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Cited by 65Axon Guidance and Neuronal SignalingProtein Structure and DynamicsReceptor Mechanisms and Signaling

Structure of the Repulsive Guidance Molecule (RGM)–Neogenin Signaling Hub

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Bell, Christian H., Healey, Eleanor, van Erp, Susan, Bishop, Benjamin, Tang, Chenxiang, Gilbert, Robert J.C., Aricescu, A. Radu, Pasterkamp, R. Jeroen +1 more·2013·Science
DOI 10.1126/science.1232322PMC PMC4730555
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Abstract

RGM Proteins: Members of the repulsive guidance molecule (RGM) family of proteins can be secreted or reside on the surface of cells where they bind to the cell surface receptor, neogenin. The RGM proteins are named for their role in axon guidance for developing neurons, but their function is also linked to a range of human diseases, including inflammation, multiple sclerosis, and cancer. Bell et al. (p. 77 ) solved the crystal structures of the external portions of the RGMB protein with portions of neogenin. The structures revealed interactions of dimers of RGMB with neogenin in which ligand binding induced conformational changes that may initiate intracellular signaling from the receptor. RGM proteins contain a site of autocatalytic cleavage that affects secretion of the proteins, and some disease-associated mutations in RGM proteins were clustered at this site.

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  • RGM proteins have high affinity for BMPs and can enhance BMP signaling in ways still incompletely understood but involving formation and internalization of a cell surface complex in which RGMb forms a bridge between BMP ligands and Neogenin (Neo).

    “RGM proteins have high affinity for BMPs and can enhance BMP signaling in ways still incompletely understood but involving formation and internalization of a cell surface complex in which RGMb forms a bridge between BMP ligands and Neogenin (Neo) (45, 46).”

    From Agouti and BMP signaling drive a naturally occurring fate conversion of melanophores to leucophores in zebrafish (2025) · cites this paper as [45]

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Authors
Bell, C. H., Healey, E., van Erp, S., Bishop, B., Tang, C., Gilbert, R. J. C., Aricescu, A. R., Pasterkamp, R. J., & Siebold, C.
Affiliations
  • Centre for Human Genetics (GB)
  • Department of Neuroscience and Pharmacology, Rudolf Magnus Institute of Neuroscience, University Medical Center Utrecht, CG Utrecht 3584, Netherlands.
  • University Medical Center Utrecht (NL)
Corresponding author
  • Healey, Eleanor
  • Siebold, Christian
ORCID
Venue
Science
Publisher
American Association for the Advancement of Science (AAAS)
Published
2013-07-05
Volume
341
Issue
6141
Pages
77-80
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
DOI
10.1126/science.1232322
PMC
PMC4730555
OpenAlex
W1966762483
Cited by
65
References
2
Citations by year
2026: 2 · 2025: 2 · 2024: 4 · 2023: 3 · 2022: 6 · 2021: 7 · 2020: 4 · 2019: 5 · 2018: 4 · 2017: 7 · 2016: 7 · 2015: 5 · 2014: 7 · 2013: 2
FWCI
3.43
Type
journal article
Language
en
Open access
Licence
cc-by
Locations
  • Science (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • Wellcome Trust (097301, 082301, 090532, 083111)
  • Cancer Research UK (A14414, 14414)
Topics
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Axon Guidance and Neuronal Signaling
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
Keywords
repulsive guidance molecules, neogenin, RGMb, dragons, crystal structure, receptor binding domain, protein fold, autocatalytic cleavage, juxtamembrane region, cell motility, cell adhesion, immune cell regulation, iron metabolism
MeSH terms
Amino Acid Sequence, Humans, Membrane Proteins, Mutation, Oligopeptides, Signal Transduction, Cell Adhesion Molecules, Neuronal, Conserved Sequence, Protein Structure, Tertiary, Crystallography, X-Ray, Biophysical Phenomena

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