Cited by 239Axon Guidance and Neuronal SignalingNeurogenesis and neuroplasticity mechanismsDevelopmental Biology and Gene Regulation

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The Reelin Receptor ApoER2 Recruits JNK-interacting Proteins-1 and -2

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Stockinger, Walter, Brandes, Christian, Fasching, Daniela, Hermann, Marcela, Gotthardt, Michael, Herz, Joachim, Schneider, Wolfgang J., Nimpf, Johannes·2000·Journal of Biological Chemistry

DOI 10.1074/jbc.m004119200

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Abstract

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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Background
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BackgroundInfluential
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“…of ApoER2 which contain a proline-rich 59 amino acid domain allows its interactionwith different adaptor proteins, such us the c-junN-terminal kinase (JNK) interacting proteins, JIP1 and JIP2, and the synaptic protein, PSD95 (Herz and Chen, 2006; Larios and Marzolo, 2012; Stockinger et al., 2000).”
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“Moreover, JIP1 interacts with members of the Src and Abl tyrosine kinase families (4, 16, 24), the lipid phosphatase SHIP2 (44), the MAPK phosphatase MKP7 (43), -amyloid precursor protein (20, 31), the small GTPase regulatory proteins Ras-GRF1, p190-RhoGEF, RalGDS, and Tiam1 (2, 8, 21), ankyrin G (35), molecular chape…”
Background
Uner Tan Syndrome: History, Clinical Evaluations, Genetics, and the Dynamics of Human Quadrupedalism
Tan, Ü. (2010) · The Open Neurology Journal · doi:10.2174/1874205x01004010078 · Cited by 30
“The VLDLR gene is part of the reelin signaling pathway, which controls neuroblast migration in the developing cerebrocerebellar structures [50], and there is evidence that the reelin signaling pathway played a key role in the evolution of the cerebral cortex from stem amniotes (stem reptiles) to mammals [51].”
Background
The E3 ubiquitin ligase IDOL regulates synaptic ApoER2 levels and is important for plasticity and learning
Gao, J., Marosi, M., Choi, J., Achiro, J. M., Kim, S., Li, S., Otis, K., Martin, K. C., Portera-Cailliau, C., & Tontonoz, P. (2017) · eLife · doi:10.7554/elife.29178 · Cited by 30
“Our data suggest that postsynaptic JIP (Stockinger et al., 2000; Verhey et al., 2001) and Tiam1 (Buchsbaum et al.”
BackgroundInfluential
Src Family Kinases Directly Regulate JIP1 Module Dynamics and Activation
Nihalani, D., Wong, H. N., Verma, R. K., & Holzman, L. B. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01479-06 · Cited by 30
“ApoER2 interacts with its ligand, reelin (29, 31).”
BackgroundInfluential
The scaffold protein IB1/JIP-1 controls the activation of JNK in rat stressed urothelium
Tawadros, T., Formenton, A., Dudler, J., Thompson, N. A., NICOD, P. H., Leisinger, H., Waeber, G., & Haefliger, J. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.2.385 · Cited by 29
Low-Density Lipoprotein Receptor-Related Protein 8 (LRP8) Is Upregulated in Granulosa Cells of Bovine Dominant Follicle: Molecular Characterization and Spatio-Temporal Expression Studies1
Fayad, T., Lefebvre, R. C., Nimpf, J., Silversides, D. W., & Lussier, J. G. (2006) · Biology of Reproduction · doi:10.1095/biolreprod.106.057216 · Cited by 28
Increased JNK Phosphorylation and Oxidative Stress in Response to Increased Glucose Flux through Increased GLUT1 Expression in Rat Retinal Endothelial Cells
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JIP1 regulates neuronal apoptosis in response to stress
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Apolipoprotein E: a cholesterol transport protein with lipid transport-independent cell signaling properties
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APOE4 -VLDL Inhibits the HDL-Activated Phosphatidylinositol 3-Kinase/Akt Pathway via the Phosphoinositol Phosphatase SHIP2
DeKroon, R. M., Robinette, J. B., Hjelmeland, A. B., Wiggins, E., Blackwell, M., Mihovilovic, M., Fujii, M., York, J. D., Hart, J. L., Kontos, C. D., et al. (2006) · Circulation Research · doi:10.1161/01.res.0000245479.03190.9f · Cited by 27
Cell and molecular mechanisms that control cortical layer formation in the brain
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Sperm associated antigen 9 (SPAG9): a new member of c-Jun NH2-terminal kinase (JNK) interacting protein exclusively expressed in testis
