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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“8 C), although in line with our results requiring the presence of JIP-1 on pAPP-containing vesicles, takes into account the possibility that the JIP-1–kinesin-1 complex might be recruited to other vesicle proteins, such as ApoER2 (Stockinger et al., 2000; Verhey et al., 2001).”
Result
Essential Role of the Apolipoprotein E Receptor-2 in Sperm Development
Andersen, O. M., Yeung, C.-H., Vorum, H., Wellner, M., Andreassen, T. K., Erdmann, B., Mueller, E.-C., Herz, J., Otto, A., Cooper, T. G., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302157200 · Cited by 112
The JNK-interacting Protein-1 Scaffold Protein Targets MAPK Phosphatase-7 to Dephosphorylate JNK
Willoughby, E. A., Perkins, G. R., Collins, M. K., & Whitmarsh, A. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m207324200 · Cited by 109
Binding of purified Reelin to ApoER2 and VLDLR mediates tyrosine phosphorylation of Disabled-1
Benhayon, D., Magdaleno, S. M., & Curran, T. (2003) · Molecular Brain Research · doi:10.1016/s0169-328x(03)00032-9 · Cited by 109
Canonical and non-canonical Reelin signaling
Bock, H. H., & May, P. (2016) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2016.00166 · Cited by 107
“Scaffold proteins of the JIP and MINT families also bind to Apoer2, but not to Vldlr (Figure 2E), in an exon 19-dependent manner (Gotthardt et al., 2000; Stockinger et al., 2000; Verhey et al., 2001; He et al., 2007; Minami et al., 2010).”
Background
Effects of UV Photographs, Photoaging Information, and Use of Sunless Tanning Lotion on Sun Protection Behaviors
Mahler, H. I. M., Kulik, J. A., Harrell, J., Correa, A., Gibbons, F. X., & Gerrard, M. (2005) · Archives of Dermatology · doi:10.1001/archpedi.161.4.356 · Cited by 106
Scaffold proteins in MAP kinase signaling: more than simple passive activating platforms
Dard, N., & Peter, M. (2006) · BioEssays · doi:10.1002/bies.20351 · Cited by 106
“Finally, JIP1/2 were found to interact with ApoER2, Megalin and LRP, three proteins that belong to the LDL receptor gene family.((52,53)) The function of these interactions remains to be elucidated, but they suggest that LDL receptors may propagate MAPK signaling through the recruitment of scaffold proteins and fulfil…”
Low‐density lipoprotein receptors regulate microglial inflammation through c‐Jun N‐terminal kinase
Pocivavsek, A., Burns, M. P., & Rebeck, G. W. (2009) · Glia · doi:10.1002/glia.20772 · Cited by 96
“Of particular relevance to this study, the cytoplasmic domain of LRP1 binds JNK-interacting proteins (JIP-1 and JIP-2) (Stockinger et al., 2000).”
Background
LRP1 integrates murine macrophage cholesterol homeostasis and inflammatory responses in atherosclerosis
Xian, X., Ding, Y., Dieckmann, M., Zhou, L., Plattner, F., Liu, M., Parks, J. S., Hammer, R. E., Boucher, P., Tsai, S. X., et al. (2017) · eLife · doi:10.7554/elife.29292 · Cited by 102
“The LRP1 cytoplasmic domain interacts with numerous intracellular adaptor and scaffold proteins (Gotthardt et al., 2000; Herz and Strickland, 2001; Stockinger et al., 2000).”
Background
LRP-1 Promotes Cancer Cell Invasion by Supporting ERK and Inhibiting JNK Signaling Pathways
Langlois, B., Perrot, G., Schneider, C., Henriet, P., Emonard, H., Martiny, L., & Dedieu, S. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011584 · Cited by 102
“The presence of JNK on LRP-1-ICD is consistent with studies performed on the Reelin receptor ApoER2 (apolipoprotein E receptor 2)/LRP-8, a close member of the LDL receptor family [48].”
Method
Modulation of lipoprotein receptor functions by intracellular adaptor proteins
Stolt-Bergner, P. C., & Bock, H. H. (2006) · Cellular Signalling · doi:10.1016/j.cellsig.2006.03.008 · Cited by 101
Multiple pathways of apolipoprotein E signaling in primary neurons
Hoe, H., Harris, D. C., & Rebeck, G. W. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.03007.x · Cited by 111
“We focused on these pathways because of the various adaptor proteins that have been identified as binding the C-termini of apoE receptors, including Dab1, JIP, and PSD-95 (Gotthard et al. 2000; Stockinger et al. 2000).”
Background
Similarities and differences in structure, expression, and functions of VLDLR and ApoER2
Reddy, S. S., Connor, T. E., Weeber, E. J., & Rebeck, W. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-30 · Cited by 93
Molecular motors: from one motor many tails to one motor many tales
Goldstein, L. S. B. (2001) · Trends in Cell Biology · doi:10.1016/s0962-8924(01)02143-2 · Cited by 99
The Reelin Receptors Apolipoprotein E receptor 2 (ApoER2) and VLDL Receptor
Dlugosz, P., & Nimpf, J. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19103090 · Cited by 91
“Indeed, a two-hybrid screen for potential binding partners led to the identification of JNK-interacting proteins JIP-1 and JIP-2, which act as molecular scaffolds for JNK-signalling and they play essential roles in cell proliferation, differentiation, migration and apoptosis [21,22].”
Background
From cholesterol transport to signal transduction: low density lipoprotein receptor, very low density lipoprotein receptor, and apolipoprotein E receptor-2
Nimpf, J. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/s1388-1981(00)00155-4 · Cited by 89
Reelin-mediated signaling in neuropsychiatric and neurodegenerative diseases
Knuesel, I. (2010) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2010.04.002 · Cited by 89
“This exon encodes the binding site that mediates the interaction of ApoER2 with PSD-95, and with JNK-interacting proteins 1 and 2 (JIP), involved in the assembly of a kinase activating complex at the cytoplasmic domain of ApoER2 (Gotthardt et al., 2000; Stockinger et al., 2000).”
