VLDLR binds RELN

Stable Identifier
R-HSA-8854466
Type
Reaction [binding]
Species
Homo sapiens
Compartment
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Reelin (RELN) (DeSilva et al. 1997) is an extracellular matrix serine protease highly expressed in the brain that plays a role in neural cell positioning during brain development by regulating their microtubule function and neuronal migration. It can bind to the extracellular domains of lipoprotein receptors VLDLR and APOER2 to induce tyrosine phosphorylation of disabled-1 (DAB1), an adaptor protein bound to the cytoplasmic tails of these receptors that is a phosphorylation target for a signaling cascade trigggered by RELN. This suggests VLDLR and APOER2 participate in transmitting the extracellular RELN signal to intracellular signaling processes initiated by DAB1 (Hiesberger et al. 1999). In post-mortem studies of schizophrenia sufferers, RELN was found to be significantly reduced (by up to 50%) in brain samples whereas DAB1 was observed to be at normal levels, suggesting a role for RELN in schizophrenia (Impagnatiello et al. 1998).

Literature References
PubMed ID Title Journal Year
9049633 The human reelin gene: isolation, sequencing, and mapping on chromosome 7

DeSilva, U, D'Arcangelo, G, Braden, VV, Chen, J, Miao, GG, Curran, T, Green, ED

Genome Res. 1997
10571241 Direct binding of Reelin to VLDL receptor and ApoE receptor 2 induces tyrosine phosphorylation of disabled-1 and modulates tau phosphorylation

Hiesberger, T, Trommsdorff, M, Howell, BW, Goffinet, A, Mumby, MC, Cooper, JA, Herz, J

Neuron 1999
9861036 A decrease of reelin expression as a putative vulnerability factor in schizophrenia

Impagnatiello, F, Guidotti, AR, Pesold, C, Dwivedi, Y, Caruncho, H, Pisu, MG, Uzunov, DP, Smalheiser, NR, Davis, JM, Pandey, GN, Pappas, GD, Tueting, P, Sharma, RP, Costa, E

Proc. Natl. Acad. Sci. U.S.A. 1998
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