The DOI matches its Crossref record; 43 of the 43 references it cites were found in a registry or an index.
Reeler/Disabled-like Disruption of Neuronal Migration in Knockout Mice Lacking the VLDL Receptor and ApoE Receptor 2
Open accessAbstract
Layering of neurons in the cerebral cortex and cerebellum requires Reelin, an extracellular matrix protein, and mammalian Disabled (mDab1), a cytosolic protein that activates tyrosine kinases. Here, we report the requirement for two other proteins, cell surface receptors termed very low density lipoprotein receptor (VLDLR) and apolipoprotein E receptor 2 (ApoER2). Both receptors can bind mDab1 on their cytoplasmic tails and are expressed in cortical and cerebellar layers adjacent to layers that express Reelin. mDab1 expression is upregulated in knockout mice that lack both VLDLR and ApoER2. Inversion of cortical layers and absence of cerebellar foliation in these animals precisely mimic the phenotype of mice lacking Reelin or mDab1. These findings suggest that VLDLR and ApoER2 participate in transmitting the extracellular Reelin signal to intracellular signaling processes initiated by mDab1.
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“These results suggest that Reelin controls neuronal migration and positioning by stimulating tyrosine phosphorylation of Dab1 via VLDLR, ApoER2, and CNR family proteins.”
From Reelin molecules assemble together to form a large protein complex, which is inhibited by the function-blocking CR-50 antibody (2000) · cites this paper as [34]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“The knockdown of both VLDLR and ApoER2 cause a Reeler-phenotype in mice, resulting in neuronal lamination defects in both the cortex and cerebellum [13].”
From PCSK9 regulates neuronal apoptosis by adjusting ApoER2 levels and signaling (2012) · cites this paper as [13]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Reelin and ApoE bind to and activate ApoER2 and VLDLR, controlling cortical and cerebellar development [13,14], promoting cell survival [15], and regulating N-methyl-D-aspartic acid (NMDA) receptor activity through phosphorylation [16,17].”
From PCSK9 regulates neuronal apoptosis by adjusting ApoER2 levels and signaling (2012) · cites this paper as [13]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“ApoER2 binds the extracellular matrix protein reelin during development [4], [6], triggering a signaling pathway that regulates neuronal migration and the formation of laminated brain structures such as the cortex, hippocampus [7] and cerebellum [4]”
From Sorting nexin 17 regulates ApoER2 recycling and reelin signaling (2014) · cites this paper as [4]
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In the citing paper
“VLDLR and APOER2 mediate Reelin signaling, which is essential for neuronal migration during brain development.”
From Deletion of neuronal Idol ameliorates Alzheimer's disease–related pathologies via APOE receptors (2025) · cites this paper as [77]
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“Reelin interaction with the VLDLR and ApoER2 is critical during development because it properly directs the positioning of neurons (16, 20, 21).”
From The E3 ubiquitin ligase IDOL induces the degradation of the low density lipoprotein receptor family members VLDLR and ApoER2 (2010) · cites this paper as [16]
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“In addition to their proposed roles in metabolism, the VLDLR and ApoER2 are critical for neuronal migration during development (16, 20, 21).”
From The E3 ubiquitin ligase IDOL induces the degradation of the low density lipoprotein receptor family members VLDLR and ApoER2 (2010) · cites this paper as [16]
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“studies in recent years have established a critical role for VLDLR and ApoER2 in the neuronal Reelin pathway that is essential for proper neuronal positioning and brain development (16–19).”
From The E3 ubiquitin ligase IDOL induces the degradation of the low density lipoprotein receptor family members VLDLR and ApoER2 (2010) · cites this paper as [16]
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“Because only the combined loss of both receptors results in severely impaired neuronal positioning (16), the ability of IDOL to simultaneously target both receptors for degradation may allow it to modulate this pathway.”
