DAB1 and Reelin effects on amyloid precursor protein and ApoE receptor 2 trafficking and processing
Open accessAbstract
Numerous cytoplasmic adaptor proteins, including JIP1, FE65, and X11alpha, affect amyloid precursor protein (APP) processing and Abeta production. Dab1 is another adaptor protein that interacts with APP as well as with members of the apoE receptor family. We examined the effect of Dab1 on APP and apoEr2 processing in transfected cells and primary neurons. Dab1 interacted with APP and apoEr2 and increased levels of their secreted extracellular domains and their cytoplasmic C-terminal fragments. These effects depended on the NPXY domains of APP and apoEr2 and on the phosphotyrosine binding domain of Dab1 but did not depend on phosphorylation of Dab1. Dab1 decreased the levels of APP beta-C-terminal fragment and secreted Abeta. Full-length Dab1 or its phosphotyrosine binding domain alone increased surface levels of APP, as determined by surface protein biotinylation and live cell staining. A ligand for apoEr2, the extracellular matrix protein Reelin, significantly increased the interaction of apoEr2 with Dab1. Surprisingly, we also found that Reelin treatment significantly increased the interaction of APP and Dab1. Moreover, Reelin treatment increased cleavage of APP and apoEr2 and decreased production of the beta-C-terminal fragment of APP and Abeta. Together, these data suggest that Dab1 alters trafficking and processing of APP and apoEr2, and this effect is influenced by extracellular ligands.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
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?
Reelin induces ApoER2 processing and degradation.
“There is also evidence showing that reelin induces ApoER2 processing [42], [43] and degradation [43], however the mechanisms by which this is accomplished by reelin is not completely clear.”
From Sorting nexin 17 regulates ApoER2 recycling and reelin signaling (2014) · cites this paper as [42]
ApoER2 trafficking is related to its susceptibility to proteolytic processing by α-secretases of the ADAM family and by the γ-secretase complex.
“Several lines of evidence relate ApoER2 trafficking with its susceptibility to proteolytic processing by the α-secretases of the ADAM family and by the γ-secretase complex [39], [42], [55], [57].”
From Sorting nexin 17 regulates ApoER2 recycling and reelin signaling (2014) · cites this paper as [42]
Some adaptor proteins regulate the proteolytic processing of ApoER2 by binding to its NPxY motif.
“Interestingly, some of these proteins also regulate the proteolytic processing of this receptor [42], [54], [55], [66] by binding to its NPxY motif.”
From Sorting nexin 17 regulates ApoER2 recycling and reelin signaling (2014) · cites this paper as [42]
Reduced Reelin expression in HRM mice exacerbates the accumulation of both Aβ and phosphorylated tau, whose production is inhibited by Reelin signaling.
“Reduced Reelin expression in HRM mice exacerbates the accumulation of both A and phosphorylated tau (94), whose production is inhibited by Reelin signaling (Ref.76 and reviewed in Ref. 31).”
From Reelin: Neurodevelopmental Architect and Homeostatic Regulator of Excitatory Synapses (2017) · cites this paper as [76]
Cites
A protein related to extracellular matrix proteins deleted in the mouse mutant reeler
D'Arcangelo, G., G. Miao, G., Chen, S.-C., Scares, H. D., Morgan, J. I., & Curran, T. (1995) · Nature · doi:10.1038/374719a0 · Cited by 1,748 · see citing works
Trommsdorff, M., Gotthardt, M., Hiesberger, T., Shelton, J., Stockinger, W., Nimpf, J., Hammer, R. E., Richardson, J. A., & Herz, J. (1999) · Cell · doi:10.1016/s0092-8674(00)80782-5 · Cited by 1,261 · see citing works
A Transcriptively Active Complex of APP with Fe65 and Histone Acetyltransferase Tip60
Cao, X., & Südhof, T. C. (2001) · Science · doi:10.1126/science.1058783 · Cited by 1,202 · see citing works
