The reelin receptor ApoER2 recruits JNK-interacting proteins-1 and -2
Open accessAbstract
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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JIP1/2 interact with ApoER2.
“It has previously been reported that c-jun-terminal kinase interacting proteins 1/2 (JIP1/2) interact with ApoER2 (Stockinger et al., 2000) as well as Tiam1 (Buchsbaum et al., 2002), the major Rac guanine nucleotide exchange factor that couples the NMDAR to Rac1 (Tolias et al., 2005).”
From The E3 ubiquitin ligase IDOL regulates synaptic ApoER2 levels and is important for plasticity and learning (2017) · cites this paper as Stockinger et al., 2000
Postsynaptic JIP and Tiam1 could be involved in mediating the effects of IDOL-ApoER2 axis on Rac1 activity.
“Our data suggest that postsynaptic JIP (Stockinger et al., 2000; Verhey et al., 2001) and Tiam1 (Buchsbaum et al., 2002) could be involved in mediating the effects of IDOL-ApoER2 axis on Rac1 activity.”
From The E3 ubiquitin ligase IDOL regulates synaptic ApoER2 levels and is important for plasticity and learning (2017) · cites this paper as Stockinger et al., 2000
JIP-1 and JIP-2 interact with rhoGEF and with the cell surface receptor for Reelin, ApoER2.
“JIP-1 and JIP-2 have additionally been found to interact with rhoGEF (Meyer et al. 1999) and with the cell surface receptor for Reelin, ApoER2 (Stockinger et al. 2000).”
From Cargo of kinesin identified as JIP scaffolding proteins and associated signaling molecules (2001) · cites this paper as Stockinger et al. 2000
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Low-Density Lipoprotein Receptor Family
Bu, G., Li, Y., & Cam, J. A. (2001) · Molecular Neurobiology · doi:10.1385/mn:23:1:53 · Cited by 157 · see citing works
“The interaction with JIPs is specific for apoER2, since neither the LDLR nor the VLDLR bind to these adaptor proteins (34).”
BackgroundLiu, C.-X., Li, Y., Obermoeller, L. M., Schwartz, A. L., & Bu, G. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102727200 · Cited by 155 · see citing works
Functions of lipoprotein receptors in neurons
Beffert, U., Stolt-Bergner, P. C., & Herz, J. (2004) · Journal of Lipid Research · doi:10.1194/jlr.r300017-jlr200 · Cited by 156 · see citing works
“with the cytoplasmic domains of both apoER2 (40, 41)”
BackgroundMOUSE MODEL OF SUBRETINAL NEOVASCULARIZATION WITH CHOROIDAL ANASTOMOSIS
Heckenlively, J. R., Hawes, N. L., Friedlander, M., Nusinowitz, S., Hurd, R. E., Davisson, M. T., & Chang, B. (2003) · Retina · doi:10.1097/00006982-200308000-00012 · Cited by 151 · see citing works
LRP1 modulates the microglial immune response via regulation of JNK and NF-κB signaling pathways
Yang, L., Liu, C., Zheng, H., Kanekiyo, T., Atagi, Y., Jia, L., Wang, D., N’Songo, A., Can, D., Xu, H., et al. (2016) · Journal of Neuroinflammation · doi:10.1186/s12974-016-0772-7 · Cited by 154 · see citing works
“Interestingly, the cytoplasmic domain of LRP1 (LRP1-ICD) binds JNK-interacting proteins (JIP-1 and JIP-2), which have been identified as modulators of the JNK signal transduction pathway [53].”
BackgroundThe Genetics of Axonal Transport and Axonal Transport Disorders
Duncan, J. E., & Goldstein, L. S. B. (2006) · PLoS Genetics · doi:10.1371/journal.pgen.0020124 · Cited by 150 · see citing works
Calsyntenin-1 Docks Vesicular Cargo to Kinesin-1
Konecna, A., Frischknecht, R., Kinter, J., Ludwig, A., Steuble, M., Meskenaïte, V., Indermühle, M., Engel, M., Cen, C., Mateos, J. M., et al. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-02-0112 · Cited by 148 · see citing works
“Several motor protein receptors and adaptors have been identified, including the integral membrane proteins ApoER2 (Stockinger et al., 2000), the -amyloid precursor protein (APP; Kamal et al.”