From The E3 ubiquitin ligase IDOL induces the degradation of the low density lipoprotein receptor family members VLDLR and ApoER2 (2010) · cites this paper as [16]
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“Similar to other members of the LDL-R family, ApoER2 contains a multifunctional NPxY motif, which is responsible for its signaling [4], [11], endocytosis [24] and also the role of facilitating the interaction with several adaptor proteins [54], [55].”
From Sorting nexin 17 regulates ApoER2 recycling and reelin signaling (2014) · cites this paper as [4]
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“However, both LRP (48,49) and other members of the LDL receptor-related family (50) have been implicated as having signaling roles in neurons, and it seems likely that the cleavage of LRP we observe could modulate such signaling.”
From The Low Density Lipoprotein Receptor-related Protein (LRP) Is a Novel β-Secretase (BACE1) Substrate (2005) · cites this paper as [50]
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“However, both LRP (48,49) and other members of the LDL receptor-related family (50) have been implicated as having signaling roles in neurons, and it seems likely that the cleavage of LRP we observe could modulate such signaling.”
From The Low Density Lipoprotein Receptor-related Protein (LRP) Is a Novel β-Secretase (BACE1) Substrate (2005) · cites this paper as [50]
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“For example, a recent report linked two members of the LDLR receptor family, the very LDLR and ER2, to signal transduction pathways in the central nervous system (54).”
From Apolipoprotein E Receptors Mediate the Effects of β-Amyloid on Astrocyte Cultures (2000) · cites this paper as [54]
In the citing paper
“Several non-apolipoprotein ligands have also been proposed for VLDLR, including Reelin2 and F-spondin55.”
From IDOL regulates systemic energy balance through control of neuronal VLDLR expression (2019) · cites this paper as [2]
In the citing paper
“Consistently, Lrp8-null mice show ectopic Purkinje cells similar to the Rbfox2-null mice59,60.”
From The neurogenetics of alternative splicing (2016) · cites this paper as [59]
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Self-citationDorrell, M. I., Aguilar, E., Jacobson, R., Yanes, O., Gariano, R., Heckenlively, J., Banin, E., Ramirez, G. A., Gasmi, M., Bird, A., et al. (2009) · Journal of Clinical Investigation · doi:10.1172/jci35977 · Cited by 127
Reduced Blood Levels of Reelin as a Vulnerability Factor in Pathophysiology of Autistic Disorder
Fatemi, S. H., Stary, J. M., & Egan, E. A. (2002) · Cellular and Molecular Neurobiology · doi:10.1023/a:1019857620251 · Cited by 122
Reelin in the years: controlling neuronal migration and maturation in the mammalian brain
D'Arcangelo, G. (2014) · Advances in Neuroscience · doi:10.1155/2014/597395 · Cited by 120
Functional Roles of the Interaction of APP and Lipoprotein Receptors
Pohlkamp, T., Wasser, C. R., & Herz, J. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00054 · Cited by 92
Self-citationCanonical and non-canonical Reelin signaling
Bock, H. H., & May, P. (2016) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2016.00166 · Cited by 107
Alzheimer disease pathology in cognitively healthy elderly: A genome-wide study
Kramer, P. L., Xu, H., Woltjer, R. L., Westaway, S. K., Clark, D., Erten-Lyons, D., Kaye, J. A., Welsh-Bohmer, K. A., Troncoso, J. C., Markesbery, W. R., et al. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.01.010 · Cited by 108
Apolipoprotein E Receptors Mediate the Effects of β-Amyloid on Astrocyte Cultures