Reelin Is a Ligand for Lipoprotein Receptors
D'Arcangelo, G., Homayouni, R., Keshvara, L., Rice, D. S., Sheldon, M., & Curran, T. (1999) · Neuron · doi:10.1016/s0896-6273(00)80860-0 · Cited by 808 · see citing works
Reelin-induced tryosine phosphorylation of Disabled 1 during neuronal positioning
Howell, B. W., Herrick, T. M., & Cooper, J. A. (1999) · Genes & Development · doi:10.1101/gad.13.6.643 · Cited by 411 · see citing works
Self-citationHowell, B. W., Lanier, L. M., Frank, R., Gertler, F. B., & Cooper, J. A. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.7.5179 · Cited by 371 · see citing works
Self-citationHerms, J. W., Anliker, B., Heber, S., Ring, S., Fuhrmann, M., Kretzschmar, H. A., Sisodia, S. S., & Müller, U. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600390 · Cited by 338 · see citing works
Ando, K., Iijima, K., Elliott, J. I., Kirino, Y., & Suzuki, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104059200 · Cited by 261 · see citing works
Ho, A., & Südhof, T. C. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308655100 · Cited by 224 · see citing works
Pietrzik, C. U., Yoon, I., Jaeger, S., Busse, T., Weggen, S., & Koo, E. H. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.5451-03.2004 · Cited by 220 · see citing works
Bock, H. H., Jossin, Y., Liu, P., Förster, E., May, P., Goffinet, A. M., & Herz, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306416200 · Cited by 213 · see citing works
Regulation of β-Amyloid Secretion by FE65, an Amyloid Protein Precursor-binding Protein
Sabo, S. L., Lanier, L. M., Ikin, A. F., Khorkova, O., Sahasrabudhe, S. R., Greengard, P., & Buxbaum, J. D. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.12.7952 · Cited by 209 · see citing works
Disabled-1 Binds to the Cytoplasmic Domain of Amyloid Precursor-Like Protein 1
Homayouni, R., Rice, D. S., Sheldon, M., & Curran, T. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-17-07507.1999 · Cited by 184 · see citing works
Regulation of Protein Tyrosine Kinase Signaling by Substrate Degradation during Brain Development
Arnaud, L., Ballif, B. A., & Cooper, J. A. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.24.9293-9302.2003 · Cited by 164 · see citing works
King, G. D., & Turner, R. S. (2004) · Experimental Neurology · doi:10.1016/j.expneurol.2003.10.011 · Cited by 149 · see citing works
Essential roles for the FE65 amyloid precursor protein‐interacting proteins in brain development
Guénette, S. Y., Chang, Y., Hiesberger, T., Richardson, J. A., Eckman, C. B., Eckman, E. A., Hammer, R. E., & Herz, J. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7600926 · Cited by 148 · see citing works
Crystal Structures of the Dab Homology Domains of Mouse Disabled 1 and 2
Yun, M., Keshvara, L. M., Park, C., Zhang, Y.-M., Dickerson, J. B., Zheng, J., Rock, C. O., Curran, T., & Park, H.-W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304384200 · Cited by 129 · see citing works
Hoe, H.-S., Wessner, D., Beffert, U., Becker, A. G., Matsuoka, Y., & Rebeck, G. W. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.21.9259-9268.2005 · Cited by 122 · see citing works
Self-citationStolt, P. C., Jeon, H., Song, H. K., Herz, J., Eck, M. J., & Blacklow, S. C. (2003) · Structure · doi:10.1016/s0969-2126(03)00068-6 · Cited by 117 · see citing works
Bressler, S. (1996) · Human Molecular Genetics · doi:10.1093/hmg/5.10.1589 · Cited by 117 · see citing works
Ho, A., Morishita, W., Hammer, R. E., Malenka, R. C., & Südhof, T. C. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252774899 · Cited by 96 · see citing works
Development of A$beta; terminal end-specific antibodies and sensitive ELISA for A$beta; variant
Horikoshi, Y., Sakaguchi, G., Becker, A. G., Gray, A. J., Duff, K., Aisen, P. S. S., Yamaguchi, H., Maeda, M., Kinoshita, N., & Matsuoka, Y. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.05.051 · Cited by 89 · see citing works