InfluentialCarter, C. J. (2006) · Neurochemistry International · doi:10.1016/j.neuint.2006.07.007 · Cited by 148 · see citing works
“The protein expression of LRP1 is increased in the frontal cortex (Qiu et al., 2001) and the receptor is also associated with amyloid plaques (Arelin et al., 2002) as is VLDLR (Vassar et al., 1999).”
InfluentialFatemi, S. H. (2001) · Molecular Psychiatry · doi:10.1038/sj.mp.4000129 · Cited by 151 · see citing works
Altered levels of Reelin and its isoforms in schizophrenia and mood disorders
Fatemi, S. H., Kroll, J., & Stary, J. M. (2001) · Neuroreport · doi:10.1097/00001756-200110290-00014 · Cited by 149 · see citing works
Differential glycosylation regulates processing of lipoprotein receptors by γ-secretase
May, P., Bock, H. H., Nimpf, J., & Herz, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305858200 · Cited by 142 · see citing works
Lindwall, C., & Kanje, M. (2005) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2005.03.002 · Cited by 144 · see citing works
LDL receptor relatives at the crossroad of endocytosis and signaling
Schneider, W. J., & Nimpf, J. (2003) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-003-2183-z · Cited by 141 · see citing works
Hoffman, P. N. (2009) · Experimental Neurology · doi:10.1016/j.expneurol.2009.09.006 · Cited by 138 · see citing works
“JIP1 also links kinesin-1 to vesicles whose membranes contain amyloid precursor protein (APP) or apolipoprotein E receptor 2 (ApoER2) (Stockinger et al., 2000; Muresan and Muresan, 2005).”
BackgroundMolecular mechanisms of lipoprotein receptor signalling
May, P., Herz, J., & Bock, H. H. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5231-z · Cited by 138 · see citing works
Smooth, rough and upside-down neocortical development
Olson, E. C., & Walsh, C. A. (2002) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(02)00305-2 · Cited by 134 · see citing works
LRP in Amyloid‐β Production and Metabolism
Bu, G., Cam, J. A., & Zerbinatti, C. (2006) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1377.005 · Cited by 133 · see citing works
Hinrich, A. J., Jodelka, F. M., Chang, J. L., Brutman, D., Bruno, A. M., Briggs, C. A., James, B. D., Stutzmann, G. E., Bennett, D. A., Miller, S. A., et al. (2016) · EMBO Molecular Medicine · doi:10.15252/emmm.201505846 · Cited by 127 · see citing works
“…of ApoER2 with PSD-95 to activate NMDA receptors and also with c-Jun amino-terminal kinase (JNK)-interacting proteins (JIP), which have been implicated in neuronal survival through interactions with JNK (Gotthardt et al, 2000; Stockinger et al, 2000; Beffert et al, 2005, 2006; Hoe et al, 2006).”
InfluentialWaetzig, V., Zhao, Y., & Herdegen, T. (2006) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2006.08.002 · Cited by 129 · see citing works
Stockinger, W., Sailler, B., Strasser, V., Recheis, B., Fasching, D., Kahr, L., Schneider, W. J., & Nimpf, J. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf435 · Cited by 130 · see citing works
Taru, H., Iijima, K., Hase, M., Kirino, Y., Yagi, Y., & Suzuki, T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108372200 · Cited by 128 · see citing works
Lipoprotein receptors – an evolutionarily ancient multifunctional receptor family
Dieckmann, M., Dietrich, M. F., & Herz, J. (2010) · Biological Chemistry · doi:10.1515/bc.2010.129 · Cited by 126 · see citing works
“…density protein (PSD95) (Beffert et al., 2005; Hoe et al., 2006b) and cJun-N-terminal kinase interacting proteins (JIPs) (Gotthardt et al., 2000; Stockinger et al., 2000) that are essential for the activation of Src family kinases and the following phosphorylation of the NMDA receptor subunits…”
Beffert, U., Durudas, A., Weeber, E. J., Stolt, P. C., Giehl, K. M., Sweatt, J. D., Hammer, R. E., & Herz, J. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.4566-05.2006 · Cited by 121 · see citing works
“…ICD in exon 19, such as mitogen-activated protein kinase 8-interacting protein 1/2 (JIP1/2) and/or PSD95 (postsynaptic density 95) (Gotthardt et al., 2000; Stockinger et al., 2000), are necessary for transmitting the Reelin signal required for enhanced LTP and modulating adult memory and behavior.”