LaDu, M. J., Shah, J. A., Reardon, C. A., Getz, G. S., Bu, G., Hu, J., Guo, L., & Van Eldik, L. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000602200 · Cited by 103
Bock, H. H., Jossin, Y., May, P., Bergner, O., & Herz, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401770200 · Cited by 102
Self-citationReversal of ApoE4-induced recycling block as a novel prevention approach for Alzheimer’s disease
Xian, X., Pohlkamp, T., Durakoglugil, M. S., Wong, C. H., Beck, J. K., Lane-Donovan, C., Plattner, F., & Herz, J. (2018) · eLife · doi:10.7554/elife.40048 · Cited by 98
Self-citationReelin deficiency causes granule cell dispersion in epilepsy
Haas, C. A., & Frotscher, M. (2010) · Experimental Brain Research · doi:10.1007/s00221-009-1948-5 · Cited by 96
Reelin depletion is an early phenomenon of Alzheimer's pathology
Herring, A., Donath, A., Steiner, K. M., Widera, M. P., Hamzehian, S., Kanakis, D., Kölble, K., ElAli, A., Hermann, D. M., Paulus, W., et al. (2012) · Journal of Alzheimer's Disease · doi:10.3233/jad-2012-112069 · Cited by 92
Reelin protects against amyloid β toxicity in vivo
Lane-Donovan, C., Philips, G. T., Wasser, C. R., Durakoglugil, M. S., Masiulis, I., Upadhaya, A., Pohlkamp, T., Coskun, C., Kotti, T., Steller, L., et al. (2015) · Science Signaling · doi:10.1126/scisignal.aaa6674 · Cited by 96
Self-citationAge-related accumulation of Reelin in amyloid-like deposits
Knuesel, I., Nyffeler, M., Mormède, C., Muhia, M., Meyer, U., Pietropaolo, S., Yee, B. K., Pryce, C. R., LaFerla, F. M., Marighetto, A., et al. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.08.011 · Cited by 94
Reduction of Crk and CrkL expression blocks reelin-induced dendritogenesis
Matsuki, T., Pramatarova, A., & Howell, B. W. (2008) · Journal of Cell Science · doi:10.1242/jcs.027334 · Cited by 92
Nakajima, C., Kulik, A., Frotscher, M., Herz, J., Schäfer, M., Bock, H. H., & May, P. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.444364 · Cited by 85
Self-citationReelin-mediated signaling in neuropsychiatric and neurodegenerative diseases
Knuesel, I. (2010) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2010.04.002 · Cited by 89
ApoE isoform-dependent changes in hippocampal synaptic function
Korwek, K. M., Trotter, J. H., LaDu, M. J., Sullivan, P. M., & Weeber, E. J. (2009) · Molecular Neurodegeneration · doi:10.1186/1750-1326-4-21 · Cited by 89
Unique Requirement for Rb/E2F3 in Neuronal Migration: Evidence for Cell Cycle-Independent Functions
McClellan, K. A., Ruzhynsky, V. A., Douda, D. N., Vanderluit, J. L., Ferguson, K. L., Chen, D., Bremner, R., Park, D. S., Leone, G., & Slack, R. S. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02100-06 · Cited by 88
Leemhuis, J., Bouché, E., Frotscher, M., Henle, F., Hein, L., Herz, J., Meyer, D. K., Pichler, M., Roth, G., Schwan, C., et al. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.4036-10.2010 · Cited by 80
Self-citationKoch, 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
Self-citationRole for Reelin in neurotransmitter release
Hellwig, S., Hack, I., Kowalski, J., Brunne, B., Jarowyj, J., Unger, A., Bock, H. H., Junghans, D., & Frotscher, M. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.3984-10.2011 · Cited by 74
Choi, H. Y., Liu, Y., Tennert, C., Sugiura, Y., Karakatsani, A., Kröger, S., Johnson, E. B., Hammer, R. E., Lin, W., & Herz, J. (2013) · eLife · doi:10.7554/elife.00220 · Cited by 71
Self-citationDing, Y., Huang, L., Xian, X., Yuhanna, I. S., Wasser, C. R., Frotscher, M., Mineo, C., Shaul, P. W., & Herz, J. (2016) · Science Signaling · doi:10.1126/scisignal.aad5578 · Cited by 72