Jagadish, N., Rana, R., Mishra, D., Kumar, M., & Suri, A. (2005) · The Keio Journal of Medicine · doi:10.2302/kjm.54.66 · Cited by 25
Ligand-induced Homotypic and Heterotypic Clustering of Apolipoprotein E Receptor 2
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Intrinsic disorder in proteins associated with oxidative stress-induced JNK signaling
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“JIP1 has also been reported to bind top190 Rho guanine nucleotide exchange factor (RhoGEF) [104], Apolipoprotein E receptor-2 (ApoER2) [105], LDL-receptor mediated protein, and megalin[106]through its PTB domain.”
Background
The Activation of Rac1 by M3 Muscarinic Acetylcholine Receptors Involves the Translocation of Rac1 and IQGAP1 to Cell Junctions and Changes in the Composition of Protein Complexes Containing Rac1, IQGAP1, and Actin
Ruiz-Velasco, R., Lanning, C. C., & Williams, C. L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202664200 · Cited by 22
LDL receptor family: Isolation, production, and ligand binding analysis
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Characterization of the binding mode of JNK-interacting protein 1 (JIP1) to kinesin-light chain 1 (KLC1)
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The apoE receptor apoER2 is involved in the maintenance of efficient synaptic plasticity
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Role of leptin in reproduction
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Apolipoprotein E Affects In Vitro Axonal Growth and Regeneration via the MAPK Signaling Pathway
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Reelin and apolipoprotein E receptor 2 in the embryonic and mature brain: effects of an evolutionary change in the apoER2 gene
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Both the phosphoinositide and receptor binding activities of Dab1 are required for Reelin-stimulated Dab1 tyrosine phosphorylation
Xu, M. F., Arnaud, L., & Cooper, J. A. (2005) · Molecular Brain Research · doi:10.1016/j.molbrainres.2005.06.001 · Cited by 18
“Lysates were incubated with glutathione Sepharose beads loaded with GST or GST-VLDLR [17] for 1.5 hr at 4 C, then the beads were washed twice in the lysis buffer, eluted, and analyzed by SDS PAGE.”
MethodInfluential
SeP, ApoER2 and megalin as necessary factors to maintain Se homeostasis in mammals
Król, M. B., Gromadzińska, J., & Wąsowicz, W. (2012) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2012.03.003 · Cited by 17
Phosphorylation of KLC1 modifies interaction with JIP1 and abolishes the enhanced fast velocity of APP transport by kinesin-1
Chiba, K., Chien, K.-Y., Sobu, Y., Hata, S., Kato, S., Nakaya, T., Okada, Y., Nairn, A. C., Kinjo, M., Taru, H., et al. (2017) · Molecular Biology of the Cell · doi:10.1091/mbc.e17-05-0303 · Cited by 17
“…scaffold proteins of the c-Jun amino-terminal kinase (JNK) family (Dickens et al., 1997) and subsequently as adaptor proteins that recruit motor proteins to membrane-bound cargoes (Meyer et al., 1999; Stockinger et al., 2000; Matsuda et al., 2001; Verhey et al., 2001; Taru et al., 2002).”
Missense mutations resulting in type 1 lissencephaly
Reiner, O., & Coquelle, F. M. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-4344-0 · Cited by 17
JIP1 binding to RBP-Jk mediates cross-talk between the Notch1 and JIP1-JNK signaling pathway
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ApoER2: Functional Tuning Through Splicing
Gallo, C. M., Ho, A., & Beffert, U. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.00144 · Cited by 16
“A poE R 2: FunctionalTuning Through S plicing TABLE 1 | Continued Alternative Exon Functional domain affected In vitro phenotype In vivo phenotype Spatiotemporal distribution Splicing regulator Associated publications Murine exon 19 (Human exon 18) Cytoplasmic insert – Binds adaptor proteins JIP1, JIP2, PSD-95, APBA1,…”
BackgroundInfluential
The Reelin receptor ApoER2 is a cargo for the adaptor protein complex AP-4: Implications for Hereditary Spastic Paraplegia
Caracci, M. O., Pizarro, H., Alarcón-Godoy, C., Fuentealba, L. M., Farfán, P., Pace, R. D., Santibáñez, N., Cavieres, V. A., Pástor, T. P., Bonifacino, J. S., et al. (2024) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2024.102575 · Cited by 14
Mixed Lineage Kinase 2 Interacts with Clathrin and Influences Clathrin-coated Vesicle Trafficking
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Signaling By Fibroblast Growth Factors: The Inside Story
Goldfarb, M. P. (2001) · Science Signaling · doi:10.1126/scisignal.1062001pe37 · Cited by 14