Self-citationPramatarova, A., Ochalski, P. G., Chen, K., Gropman, A. L., Myers, S., Min, K., & Howell, B. W. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.20.7210-7221.2003 · Cited by 88 · see citing works
Self-citationQiu, Z., Crutcher, K. A., Hyman, B. T., & Rebeck, G. W. (2003) · Neuroscience · doi:10.1016/j.neuroscience.2003.08.017 · Cited by 86 · see citing works
Self-citationRegulation of ApoE receptor proteolysis by ligand binding
Hoe, H.-S., & Rebeck, G. W. (2005) · Molecular Brain Research · doi:10.1016/j.molbrainres.2005.02.013 · Cited by 85 · see citing works
Self-citationTaru, H., Kirino, Y., & Suzuki, T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203713200 · Cited by 85 · see citing works
Disabled1 Regulates the Intracellular Trafficking of Reelin Receptors
Morimura, T., Hattori, M., Ogawa, M., & Mikoshiba, K. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m409048200 · Cited by 82 · see citing works
Chang, Y., Tesco, G., Jeong, W. J., Lindsley, L., Eckman, E. A., Eckman, C. B., Tanzi, R. E., & Guénette, S. Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m309561200 · Cited by 80 · see citing works
FE65 interaction with the ApoE receptor ApoEr2
Hoe, H.-S., Magill, L. A., Guenette, S., Fu, Z., Vicini, S., & Rebeck, G. W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600728200 · Cited by 69 · see citing works
Self-citationLee, J., Lau, K., Perkinton, M. S., Standen, C. L., Rogelj, B., Falinska, A. M., McLoughlin, D. M., & Miller, C. C. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405602200 · Cited by 69 · see citing works
Modulation of Amyloid Precursor Protein Metabolism by X11α/Mint-1
Mueller, H. T., Borg, J., Margolis, B. L., & Turner, R. S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m008453200 · Cited by 60 · see citing works
Guénette, S. Y., Chang, Y., Hyman, B. T., Tanzi, R. E., & Rebeck, G. W. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01009.x · Cited by 24 · see citing works
Self-citationHerrick, T. M., & Cooper, J. A. (2004) · Molecular Brain Research · doi:10.1016/j.molbrainres.2004.03.022 · Cited by 19 · see citing works
The Reelin Signaling Pathway in Mouse Cortical Development
Bar, I., de Rouvroit, C. L., & Goffinet, A. M. (2000) · European Journal of Morphology · doi:10.1076/ejom.38.5.321.7361 · Cited by 19 · see citing works
Flagged first, then by citations
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
Young-Pearse, T. L., Bai, J., Chang, R., Zheng, J. B., LoTurco, J. J., & Selkoe, D. J. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4701-07.2007 · Cited by 369 · see citing works
Substrate specificity of γ-secretase and other intramembrane proteases
Beel, A. J., & Sanders, C. R. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-7462-2 · Cited by 270 · see citing works
The Reelin signaling pathway promotes dendritic spine development in hippocampal neurons
Niu, S., Yabut, O., & D'Arcangelo, G. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.1917-08.2008 · Cited by 266 · see citing works
Interaction of Reelin with Amyloid Precursor Protein Promotes Neurite Outgrowth
Hoe, H.-S., Lee, K. J., Carney, R. S. E., Lee, J., Markova, A., Lee, J.-Y., Howell, B. W., Hyman, B. T., Pak, D. T. S., Bu, G., et al. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.4872-08.2009 · Cited by 219 · see citing works
Self-citationInteraction between Reelin and Notch Signaling Regulates Neuronal Migration in the Cerebral Cortex
Hashimoto‐Torii, K., Torii, M., Sarkisian, M. R., Bartley, C. M., Shen, J., Radtke, F., Gridley, T., Šestan, N., & RAKIC, P. T. (2008) · Neuron · doi:10.1016/j.neuron.2008.09.026 · Cited by 216 · see citing works
The brain interstitial system: Anatomy, modeling, in vivo measurement, and applications
Lei, Y., Han, H., Yuan, F., Javeed, A., & Zhao, Y. L. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.12.007 · Cited by 215 · see citing works
