TY - JOUR
T1 - Reelin binds α3β1 integrin and inhibits neuronal migration
AU - Dulabon, Lori
AU - Olson, Eric C.
AU - Taglienti, Mary G.
AU - Eisenhuth, Scott
AU - McGrath, Barbara
AU - Walsh, Christopher A.
AU - Kreidberg, Jordan A.
AU - Anton, E. S.
N1 - Funding Information:
The authors thank Murcy Moise, Sarah Engler, Dr. Khalequz Zaman, Dr. Jorge Gonzalez, and Peter Lin for exceptional assistance with experiments. We thank Drs. Joan Brugge, Anjenn Chenn, Andre Goffinet, Michael Greenberg, Joachim Herz, Ed Monuki, and Davie Van Vactor for their helpful comments. C. A. W. was supported by grants from the National Institute of Neurological Disorders and Stroke (RO1 NS38097 and PO1 NS39404), the National Alliance for Autism Research, and the National Alliance for Research in Schizophrenia and Depression. E. C. O. was supported by a National Institutes of Health postdoctoral training grant. This research was supported by grants from the National Institutes of Health, the March of Dimes Foundation, and the Whitehall Foundation to E. A.
PY - 2000
Y1 - 2000
N2 - Mice that are mutant for Reelin or Dab1, or doubly mutant for the VLDL receptor (VLDLR) and ApoE receptor 2 (ApoER2), show disorders of cerebral cortical lamination. How Reelin and its receptors regulate laminar organization of cerebral cortex is unknown. We show that Reelin inhibits migration of cortical neurons and enables detachment of neurons from radial glia. Recombinant and native Reelin associate with α3β1 integrin, which regulates neuron-glia interactions and is required to achieve proper laminar organization. The effect of Reelin on cortical neuronal migration in vitro and in vivo depends on interactions between Reelin and α3β1 integrin. Absence of α3β1 leads to a reduction of Dab1, a signaling protein acting downstream of Reelin. Thus, Reelin may arrest neuronal migration and promote normal cortical lamination by binding α3β1 integrin and modulating integrin-mediated cellular adhesion.
AB - Mice that are mutant for Reelin or Dab1, or doubly mutant for the VLDL receptor (VLDLR) and ApoE receptor 2 (ApoER2), show disorders of cerebral cortical lamination. How Reelin and its receptors regulate laminar organization of cerebral cortex is unknown. We show that Reelin inhibits migration of cortical neurons and enables detachment of neurons from radial glia. Recombinant and native Reelin associate with α3β1 integrin, which regulates neuron-glia interactions and is required to achieve proper laminar organization. The effect of Reelin on cortical neuronal migration in vitro and in vivo depends on interactions between Reelin and α3β1 integrin. Absence of α3β1 leads to a reduction of Dab1, a signaling protein acting downstream of Reelin. Thus, Reelin may arrest neuronal migration and promote normal cortical lamination by binding α3β1 integrin and modulating integrin-mediated cellular adhesion.
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U2 - 10.1016/S0896-6273(00)00007-6
DO - 10.1016/S0896-6273(00)00007-6
M3 - Article
C2 - 10939329
AN - SCOPUS:0033624279
SN - 0896-6273
VL - 27
SP - 33
EP - 44
JO - Neuron
JF - Neuron
IS - 1
ER -