PlantImRecepV1, Main, Exploration, bibRecord, 000062

Repulsive guidance molecules lock growth differentiation factor 5 in an inhibitory complex.

Identifieur interne : 000062 ( Main/Exploration ); précédent : 000061; suivant : 000063

Repulsive guidance molecules lock growth differentiation factor 5 in an inhibitory complex.

Auteurs : Tomas Malinauskas [Royaume-Uni] ; Tina V. Peer [Allemagne] ; Benjamin Bishop [Royaume-Uni] ; Thomas D. Mueller [Royaume-Uni] ; Christian Siebold [Royaume-Uni]

Source :

Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2020.

RBID : pubmed:32576689

Descripteurs français

English descriptors

Abstract

Repulsive guidance molecules (RGMs) are cell surface proteins that regulate the development and homeostasis of many tissues and organs, including the nervous, skeletal, and immune systems. They control fundamental biological processes, such as migration and differentiation by direct interaction with the Neogenin (NEO1) receptor and function as coreceptors for the bone morphogenetic protein (BMP)/growth differentiation factor (GDF) family. We determined crystal structures of all three human RGM family members in complex with GDF5, as well as the ternary NEO1-RGMB-GDF5 assembly. Surprisingly, we show that all three RGMs inhibit GDF5 signaling, which is in stark contrast to RGM-mediated enhancement of signaling observed for other BMPs, like BMP2. Despite their opposite effect on GDF5 signaling, RGMs occupy the BMP type 1 receptor binding site similar to the observed interactions in RGM-BMP2 complexes. In the NEO1-RGMB-GDF5 complex, RGMB physically bridges NEO1 and GDF5, suggesting cross-talk between the GDF5 and NEO1 signaling pathways. Our crystal structures, combined with structure-guided mutagenesis of RGMs and BMP ligands, binding studies, and cellular assays suggest that RGMs inhibit GDF5 signaling by competing with GDF5 type 1 receptors. While our crystal structure analysis and in vitro binding data initially pointed towards a simple competition mechanism between RGMs and type 1 receptors as a possible basis for RGM-mediated GDF5 inhibition, further experiments utilizing BMP2-mimicking GDF5 variants clearly indicate a more complex mechanism that explains how RGMs can act as a functionality-changing switch for two structurally and biochemically similar signaling molecules.

DOI: 10.1073/pnas.2000561117
PubMed: 32576689
PubMed Central: PMC7354924

Affiliations:

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<term>Cell Adhesion Molecules, Neuronal (ultrastructure)</term>
<term>Crystallography, X-Ray (MeSH)</term>
<term>GPI-Linked Proteins (metabolism)</term>
<term>GPI-Linked Proteins (ultrastructure)</term>
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<term>Growth Differentiation Factor 5 (ultrastructure)</term>
<term>Hemochromatosis Protein (metabolism)</term>
<term>Hemochromatosis Protein (ultrastructure)</term>
<term>Membrane Proteins (metabolism)</term>
<term>Membrane Proteins (ultrastructure)</term>
<term>Nerve Tissue Proteins (metabolism)</term>
<term>Nerve Tissue Proteins (ultrastructure)</term>
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<term>Recombinant Proteins (metabolism)</term>
<term>Recombinant Proteins (ultrastructure)</term>
<term>Signal Transduction (MeSH)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Cristallographie aux rayons X (MeSH)</term>
<term>Domaines protéiques (MeSH)</term>
<term>Facteur-5 de croissance et de différenciation (métabolisme)</term>
<term>Facteur-5 de croissance et de différenciation (ultrastructure)</term>
<term>Molécules d'adhérence cellulaire neuronale (métabolisme)</term>
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<term>Protéine de l'hémochromatose (ultrastructure)</term>
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<term>Protéine morphogénétique osseuse de type 2 (ultrastructure)</term>
<term>Protéines de tissu nerveux (métabolisme)</term>
<term>Protéines de tissu nerveux (ultrastructure)</term>
<term>Protéines liées au GPI (métabolisme)</term>
<term>Protéines liées au GPI (ultrastructure)</term>
<term>Protéines membranaires (métabolisme)</term>
<term>Protéines membranaires (ultrastructure)</term>
<term>Protéines recombinantes (métabolisme)</term>
<term>Protéines recombinantes (ultrastructure)</term>
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<term>Growth Differentiation Factor 5</term>
<term>Hemochromatosis Protein</term>
<term>Membrane Proteins</term>
<term>Nerve Tissue Proteins</term>
<term>Recombinant Proteins</term>
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<term>Growth Differentiation Factor 5</term>
<term>Hemochromatosis Protein</term>
<term>Membrane Proteins</term>
<term>Nerve Tissue Proteins</term>
<term>Recombinant Proteins</term>
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<term>Molécules d'adhérence cellulaire neuronale</term>
<term>Protéine de l'hémochromatose</term>
<term>Protéine morphogénétique osseuse de type 2</term>
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<term>Protéines recombinantes</term>
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<front><div type="abstract" xml:lang="en">Repulsive guidance molecules (RGMs) are cell surface proteins that regulate the development and homeostasis of many tissues and organs, including the nervous, skeletal, and immune systems. They control fundamental biological processes, such as migration and differentiation by direct interaction with the Neogenin (NEO1) receptor and function as coreceptors for the bone morphogenetic protein (BMP)/growth differentiation factor (GDF) family. We determined crystal structures of all three human RGM family members in complex with GDF5, as well as the ternary NEO1-RGMB-GDF5 assembly. Surprisingly, we show that all three RGMs inhibit GDF5 signaling, which is in stark contrast to RGM-mediated enhancement of signaling observed for other BMPs, like BMP2. Despite their opposite effect on GDF5 signaling, RGMs occupy the BMP type 1 receptor binding site similar to the observed interactions in RGM-BMP2 complexes. In the NEO1-RGMB-GDF5 complex, RGMB physically bridges NEO1 and GDF5, suggesting cross-talk between the GDF5 and NEO1 signaling pathways. Our crystal structures, combined with structure-guided mutagenesis of RGMs and BMP ligands, binding studies, and cellular assays suggest that RGMs inhibit GDF5 signaling by competing with GDF5 type 1 receptors. While our crystal structure analysis and in vitro binding data initially pointed towards a simple competition mechanism between RGMs and type 1 receptors as a possible basis for RGM-mediated GDF5 inhibition, further experiments utilizing BMP2-mimicking GDF5 variants clearly indicate a more complex mechanism that explains how RGMs can act as a functionality-changing switch for two structurally and biochemically similar signaling molecules.</div>
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<ArticleTitle>Repulsive guidance molecules lock growth differentiation factor 5 in an inhibitory complex.</ArticleTitle>
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<Abstract><AbstractText>Repulsive guidance molecules (RGMs) are cell surface proteins that regulate the development and homeostasis of many tissues and organs, including the nervous, skeletal, and immune systems. They control fundamental biological processes, such as migration and differentiation by direct interaction with the Neogenin (NEO1) receptor and function as coreceptors for the bone morphogenetic protein (BMP)/growth differentiation factor (GDF) family. We determined crystal structures of all three human RGM family members in complex with GDF5, as well as the ternary NEO1-RGMB-GDF5 assembly. Surprisingly, we show that all three RGMs inhibit GDF5 signaling, which is in stark contrast to RGM-mediated enhancement of signaling observed for other BMPs, like BMP2. Despite their opposite effect on GDF5 signaling, RGMs occupy the BMP type 1 receptor binding site similar to the observed interactions in RGM-BMP2 complexes. In the NEO1-RGMB-GDF5 complex, RGMB physically bridges NEO1 and GDF5, suggesting cross-talk between the GDF5 and NEO1 signaling pathways. Our crystal structures, combined with structure-guided mutagenesis of RGMs and BMP ligands, binding studies, and cellular assays suggest that RGMs inhibit GDF5 signaling by competing with GDF5 type 1 receptors. While our crystal structure analysis and in vitro binding data initially pointed towards a simple competition mechanism between RGMs and type 1 receptors as a possible basis for RGM-mediated GDF5 inhibition, further experiments utilizing BMP2-mimicking GDF5 variants clearly indicate a more complex mechanism that explains how RGMs can act as a functionality-changing switch for two structurally and biochemically similar signaling molecules.</AbstractText>
<CopyrightInformation>Copyright © 2020 the Author(s). Published by PNAS.</CopyrightInformation>
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	Serveur d'exploration sur les récepteurs immunitaires végétaux
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Serveur d'exploration sur les récepteurs immunitaires végétaux

Repulsive guidance molecules lock growth differentiation factor 5 in an inhibitory complex.

Repulsive guidance molecules lock growth differentiation factor 5 in an inhibitory complex.

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