Phosphorylation of DCC by ERK2 Is Facilitated by Direct Docking of the Receptor P1 Domain to the Kinase
Open accessAbstract
Netrin receptor DCC plays critical roles in many cellular processes, including axonal outgrowth and migration, angiogenesis, and apoptosis, but the molecular basis of DCC-mediated signaling is largely unclear. ERK2, a member of the MAPK family, is one of the few proteins known to be involved in DCC-mediated signaling. Here, we report that ERK2 directly interacts with DCC, and the ERK2-binding region was mapped to the conserved intracellular P1 domain of the receptor. The structure of ERK2 in complex with the P1 domain of DCC reveals that DCC contains a MAPK docking motif. The docking of the P1 domain onto ERK2 physically positions several phosphorylation sites of DCC in the vicinity of the kinase active site. We further show that the docking interaction between the P1 domain and ERK2 is essential for the ERK2-mediated phosphorylation of DCC. We conclude that DCC signaling is directly coupled with MAPK signaling cascades.
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MAPK docking is a well-characterized protein-peptide interaction system.
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- Authors
- Ma, W., Shang, Y., Wei, Z., Wen, W., Wang, W., & Zhang, M.
- Affiliations
- Fudan University (CN)
- Hong Kong University of Science and Technology (HK)
- Corresponding author
- Wang, Wenning
- Zhang, Mingjie
- Venue
- Structure
- Publisher
- Elsevier BV
- Published
- 2010-11
- Volume
- 18
- Issue
- 11
- Pages
- 1502-1511
- ISSN
- 0969-2126 (ISSN-L)
- OpenAlex
- W1964973231
- Cited by
- 31
- References
- 46
- Citations by year
- 2026: 2 · 2023: 2 · 2022: 1 · 2019: 1 · 2018: 1 · 2017: 1 · 2016: 4 · 2015: 4 · 2014: 1 · 2013: 6 · 2012: 3
- FWCI
- 1.81
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 989 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Structure (publishedVersion)
- PubMed (publishedVersion)
- Rare & Special e-Zone (The Hong Kong University of Science and Technology) (submittedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Axon Guidance and Neuronal Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Melanoma and MAPK Pathways
- Keywords
- DCC receptor, ERK2, receptor phosphorylation, protein-protein interaction, axon growth, netrin signaling, MAPK signaling, protein complex structure
- MeSH terms
- DCC Receptor, Animals, Crystallography, Fluorescence Polarization, Models, Molecular, Phosphorylation, Protein Binding, Receptors, Cell Surface, Mass Spectrometry, Signal Transduction, Protein Structure, Tertiary, Mitogen-Activated Protein Kinase 1, Tumor Suppressor Proteins, Rats
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