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The Reelin Receptor ApoER2 Recruits JNK-interacting Proteins-1 and -2
Open accessAbstract
Correct positioning of neurons during embryonic development of the brain depends, among other processes, on the proper transmission of the reelin signal into the migrating cells via the interplay of its receptors with cytoplasmic signal transducers. Cellular components of this signaling pathway characterized to date are cell surface receptors for reelin like apolipoprotein E receptor 2 (ApoER2), very low density lipoprotein receptor (VLDLR), and cadherin-related neuronal receptors, and intracellular components like Disabled-1 and the nonreceptor tyrosine kinase Fyn, which bind to the intracellular domains of the ApoER2 and VLDL receptor or of cadherin-related neuronal receptors, respectively. Here we show that ApoER2, but not VLDLR, also binds the family of JNK-interacting proteins (JIPs), which act as molecular scaffolds for the JNK-signaling pathway. The ApoER2 binding domain on JIP-2 does not overlap with the binding sites for MLK3, MKK7, and JNK. These results suggest that ApoER2 is able to assemble a multiprotein complex containing Disabled-1 and JIPs, together with their binding partners, to the cell surface of neurons. This complex might participate in ApoER2-specific reelin signaling and thus would explain the different phenotype of mice lacking the ApoER2 from that of VLDLR-deficient mice.
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“It has previously been reported that c-jun-terminal kinase interacting proteins 1/2 (JIP1/2) interact with ApoER2 (Stockinger et al., 2000) as well as Tiam1 (Buchsbaum et al., 2002), the major Rac guanine nucleotide exchange factor that couples the NMDAR to Rac1 (Tolias et al., 2005).”
From The E3 ubiquitin ligase IDOL regulates synaptic ApoER2 levels and is important for plasticity and learning (2017) · cites this paper as Stockinger et al., 2000
In the citing paper
“Our data suggest that postsynaptic JIP (Stockinger et al., 2000; Verhey et al., 2001) and Tiam1 (Buchsbaum et al., 2002) could be involved in mediating the effects of IDOL-ApoER2 axis on Rac1 activity.”
From The E3 ubiquitin ligase IDOL regulates synaptic ApoER2 levels and is important for plasticity and learning (2017) · cites this paper as Stockinger et al., 2000
In the citing paper
“JIP-1 and JIP-2 have additionally been found to interact with rhoGEF (Meyer et al. 1999) and with the cell surface receptor for Reelin, ApoER2 (Stockinger et al. 2000).”
From Cargo of kinesin identified as JIP scaffolding proteins and associated signaling molecules (2001) · cites this paper as Stockinger et al. 2000
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“In addition, JIP1 and JIP2 contain a phosphotyrosine-binding domain, which interacts with the reelin receptor APOER2 (Ref”
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Metadata
- Authors
- Stockinger, W., Brandes, C., Fasching, D., Hermann, M., Gotthardt, M., Herz, J., Schneider, W. J., & Nimpf, J.
- Affiliations
- University of Vienna (AT)
- The University of Texas Southwestern Medical Center (US)
- Corresponding author
- Nimpf, Johannes
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-08
- Volume
- 275
- Issue
- 33
- Pages
- 25625-25632
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2022840078
- Cited by
- 239
- References
- 51
- Citations by year
- 2025: 2 · 2024: 3 · 2023: 3 · 2022: 5 · 2020: 2 · 2019: 2 · 2018: 6 · 2017: 6 · 2016: 5 · 2015: 4 · 2014: 4 · 2013: 4 · 2012: 6
- FWCI
- 11.86
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- MDC Repository (Max-Delbrueck-Center for Molecular Medicine) (submittedVersion)
- Funders
- National Heart, Lung, and Blood Institute (R37HL063762)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Axon Guidance and Neuronal Signaling
- Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
- Keywords
- ApoER2, Reelin signaling, JNK signaling, VLDLR, Disabled-1, Fyn, neuronal migration, signal transduction, protein complex formation, Reelin receptors
- MeSH terms
- Reelin Protein, Amino Acid Sequence, Animals, Brain, Carrier Proteins, Cell Differentiation, Cells, Cultured, Cytoplasm, Epididymis, Glutathione Transferase, Humans, Immunohistochemistry, Male, Microscopy, Fluorescence, Models, Biological, Molecular Sequence Data, Nerve Tissue Proteins, Neurons, Proline, Protein Binding, Serine Endopeptidases, Stem Cells, Tissue Distribution, Blotting, Northern, Signal Transduction, Cell Adhesion Molecules, Neuronal, Extracellular Matrix Proteins, Sequence Homology, Amino Acid, Alternative Splicing, DNA, Complementary, Receptors, Lipoprotein, Reverse Transcriptase Polymerase Chain Reaction, Two-Hybrid System Techniques, LDL-Receptor Related Proteins, Adaptor Proteins, Signal Transducing, Mice
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