: 20180215 Latest Revision: 20200930
Update Code:: 20240104
PubMed Central ID:: PMC5773555
DOI:: 10.1038/s41467-017-02414-2
PMID:: 29348579
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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.

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