Reelin molecules assemble together to form a large protein complex, which is inhibited by the function-blocking CR-50 antibody.

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.

authors

Utsunomiya-Tate N,Kubo K,Tate S,Kainosho M,Katayama E,Nakajima K,Mikoshiba K

doi

10.1073/pnas.160272497

keywords:

subject

Has Abstract

pub_date

2000-08-15 00:00:00

pages

9729-34

issue

17

eissn

0027-8424

issn

1091-6490

pii

160272497

journal_volume

97

pub_type

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