MAPK-upstream protein kinase (MUK) regulates the radial migration of immature neurons in telencephalon of mouse embryo
Hirai, S.-I., Kawaguchi, A., Hirasawa, R., Baba, M., Ohnishi, T., & Ohno, S. (2002) · Development · doi:10.1242/dev.129.19.4483 · Cited by 86
Genetic Modulation of Tau Phosphorylation in the Mouse
Brich, J., Shie, F., Howell, B. W., Li, R., Tus, K., Wakeland, E. K., Jin, L., Mumby, M. C., Churchill, G. A., Herz, J., et al. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-01-00187.2003 · Cited by 84
“However, it was not evident whether Dab1 would be involved in the regulation of tau phosphorylation, because VLDLR and ApoER2 have Dab1-independent binding functions (Stockinger et al., 2000).”
Background
Localization of ApoER2, VLDLR and Dab1 in radial glia: groundwork for a new model of reelin action during cortical development
Luque, J. M., Morante, J., & Fairén, A. (2003) · Developmental Brain Research · doi:10.1016/s0165-3806(02)00604-1 · Cited by 86
The Abluminal Endothelial Membrane in Neurovascular Remodeling in Health and Disease
Hermann, D. M., & ElAli, A. (2012) · Science Signaling · doi:10.1126/scisignal.2002886 · Cited by 86
Conserved and divergent patterns of Reelin expression in the zebrafish central nervous system
Costagli, A., Kapsimali, M., Wilson, S. W., & Mione, M. (2002) · The Journal of Comparative Neurology · doi:10.1002/cne.10292 · Cited by 83
“…stabilizing the organization of the synaptic cleft, are thought to signal through the receptor molecules and promote the stabilization of dendritic spine microtubules through Dab1 phosphorylation and interactions with various cytoskeletal components (Stockinger et al., 2000; Feng and Walsh, 2001).”
Background
A secreted soluble form of ApoE receptor 2 acts as a dominant-negative receptor and inhibits Reelin signaling
Koch, S., Strasser, V., Hauser, C., Fasching, D., Brandes, C., Bajari, T. M., Schneider, W. J., & Nimpf, J. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf599 · Cited by 80
Gene Expression Profiling of Differentially Expressed Genes in Granulosa Cells of Bovine Dominant Follicles Using Suppression Subtractive Hybridization1
Fayad, T., Lévesque, V., Sirois, J., Silversides, D. W., & Lussier, J. G. (2004) · Biology of Reproduction · doi:10.1095/biolreprod.103.021709 · Cited by 81
“Furthermore, the ApoER2 contains a specific 59 amino acid proline-rich region found in its cytoplasmic domain that interacts with the c-Jun N-terminal kinase interacting protein (JIP) family [55, 56].”
Background
Trafficking of signaling modules by kinesin motors
Schnapp, B. J. (2003) · Journal of Cell Science · doi:10.1242/jcs.00488 · Cited by 82
“Among the many different transmembrane receptors implicated in JNK signaling is ApoER2, the Reelin receptor (Stockinger et al., 2000).”
Background
Molecular biology of apolipoprotein E
Strittmatter, W. J., & Hill, C. B. (2002) · Current Opinion in Lipidology · doi:10.1097/00041433-200204000-00002 · Cited by 80
Do Disorders of Movement Cause Movement Disorders and Dementia?
Goldstein, L. S. B. (2003) · Neuron · doi:10.1016/s0896-6273(03)00630-5 · Cited by 78
The LDL receptor gene family: signaling functions during development
Howell, B. W., & Herz, J. (2001) · Current Opinion in Neurobiology · doi:10.1016/s0959-4388(00)00176-8 · Cited by 78
Alternative Splicing in the Ligand Binding Domain of Mouse ApoE Receptor-2 Produces Receptor Variants Binding Reelin but Not α2-Macroglobulin
Brandes, C., Kahr, L., Stockinger, W., Hiesberger, T., Schneider, W. J., & Nimpf, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102662200 · Cited by 78
ApoE receptor 2 controls neuronal survival in the adult brain
Beffert, U., Nematollah Farsian, F., Masiulis, I., Hammer, R. E., Yoon, S. O., Giehl, K. M., & Herz, J. (2006) · Current Biology · doi:10.1016/j.cub.2006.10.029 · Cited by 84
“PSD95 and JIPs interact with sequences within exon 19 (blue).”
BackgroundInfluential
Expanding functions of lipoprotein receptors
Herz, J., Chen, Y., Masiulis, I., & Zhou, L. (2008) · Journal of Lipid Research · doi:10.1194/jlr.r800077-jlr200 · Cited by 80
“for cJun-N-terminal kinase interacting proteins ( JIPs) (21, 22), in the ICD of Apoer2 (19).”
Background
Identification of a Major Cyclic AMP-Dependent Protein Kinase A Phosphorylation Site within the Cytoplasmic Tail of the Low-Density Lipoprotein Receptor-Related Protein: Implication for Receptor-Mediated Endocytosis
Li, Y., van Kerkhof, P., Marzolo, M., Strous, G. J., & Bu, G. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.4.1185-1195.2001 · Cited by 75
“Recently, studies have revealed new roles of LDLR family members as transducers of extracellular signals (17, 22, 24, 43, 46, 47).”
Background
Apolipoprotein E (apoE) isoforms differentially induce nitric oxide production in endothelial cells
Sacre, S. M., Stannard, A. K., & Owen, J. S. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00261-8 · Cited by 73

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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