Nckβ Interacts with Tyrosine-Phosphorylated Disabled 1 and Redistributes in Reelin-Stimulated Neurons

• DOI: 10.1128/mcb.23.20.7210-7221.2003
• Publication Date: 2003-09-29T23:28:21Z
• Authors: Albéna Pramatarova; Pawel G. Ochalski; Kelian Chen; Andrea Gropman; Sage Myers; Kyung-Tai Min; Brian W. Howell
• Keywords: DAB1

The tyrosine phosphorylation sites of the Disabled 1 (Dab1) docking protein are essential for transmission Reelin signal, which regulates neuronal placement. Here we identify Nckβ as a phosphorylation-dependent, Dab1-interacting protein. SH2 domain but not Nckα binds Dab1 phosphorylated on Reelin-regulated site, Y220, or Y232. is coexpressed with in developing brain and cultured neurons, where stimulation leads to redistribution from cell soma into processes. We found that tyrosine-phosphorylated synergy disrupts actin cytoskeleton transfected cells. In Drosophila melanogaster, exogenous expression mouse causes site-dependent morphological changes compound eye. This phenotype enhanced by overexpression Nck Dock, suggesting conserved interaction between family members. suggest model recruitment membrane, it acts remodel cytoskeleton.