Jossin, Y. (2020) · Biomolecules · doi:10.3390/biom10060964 · Cited by 208 · see citing works
Transcriptomic and genetic studies identify IL-33 as a candidate gene for Alzheimer's disease
Chapuis, J., Hot, D., Hansmannel, F., Kerdraon, O., Ferreira, S., Hubans, C., Maurage, C. A., Huot, L., Bensemain, F., Laumet, G., et al. (2009) · Molecular Psychiatry · doi:10.1038/mp.2009.10 · Cited by 201 · see citing works
ROCK and Rho: Biochemistry and Neuronal Functions of Rho-Associated Protein Kinases
Schmandke, A., Schmandke, A., & Strittmatter, S. M. (2007) · The Neuroscientist · doi:10.1177/1073858407303611 · Cited by 170 · see citing works
Lee, J., Retamal, C., Cuitiño, L., Caruano-Yzermans, A., Shin, J.-E., van Kerkhof, P., Marzolo, M.-P., & Bu, G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800642200 · Cited by 162 · see citing works
Trafficking regulation of proteins in Alzheimer’s disease
Jiang, S., Li, Y., Zhang, X., Bu, G.-J., Xu, H.-X., & Zhang, Y.-W. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-6 · Cited by 153 · see citing works
Physiology and pharmacology of amyloid precursor protein
Cho, Y., Bae, H., Okun, E., Arumugam, T. V., & Jo, D. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2022.108122 · Cited by 145 · see citing works
Amyloid precursor protein and its homologues: a family of proteolysis-dependent receptors
Jacobsen, K. T., & Iverfeldt, K. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0020-8 · Cited by 139 · see citing works
Kocherhans, S., Madhusudan, A., Doehner, J., Breu, K. S., Nitsch, R. M., Fritschy, J.-M., & Knuesel, I. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.0418-10.2010 · Cited by 132 · see citing works
Lee, K. J., Moussa, C., Lee, Y. J., Sung, Y., Howell, B. W., Turner, R. S., Pak, D. T. S., & Hoe, H.-S. (2010) · Neuroscience · doi:10.1016/j.neuroscience.2010.04.078 · Cited by 133 · see citing works
Self-citationEmerging topics in Reelin function
Förster, E., Bock, H. H., Herz, J., Chai, X., Frotscher, M., & Zhao, S. (2010) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2010.07222.x · Cited by 130 · see citing works
Pujadas, L., Rossi, D., Andrés, R., Teixeira, C. M., Serra-Vidal, B., Parcerisas, A., Maldonado, R., Giralt, E., Carulla, N., & Soriano, E. (2014) · Nature Communications · doi:10.1038/ncomms4443 · Cited by 129 · see citing works
Urbanus, R. T., Pennings, M. T. T., Derksen, R. H. W. M., & de Groot, P. G. (2008) · Journal of Thrombosis and Haemostasis · doi:10.1111/j.1538-7836.2008.03021.x · Cited by 129 · see citing works
Marzolo, M.-P., & Bu, G. (2009) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2008.10.005 · Cited by 122 · see citing works
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 · see citing works
Reelin: Neurodevelopmental Architect and Homeostatic Regulator of Excitatory Synapses
Wasser, C. R., & Herz, J. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.r116.766782 · Cited by 111 · see citing works
APP Receptor? To Be or Not To Be
Deyts, C., Thinakaran, G., & Parent, A. (2016) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2016.01.005 · Cited by 109 · see citing works
He, X., Cooley, K., Chung, C. H. Y., Dashti, N., & Tang, J. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.3993-06.2007 · Cited by 107 · see citing works
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 · see citing works
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 · see citing works
Single-Cell Detection of Secreted Aβ and sAPPα from Human IPSC-Derived Neurons and Astrocytes
Liao, M.-C., Muratore, C., Gierahn, T. M., Sullivan, S. E., Srikanth, P., Jager, P. L. D., Love, J. C., & Young‐Pearse, T. L. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.2735-15.2016 · Cited by 96 · see citing works
Age-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 · see citing works
The ApoE receptors Vldlr and Apoer2 in central nervous system function and disease
