Abstract:
:Reelin is a key mediator of ordered neuronal alignment in the brain. Here, we demonstrate that Reelin molecules assemble with each other to form a huge protein complex both in vitro and in vivo. The Reelin-Reelin interaction clearly is inhibited by the function-blocking anti-Reelin antibody, CR-50, at a concentration known to inhibit Reelin function. This assembly is mediated by electrostatic interaction of the CR-50 epitope region. Recombinant CR-50 epitope fragments spontaneously constitute a soluble, string-like homopolymer with a regularly repeated structure composed of more than 40 monomers. Mutated Reelin, which lacks the CR-50 epitope region, cannot form a homopolymer and fails to induce efficient tyrosine phosphorylation of Disabled 1 (Dab1), which should occur to transduce the Reelin signal. These data suggest that Reelin exerts its biological function by composing a large protein assembly driven by the CR-50 epitope region, proposing a novel model of the Reelin signaling in neurodevelopment.
journal_name
Proc Natl Acad Sci U S Aauthors
Utsunomiya-Tate N,Kubo K,Tate S,Kainosho M,Katayama E,Nakajima K,Mikoshiba Kdoi
10.1073/pnas.160272497keywords:
subject
Has Abstractpub_date
2000-08-15 00:00:00pages
9729-34issue
17eissn
0027-8424issn
1091-6490pii
160272497journal_volume
97pub_type
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