Reconstitution of the Reelin Signaling Pathway in Fibroblasts Demonstrates that Dab1 Phosphorylation Is Independent of Receptor Localization in Lipid Rafts
Open accessAbstract
The Reelin signaling pathway operates in migrating neurons and is indispensable for their correct positioning during embryonic brain development. Many biochemical and cell biological studies to dissect the Reelin pathway at the molecular level are hampered by the lack of a cell line harboring a functional Reelin signaling pathway. Here we present fibroblast cell lines in which all required functional components of the pathway have been reconstituted. These cells react upon Reelin treatment in the same way as primary neurons. We have subsequently used these cell lines to study the subcellular localization of ApoER2 and the VLDL receptor and could demonstrate that receptor-mediated Dab1 phosphorylation does not depend on lipid rafts and that phosphorylated Dab1 remains bound to the receptor tail when the pathway is activated by Reelin.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Ligand-activated LXR decreases VLDLR and APOER2 protein levels in 3T3 fibroblasts stably expressing these receptors.
“In similar studies, we also found that ligand-activated LXR decreased the level of VLDLR and APOER2 in 3T3 fibroblasts stably expressing these receptors (Fig. 1C) (22).”
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 [22]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Hiesberger, T., Trommsdorff, M., Howell, B. W., Goffinet, A., Mumby, M. C., Cooper, J. A., & Herz, J. (1999) · Neuron · doi:10.1016/s0896-6273(00)80861-2 · Cited by 916 · see citing works
Proteins of the CNR Family Are Multiple Receptors for Reelin
Senzaki, K., Ogawa, M., & Yagi, T. (1999) · Cell · doi:10.1016/s0092-8674(00)81552-4 · Cited by 272 · see citing works
Methodological factors influencing measurement and processing of plasma reelin in humans
Lugli, G., Krueger, J. M., Davis, J. M., Persico, A. M., Keller, F., & Smalheiser, N. R. (2003) · BMC Biochemistry · doi:10.1186/1471-2091-4-9 · Cited by 60 · see citing works
Flagged first, then by citations
Research works printed but not linked: 2
- [1]1. Andjelkovic, M., T. Jakubowicz, P. Cron, X. F. Ming, J. W. Han, and B. A. Hemmings. 1996. Activation and phosphorylation of a pleckstrin homology domain containing protein kinase (RAC-PK/PKB) promoted by serum and protein phosphatase inhibitors. Proc. Natl. Acad. Sci. USA 93: 5699-5704.
- [44]44. Stolt, P. C., H. Jeon, H. K. Song, J. Herz, M. J. Eck, and S. C. Blacklow. 2003. Origins of Peptide selectivity and phosphoinositide binding revealed by structures of Disabled-1 PTB domain complexes. Structure (Cambridge) 11: 569-579.
Cited by
Sorted by citations
Reelin, lipoprotein receptors and synaptic plasticity
Herz, J., & Chen, Y. (2006) · Nature Reviews Neuroscience · doi:10.1038/nrn2009 · Cited by 524 · see citing works
Nova2 Regulates Neuronal Migration through an RNA Switch in Disabled-1 Signaling
Yano, M., Hayakawa-Yano, Y., Mele, A., & Darnell, R. B. (2010) · Neuron · doi:10.1016/j.neuron.2010.05.007 · Cited by 176 · see citing works
Hong, C., Duit, S., Jalonen, P., Out, R., Scheer, L., Sorrentino, V., Boyadjian, R., Rodenburg, K. W., Foley, E., Korhonen, L., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.123729 · Cited by 142 · see citing works
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 · see citing works
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 · see citing works
Self-citationApoER2 processing by presenilin-1 modulates reelin expression
Balmaceda, V., Cuchillo‐Ibáñez, I., Pujadas, L., García‐Ayllón, M., Saura, C. A., Nimpf, J., Soriano, E., & Sáez‐Valero, J. (2014) · The FASEB Journal · doi:10.1096/fj.13-239350 · Cited by 40 · see citing works
Self-citationMinami, S. S., Sung, Y. M., Dumanis, S. B., Chi, S. H., Burns, M. P., Ann, E.-J., Suzuki, T., Turner, R. S., Park, H.-S., Pak, D. T. S., et al. (2010) · The FASEB Journal · doi:10.1096/fj.09-138123 · Cited by 28 · see citing works
- Authors
- Mayer, H., Duit, S., Hauser, C., Schneider, W. J., & Nimpf, J.
- Affiliations
- Max Perutz Labs (AT)
- Corresponding author
- Nimpf, Johannes
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2006-01-01
- Volume
- 26
- Issue
- 1
- Pages
- 19-27
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- PMC
- PMC1317641
- OpenAlex
- W2149800308
- Cited by
- 39
- References
- 3
- Citations by year
- 2025: 2 · 2021: 2 · 2019: 1 · 2018: 3 · 2017: 1 · 2016: 2 · 2015: 2 · 2014: 4 · 2013: 1 · 2012: 2
- FWCI
- 0.91
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Molecular and Cellular Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Université Catholique de Louvain
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Axon Guidance and Neuronal Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
- Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
- Keywords
- ApoER2, VLDL receptor, lipid rafts, fibroblast cell lines, receptor localization, neuronal migration, brain development
- MeSH terms
- Reelin Protein, Animals, Fibroblasts, Nerve Tissue Proteins, Phosphorylation, Receptors, LDL, Serine Endopeptidases, Signal Transduction, Cell Adhesion Molecules, Neuronal, Extracellular Matrix Proteins, Receptors, Lipoprotein, Membrane Microdomains, LDL-Receptor Related Proteins, NIH 3T3 Cells, Mice
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