Lane-Donovan, C., & Herz, J. (2017) · Journal of Lipid Research · doi:10.1194/jlr.r075507 · Cited by 94 · see citing works
Neural ECM molecules in synaptic plasticity, learning, and memory
Senkov, O., Anđjus, P. R., Radenović, L., Soriano, E., & Dityatev, A. E. (2014) · Progress in brain research · doi:10.1016/b978-0-444-63486-3.00003-7 · Cited by 94 · see citing works
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 · see citing works
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 · see citing works
Hoe, H.-S., Cooper, M. J., Burns, M. P., Lewis, P. A., van der Brug, M., Chakraborty, G., Cartagena, C. M., Pak, D. T. S., Cookson, M. R., & Rebeck, G. W. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.3135-07.2007 · Cited by 90 · see citing works
Self-citationExercise during pregnancy mitigates Alzheimer‐like pathology in mouse offspring
Herring, A., Donath, A., Yarmolenko, M., Uslar, E., Conzen, C., Kanakis, D. N., Bosma, C., Worm, K., Paulus, W., & Keyvani, K. (2011) · The FASEB Journal · doi:10.1096/fj.11-193193 · Cited by 92 · see citing works
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 · see citing works
Krstic, D., Rodríguez, M. E., & Knuesel, I. (2012) · PLoS ONE · doi:10.1371/journal.pone.0047793 · Cited by 92 · see citing works
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 · see citing works
Reelin signaling in development, maintenance, and plasticity of neural networks
Stranahan, A. M., Erion, J., & Wosiski‐Kuhn, M. (2013) · Ageing Research Reviews · doi:10.1016/j.arr.2013.01.005 · Cited by 90 · see citing works
Rogers, J. T., Zhao, L., Trotter, J. H., Rusiana, I., Peters, M. M., Li, Q., Donaldson, E., Banko, J. L., Keenoy, K. E., Rebeck, G. W., et al. (2012) · Journal of Psychopharmacology · doi:10.1177/0269881112463468 · Cited by 87 · see citing works
Self-citationECM in brain aging and dementia
Morawski, M., Filippov, M., Tzinia, A., Tsilibary, E., & Vargova, L. (2014) · Progress in Brain Research · doi:10.1016/b978-0-444-63486-3.00010-4 · Cited by 84 · see citing works
Hoe, H., Lee, H., & Pak, D. T. S. (2010) · CNS Neuroscience & Therapeutics · doi:10.1111/j.1755-5949.2010.00221.x · Cited by 84 · see citing works
Self-citationNeuronal protein trafficking associated with Alzheimer disease
Tang, B. L. (2009) · Cell Adhesion & Migration · doi:10.4161/cam.3.1.7254 · Cited by 83 · see citing works
Joshi, P., Liang, J. O., DiMonte, K., Sullivan, J., & Pimplikar, S. W. (2009) · Developmental Biology · doi:10.1016/j.ydbio.2009.07.041 · Cited by 82 · see citing works
Wolfe, M. S., & Guénette, S. Y. (2007) · Journal of Cell Science · doi:10.1242/jcs.03481 · Cited by 77 · see citing works
HIV-1 Tat Interacts with and Regulates the Localization and Processing of Amyloid Precursor Protein
Kim, J., Yoon, J., & Kim, Y.-S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0077972 · Cited by 74 · see citing works
Linking pathways in the developing and aging brain with neurodegeneration
Kovács, G. G., Adle‐Biassette, H., Milenković, I., Cipriani, S., van Scheppingen, J., & Aronica, E. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2014.03.045 · Cited by 67 · see citing works
Cousins, S. L., Hoey, S. E., Stephenson, F. A., & Perkinton, M. S. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06424.x · Cited by 68 · see citing works
Pancortins interact with amyloid precursor protein and modulate cortical cell migration
Rice, H. C., Townsend, M., Bai, J., Suth, S., Cavanaugh, W., Selkoe, D. J., & Young‐Pearse, T. L. (2012) · Development · doi:10.1242/dev.082909 · Cited by 66 · see citing works
β-amyloid controls altered Reelin expression and processing in Alzheimer's disease
Botella-López, A., Cuchillo‐Ibáñez, I., Cotrufo, T., Mok, S. S., Li, Q., Jiménez, M. S. B., Dierssen, M., Soriano, E., & Sáez‐Valero, J. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.12.006 · Cited by 64 · see citing works
Magnesium Modulates Amyloid-β Protein Precursor Trafficking and Processing