Self-citationFuentealba, R. A., Barría, M. I., Lee, J., Cam, J., Araya, C., Escudero, C. A., Inestrosa, N. C., Bronfman, F. C., Bu, G., & Marzolo, M.-P. (2007) · Molecular Neurodegeneration · doi:10.1186/1750-1326-2-14 · Cited by 70
Duit, S., Mayer, H., Blake, S. M., Schneider, W. J., & Nimpf, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.025973 · Cited by 71
Self-citationThe generation and function of soluble apoE receptors in the CNS
Rebeck, G. W., LaDu, M. J., Estus, S., Bu, G., & Weeber, E. J. (2006) · Molecular Neurodegeneration · doi:10.1186/1750-1326-1-15 · Cited by 66
Tinnes, S., Schäfer, M. K. E., Flubacher, A., Münzner, G., Frotscher, M., & Haas, C. A. (2011) · The FASEB Journal · doi:10.1096/fj.10-168294 · Cited by 58
Differential splicing and glycosylation of Apoer2 alters synaptic plasticity and fear learning
Wasser, C. R., Masiulis, I., Durakoglugil, M. S., Lane-Donovan, C., Xian, X., Beffert, U., Agarwala, A., Hammer, R. E., & Herz, J. (2014) · Science Signaling · doi:10.1126/scisignal.2005438 · Cited by 48
Self-citationApoE receptor 2 regulates synapse and dendritic spine formation
Dumanis, S. B., Cha, H.-J., Song, J. M., Trotter, J. H., Spitzer, M., Lee, J.-Y., Weeber, E. J., Turner, R. S., Pak, D. T. S., Rebeck, G. W., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017203 · Cited by 45
Differential gene expression in migratory streams of cortical interneurons
Antypa, M., Faux, C., Eichele, G., Parnavelas, J. G., & Andrews, W. D. (2011) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2011.07896.x · Cited by 49
Zolochevska, O., & Taglialatela, G. (2016) · Current Pharmaceutical Design · doi:10.2174/1381612822666160518142110 · Cited by 49
Larouche, M., Beffert, U., Herz, J., & Hawkes, R. (2008) · PLoS ONE · doi:10.1371/journal.pone.0001653 · Cited by 49
Self-citationSorting nexin 17 regulates ApoER2 recycling and reelin signaling
Sotelo, P., Farfán, P., Benitez, M. L., Bu, G., & Marzolo, M.-P. (2014) · PLoS ONE · doi:10.1371/journal.pone.0093672 · Cited by 47
Metadata
- Authors
- Trommsdorff, M., Gotthardt, M., Hiesberger, T., Shelton, J., Stockinger, W., Nimpf, J., Hammer, R. E., Richardson, J. A., & Herz, J.
- Affiliations
- The University of Texas Southwestern Medical Center (US)
- University of Vienna (AT)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Herz, Joachim
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1999-06
- Volume
- 97
- Issue
- 6
- Pages
- 689-701
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2079396188
- Cited by
- 1,261
- References
- 43
- Citations by year
- 2026: 8 · 2025: 28 · 2024: 16 · 2023: 24 · 2022: 23 · 2021: 32 · 2020: 30 · 2019: 27 · 2018: 30 · 2017: 49 · 2016: 42 · 2015: 32 · 2014: 38 · 2013: 47 · 2012: 57
- FWCI
- 27.71
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- MDC Repository (Max-Delbrueck-Center for Molecular Medicine) (submittedVersion)
- Funders
- National Institute on Aging (P30AG012300, AG 12300)
- National Heart, Lung, and Blood Institute (HL-20948, R37HL063762, P01HL020948)
- 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
- reelin, VLDL receptor, neuronal migration, cortical lamination, cerebellar foliation, Reelin signaling, knockout mice, extracellular matrix, tyrosine kinase signaling
- MeSH terms
- Reelin Protein, Amino Acid Sequence, Animals, Cell Line, Cell Movement, Cerebral Cortex, Dendrites, Female, Mice, Mutant Strains, Molecular Sequence Data, Nerve Tissue Proteins, Purkinje Cells, Receptors, LDL, Recombinant Fusion Proteins, Serine Endopeptidases, Cell Adhesion Molecules, Neuronal, Up-Regulation, Extracellular Matrix Proteins, Receptors, Lipoprotein, Mice, Knockout, LDL-Receptor Related Proteins, Mice
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