BackgroundMarzolo, M.-P., & Bu, G. (2009) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2008.10.005 · Cited by 122 · see citing works
“[96] Stockinger W, Brandes C, Fasching D, Hermann M, Gotthardt M, Herz J, et al.”
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 · see citing works
“Recent work by several laboratories (D’Arcangelo et al., 1995, 1997, 1999; Dulabon et al., 2000; Hiesberger et al., 1999; Senzaki et al., 1999; Stockinger et al., 2000 ) point to multiple proteins as likely receptors for Reelin protein binding.”
BackgroundBu, G. (2001) · International review of cytology · doi:10.1016/s0074-7696(01)09011-8 · Cited by 120 · see citing works
Harris, K. K., Lamson, R. E., Nelson, B., Hughes, T. R., Marton, M. J., Roberts, C. J., Boone, C. M., & Pryciak, P. M. (2001) · Current Biology · doi:10.1016/s0960-9822(01)00567-x · Cited by 119 · see citing works
Kajino‐Sakamoto, R., Byrd, D. T., Brown, H. M., Hisamoto, N., Matsumoto, K., & Jin, Y. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-07-0553 · Cited by 117 · see citing works
“Binding of JIP1 and JIP2 to ApoER2 Reelin receptor may tether kinesin-1 to vesicles containing ApoER2 (Stockinger et al., 2000; Verhey et al., 2001).”
BackgroundMuresan, Z. L., & Mureşan, V. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200502043 · Cited by 112 · see citing works
“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).”
ResultEssential 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 · see citing works
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 · see citing works
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 110 · 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
“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).”
BackgroundMahler, 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 · see citing works
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 · see citing works
“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. (2008) · Glia · doi:10.1002/glia.20772 · Cited by 106 · see citing works
“Of particular relevance to this study, the cytoplasmic domain of LRP1 binds JNK-interacting proteins (JIP-1 and JIP-2) (Stockinger et al., 2000).”
BackgroundXian, 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 103 · see citing works
“The LRP1 cytoplasmic domain interacts with numerous intracellular adaptor and scaffold proteins (Gotthardt et al., 2000; Herz and Strickland, 2001; Stockinger et al., 2000).”
BackgroundLRP-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 · see citing works
“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].”
MethodModulation 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 · see citing works
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 · see citing works
“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).”
BackgroundSimilarities 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
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 98 · 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
“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].”
BackgroundNimpf, J. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/s1388-1981(00)00155-4 · Cited by 90 · 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
“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).”
Hirai, S.-I., Kawaguchi, A., Hirasawa, R., Baba, M., Ohnishi, T., & Ohno, S. (2002) · Development · doi:10.1242/dev.129.19.4483 · Cited by 87 · see citing works
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 83 · see citing works
“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).”
BackgroundLuque, J. M., Morante, J., & Fairén, A. (2003) · Developmental Brain Research · doi:10.1016/s0165-3806(02)00604-1 · Cited by 85 · see citing works
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 83 · see citing works
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 82 · see citing works
“…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).”
BackgroundKoch, 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 · see citing works
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 · see citing works
“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].”
BackgroundTrafficking of signaling modules by kinesin motors
Schnapp, B. J. (2003) · Journal of Cell Science · doi:10.1242/jcs.00488 · Cited by 81 · see citing works
“Among the many different transmembrane receptors implicated in JNK signaling is ApoER2, the Reelin receptor (Stockinger et al., 2000).”
BackgroundMolecular biology of apolipoprotein E
Strittmatter, W. J., & Hill, C. B. (2002) · Current Opinion in Lipidology · doi:10.1097/00041433-200204000-00002 · Cited by 80 · see citing works
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 79 · see citing works
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 79 · see citing works
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 · see citing works
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 · see citing works
“PSD95 and JIPs interact with sequences within exon 19 (blue).”
BackgroundInfluentialExpanding 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 75 · see citing works
“for cJun-N-terminal kinase interacting proteins ( JIPs) (21, 22), in the ICD of Apoer2 (19).”
BackgroundLi, 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 · see citing works
“Recently, studies have revealed new roles of LDLR family members as transducers of extracellular signals (17, 22, 24, 43, 46, 47).”
BackgroundApolipoprotein 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 · see citing works
- 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
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-08
- Volume
- 275
- Issue
- 33
- Pages
- 25625-25632
- ISSN
- 0021-9258 (ISSN-L)
- 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
- 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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