Yu, J. H., Sun, M., Chen, Z., Lu, J., Liu, Y., Zhou, L., Xu, X., Fan, D., & Chui, D. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-091444 · Cited by 61 · see citing works
Contribution of GABAergic interneurons to amyloid-β plaque pathology in an APP knock-in mouse model
Rice, H. C., Marcassa, G., Chrysidou, I., Horré, K., Young‐Pearse, T. L., Müller, U., Saito, T., Saido, T. C., Vassar, R. J., de Wit, J., et al. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0356-y · Cited by 51 · see citing works
Impaired migration signaling in the hippocampus following prenatal hypoxia
Golan, M. H., Mane, R., Molczadzki, G., Zuckerman, M., Kaplan-Louson, V., Huleihel, M., & Perez-Polo, J. R. (2009) · Neuropharmacology · doi:10.1016/j.neuropharm.2009.07.028 · Cited by 52 · see citing works
Rice, H. C., Young‐Pearse, T. L., & Selkoe, D. J. (2013) · Biochemistry · doi:10.1021/bi400165f · Cited by 51 · see citing works
Fyn Modulation of Dab1 Effects on Amyloid Precursor Protein and ApoE Receptor 2 Processing
Hoe, H., Minami, S., Makarova, A., Lee, J., Hyman, B. T., Matsuoka, Y., & Rebeck, G. W. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704140200 · Cited by 49 · see citing works
Self-citationBignante, E. A., Heredia, F., Morfini, G. A., & Lorenzo, A. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.04.021 · Cited by 46 · see citing works
Sorting 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 · see citing works
The β-amyloid peptide compromises Reelin signaling in Alzheimer’s disease
Cuchillo‐Ibáñez, I., Mata‐Balaguer, T., Balmaceda, V., Arranz, J. J., Nimpf, J., & Sáez‐Valero, J. (2016) · Scientific Reports · doi:10.1038/srep31646 · Cited by 47 · see citing works
The Role of Reelin Signaling in Alzheimer’s Disease
Yu, N., Tan, M., Yu, J., Xie, A., & Tan, L. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9459-9 · Cited by 44 · see citing works
Mantuano, E., Lam, M. S., Shibayama, M., Campana, W. M., & Gonias, S. L. (2015) · Journal of Cell Science · doi:10.1242/jcs.173765 · Cited by 45 · see citing works
Platelets express three different splice variants of ApoER2 that are all involved in signaling
Pennings, M. T. T., Derksen, R. H. W. M., Urbanus, R. T., Tekelenburg, W. L. H., Hemrika, W., & de Groot, P. G. (2007) · Journal of Thrombosis and Haemostasis · doi:10.1111/j.1538-7836.2007.02605.x · Cited by 44 · see citing works
Sex Differences in Alzheimer’s Disease: Where Do We Stand?
Medeiros, A. D. M., & Silva, R. H. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-180213 · Cited by 42 · see citing works
Reelin Signaling in Neurodevelopmental Disorders and Neurodegenerative Diseases
Joly‐Amado, A., Kulkarni, N., & Nash, K. R. (2023) · Brain Sciences · doi:10.3390/brainsci13101479 · Cited by 43 · see citing works
Reelin links Apolipoprotein E4, Tau, and Amyloid‐β in Alzheimer’s disease
Yi, L. X., Zeng, L., Wang, Q., Tan, E. K., & Zhou, Z. D. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102339 · Cited by 41 · see citing works
Functional interactions of APP with the apoE receptor family
Hoe, H., & Rebeck, G. W. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05517.x · Cited by 41 · 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
Adapting for endocytosis: roles for endocytic sorting adaptors in directing neural development
Yap, C. C., & Winckler, B. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00119 · Cited by 38 · see citing works
Intracellular cholesterol homeostasis and amyloid precursor protein processing
Burns, M. P., & Rebeck, G. W. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2010.03.004 · Cited by 39 · see citing works
Self-citationAPP Protein Family Signaling at the Synapse: Insights from Intracellular APP-Binding Proteins
Guénette, S. Y., Strecker, P., & Kins, S. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00087 · Cited by 39 · see citing works
A genetic interaction between the APP and Dab1 genes influences brain development