Single molecule, long-read Apoer2 sequencing identifies conserved and species-specific splicing patterns
Gallo, C. M., Labadorf, A. T., Ho, A., & Beffert, U. (2022) · Genomics · doi:10.1016/j.ygeno.2022.110318 · Cited by 11
Human APOER2 Isoforms Have Differential Cleavage Events and Synaptic Properties
Omuro, K. C., Gallo, C. M., Scrandis, L., Ho, A., & Beffert, U. (2022) · Journal of Neuroscience · doi:10.1523/jneurosci.1800-21.2022 · Cited by 10
“The fourth domain is the hydrophobic transmembrane region (exons 16–17) and the fifth domain is the cytoplasmic tail (exon 18–19) that directs the receptor to clathrin-coated pits necessary for endocytosis and binds cytosolic adaptor proteins (Kim et al., 1996; Novak et al., 1996; Brandes et al., 1997; Gotthardt et al…”
Background
The interaction of Kinesin-1 with its adaptor protein JIP1 can be regulated via proteins binding to the JIP1-PTB domain
Satake, T., Otsuki, K., Banba, Y., Suenaga, J., Hirano, H., Yamanaka, Y., Ohno, S., & Hirai, S.-I. (2013) · BMC Cell Biology · doi:10.1186/1471-2121-14-12 · Cited by 12
“Ito M, Yoshioka K, Akechi M, Yamashita S, Takamatsu N, Sugiyama K, Hibi M, Nakabeppu Y, Shiba T, Yamamoto KI: JSAP1, a novel jun N-terminal protein kinase (JNK)-binding protein that functions as a Scaffold factor in the JNK signaling pathway.”
BackgroundInfluential
Stigmasterol promotes neuronal migration via reelin signaling in neurosphere migration assays
Haque, M. N., & Moon, I. S. (2018) · Nutritional Neuroscience · doi:10.1080/1028415x.2018.1544970 · Cited by 11
Regulation of the hippocampal translatome by Apoer2-ICD release
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“A second alternatively spliced exon (19 in mice, 18 in humans) encodes a proline-rich cytosolic domain, which is differentially spliced in an activity-dependent manner [2, 74].”
Background
The Impact of JNK on Neuronal Migration
Zdrojewska, J., & Coffey, E. T. (2013) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-7687-6_3 · Cited by 11
The Transmembrane Domain and PXXP Motifs of ApoE Receptor 2 Exclude It from Carrying out Clathrin-mediated Endocytosis
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Regulatory mechanism of Reelin activity: a platform for exploiting Reelin as a therapeutic agent
Hattori, M. (2025) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2025.1546083 · Cited by 10
“…canonical receptors on neuronal cells and induces the tyrosine phosphorylation of an intracellular adaptor protein called Dab1 (Hiesberger et al., 1999; Howell et al., 1999, 2000; Feng and Cooper, 2009), which is then rapidly degraded (Rice et al., 1998; Howell et al., 1999; Feng et al., 2007).”
Novel aspects of the apolipoprotein-E receptor family: regulation and functional role of their proteolytic processing
Larios, J. A., & Marzolo, M.-P. (2012) · Frontiers in Biology · doi:10.1007/s11515-011-1186-7 · Cited by 9
“Some of these proteins, including JIP1/2 (Stockinger et al., 2000), PSD95 (Herz and Chen, 2006) and the adaptor protein X11α/βMint (He et al.”
BackgroundInfluential
A collection of cDNAs enriched in upper cortical layers of the embryonic mouse brain
Garcı́a-Frigola, C., Burgaya, F., Calbet, M., López‐Doménech, G., de Lecea, L., & Soriano, E. (2004) · Molecular Brain Research · doi:10.1016/j.molbrainres.2003.12.014 · Cited by 10
Populations of Radial Glial Cells Respond Differently to Reelin and Neuregulin1 in a Ferret Model of Cortical Dysplasia
Poluch, S., & Juliano, S. L. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013709 · Cited by 10
“The role of the reelin receptors ApoER2 and VLVDR was evaluated using RAP, which blocks both receptors [46,47], or using SP600125 which blocks ApoER2 by inhibiting JIP activity [49].”
BackgroundMethod
Low-density lipoprotein receptor-related protein 8 gene polymorphisms and dementia
Helbecque, N., Cottel, D., & Amouyel, P. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.05.024 · Cited by 10

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
ORCID: Hermann, Marcela
Gotthardt, Michael
Herz, Joachim
Schneider, Wolfgang J.
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)
DOI: 10.1074/jbc.m004119200
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: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 7367 d)
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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The Reelin Receptor ApoER2 Recruits JNK-interacting Proteins-1 and -2

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