The reelin receptor ApoER2 recruits JNK-interacting proteins-1 and -2

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Item Type:	Article
Title:	The reelin receptor ApoER2 recruits JNK-interacting proteins-1 and -2
Creators Name:	Stockinger, W., Brandes, C., Fasching, D., Hermann, M., Gotthardt, M., Herz, J., Schneider, W.J. and Nimpf, J.
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.
Keywords:	Signal Transducing Adaptor Proteins, Alternative Splicing, Amino Acid Sequence, Northern Blotting, Brain, Carrier Proteins, Neuronal Cell Adhesion Molecules, Cell Differentiation, Cultured Cells, Cytoplasm, Complementary DNA, Epididymis, Extracellular Matrix Proteins, Glutathione Transferase, Immunohistochemistry, Fluorescence Microscopy, Biological Models, Molecular Sequence Data, Nerve Tissue Proteins, Neurons, Proline, Protein Binding, Lipoprotein Receptors, Reverse Transcriptase Polymerase Chain Reaction, Amino Acid Sequence Homology, Serine Endopeptidases, Signal Transduction, Stem Cells, Tissue Distribution, Two-Hybrid System Techniques, Animals, Mice
Source:	Journal of Biological Chemistry
ISSN:	0021-9258
Publisher:	American Society for Biochemistry and Molecular Biology
Volume:	275
Number:	33
Page Range:	25625-25632
Date:	18 August 2000
Official Publication:	https://doi.org/10.1074/jbc.M004119200
PubMed:	View item in PubMed

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