Pramatarova, A., Chen, K., & Howell, B. W. (2007) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2007.09.008 · Cited by 38 · see citing works
Self-citationLammert, D. B., Middleton, F. A., Pan, J. Q., Olson, E. C., & Howell, B. W. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.14045 · Cited by 36 · see citing works
Self-citationBracher-Smith, M., Leonenko, G., Baker, E., Crawford, K., Graham, A. C., Salih, D. A., Howell, B. W., Hardy, J., & Escott-Price, V. (2022) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2022.07.009 · Cited by 31 · see citing works
Self-citationReelin proteolysis affects signaling related to normal synapse function and neurodegeneration
Lussier, A. L., Weeber, E. J., & Rebeck, G. W. (2016) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2016.00075 · Cited by 31 · see citing works
Self-citationDecisive role of Reelin signaling during early stages of Alzheimer’s disease
Krstic, D., Pfister, S., Notter, T., & Knuesel, I. (2013) · Neuroscience · doi:10.1016/j.neuroscience.2013.04.042 · Cited by 33 · see citing works
Hunter, S., & Brayne, C. (2012) · Alzheimer s Research & Therapy · doi:10.1186/alzrt108 · Cited by 31 · see citing works
Disabled‐1 is a large common fragile site gene, inactivated in multiple cancers
McAvoy, S., Zhu, Y., Perez, D. S., James, C. D., & Smith, D. I. (2007) · Genes Chromosomes and Cancer · doi:10.1002/gcc.20519 · Cited by 32 · see citing works
Reelin-mediated Signaling during Normal and Pathological Forms of Aging.
Doehner, J., & Knuesel, I. (2010) · Europe PMC (PubMed Central) · Cited by 31 · see citing works
The role of lipoprotein receptors on the physiological function of APP
Wagner, T., & Pietrzik, C. U. (2011) · Experimental Brain Research · doi:10.1007/s00221-011-2876-8 · Cited by 31 · see citing works
Britto, J. M., Tait, K. J., Johnston, L. A., Hammond, V. E., Kalloniatis, M., & Tan, S. (2010) · Cerebral Cortex · doi:10.1093/cercor/bhq168 · Cited by 31 · see citing works
Manucat-Tan, N. B., Saadipour, K., Wang, Y., Bobrovskaya, L., & Zhou, X. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1106-9 · Cited by 29 · see citing works
Trafficking in neurons: Searching for new targets for Alzheimer's disease future therapies
Musardo, S., Saraceno, C., Pelucchi, S., & Marcello, E. E. (2013) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2013.07.019 · Cited by 29 · see citing works
Pasten, C., Cerda, J., Jausoro, I., Court, F. A., Cáceres, A., & Marzolo, M.-P. (2015) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2015.09.004 · Cited by 29 · see citing works
Mata‐Balaguer, T., Cuchillo‐Ibáñez, I., Calero, M., Ferrer, I., & Sáez‐Valero, J. (2018) · The FASEB Journal · doi:10.1096/fj.201700736rr · Cited by 28 · see citing works
Minami, 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
Self-citationBórquez, D. A., & González-Billault, C. E. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/353145 · Cited by 28 · see citing works
Opposite Epigenetic Associations With Alcohol Use and Exercise Intervention
Chen, J., Hutchison, K. E., Bryan, A. D., Filbey, F. M., Calhoun, V. D., Claus, E. D., Lin, D., Jing Sui (Beijing Normal University), my correct affiliation is beijing normal university, N. Q. U. O. S. A. T., Du, Y., & Liu, J. (2018) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2018.00594 · Cited by 28 · see citing works
Kondo, T., Hara, N., Koyama, S., Yada, Y., Tsukita, K., Nagahashi, A., Ikeuchi, T., Ishii, K., Asada, T., Arai, T., et al. (2022) · Nature Aging · doi:10.1038/s43587-021-00158-9 · Cited by 26 · see citing works
Madhusudan, A., Sidler, C., & Knuesel, I. (2009) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2009.06884.x · Cited by 28 · see citing works
Gao, H., Yu, T., He, Q., Song, F., & Saffen, D. W. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.05.044 · Cited by 27 · see citing works
Volloch, V., & Rits‐Volloch, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241512246 · Cited by 28 · see citing works
Minami, S., Hoe, H., & Rebeck, G. W. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07296.x · Cited by 24 · see citing works
Self-citationLigand-induced Homotypic and Heterotypic Clustering of Apolipoprotein E Receptor 2
Divekar, S. D., Burrell, T. C., Lee, J. E., Weeber, E. J., & Rebeck, G. W. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.537548 · Cited by 22 · see citing works
Self-citationMedoro, A., Bartollino, S., Mignogna, D., Passarella, D., Porcile, C., Pagano, A., Florio, T., Nizzari, M., Guerra, G., Marco, R. D., et al. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170628 · Cited by 24 · see citing works
Matrone, C. (2013) · BioEssays · doi:10.1002/bies.201300041 · Cited by 24 · see citing works
Insulysin Cleaves the APP Cytoplasmic Fragment at Multiple Sites
Venugopal, C., Pappolla, M. A., & Sambamurti, K. (2007) · Neurochemical Research · doi:10.1007/s11064-007-9449-z · Cited by 24 · see citing works
Regulated Proteolysis of APP and ApoE Receptors
Hoe, H., & Rebeck, G. W. (2008) · Molecular Neurobiology · doi:10.1007/s12035-008-8017-0 · Cited by 23 · see citing works
Self-citationBeyer, A.-S., von Einem, B., Schwanzar, D., Kammerl, I. E., Hellrung, A., Thal, D. R., Ingelsson, M., Makarova, A., Deng, M., Chhabra, E. S., et al. (2010) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.06.006 · Cited by 23 · see citing works
The Effects of Alpha Boswellic Acid on Reelin Expression and Tau Phosphorylation in Human Astrocytes
Fathi, E., Katouli, F. H., Riazi, G. H., Shasaltaneh, M. D., Parandavar, E., Bayati, S., Afrasiabi, A., & Nazari, R. (2016) · NeuroMolecular Medicine · doi:10.1007/s12017-016-8437-3 · Cited by 24 · see citing works
APP involvement in retinogenesis of mice
Dinet, V., An, N., Ciccotosto, G. D., Bruban, J., Maoui, A., Bellingham, S. A., Hill, A. F., Andersen, O. M., Nykjær, A., Jonet, L., et al. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0762-2 · Cited by 21 · see citing works
Regulation of the Physiological Function and Metabolism of AβPP by AβPP Binding Proteins
Taru, H., & Suzuki, T. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1148 · Cited by 20 · see citing works
Novel D isabled‐1‐expressing neurons identified in adult brain and spinal cord
Abadesco, A. D., Cilluffo, M. C., Yvone, G. M., Carpenter, E. M., Howell, B. W., & Phelps, P. E. (2013) · European Journal of Neuroscience · doi:10.1111/ejn.12416 · Cited by 20 · see citing works
Self-citation
- Authors
- Hoe, H.-S., Tran, T. S., Matsuoka, Y., Howell, B. W., & Rebeck, G. W.
- Affiliations
- Georgetown University Medical Center (US)
- National Institutes of Health (US)
- Corresponding author
- Rebeck, G. William
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2006-11
- Volume
- 281
- Issue
- 46
- Pages
- 35176-35185
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2058881577
- Cited by
- 174
- References
- 34
- Citations by year
- 2026: 4 · 2025: 6 · 2024: 7 · 2023: 7 · 2022: 5 · 2021: 5 · 2020: 3 · 2019: 1 · 2018: 6 · 2017: 9 · 2016: 13 · 2015: 8 · 2014: 12 · 2013: 14 · 2012: 12
- FWCI
- 9.13
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institute on Aging (R01AG014473, K01AG022455)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- Dab1, reelin, amyloid precursor protein, APP processing, amyloid-beta, adaptor proteins, NPXY motif, phosphotyrosine binding domain, protein trafficking, extracellular matrix ligands, neurons
- MeSH terms
- Reelin Protein, Animals, Cell Line, Chlorocebus aethiops, Gene Expression Regulation, Humans, Nerve Tissue Proteins, Phosphorylation, Serine Endopeptidases, Cell Adhesion Molecules, Neuronal, Extracellular Matrix Proteins, Amyloid beta-Protein Precursor, Receptors, Lipoprotein, Protein Transport, LDL-Receptor Related Proteins, Adaptor Proteins, Signal Transducing
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