BROWSE

Related Researcher

Author

Min, Kyung-Tai
Molecular & Cellular Neurobiology Lab(Min Lab)
Research Interests
  • Local protein synthesis, learning & memory, behavior, mitochondrial dynamics

ITEM VIEW & DOWNLOAD

Nck beta interacts with tyrosine-phosphorylated Disabled 1 and redistributes in reelin-stimulated neurons

Cited 55 times inthomson ciCited 55 times inthomson ci
Title
Nck beta interacts with tyrosine-phosphorylated Disabled 1 and redistributes in reelin-stimulated neurons
Author
Pramatarova, AOchalski, PGChen, KGropman, AMyers, SMin, Kyung-TaiHowell, BW
Keywords
PHOTORECEPTOR AXON GUIDANCE; AMYLOID PRECURSOR PROTEIN; LAMINAR ORGANIZATION; SIGNALING PATHWAY; BRAIN-DEVELOPMENT; CORTICAL-NEURONS; ADAPTER PROTEINS; DIRECT BINDING; VLDL RECEPTOR; MOUSE-BRAIN
Issue Date
200310
Publisher
AMER SOC MICROBIOLOGY
Citation
MOLECULAR AND CELLULAR BIOLOGY, v.23, no.20, pp.7210 - 7221
Abstract
The tyrosine phosphorylation sites of the Disabled I (Dab1) docking protein are essential for the transmission of the Reelin signal, which regulates neuronal placement. Here we identify Nckbeta as a phosphorylation-dependent, Dab1-interacting protein. The SH2 domain of Nckbeta but not Nckalpha binds Dab1 phosphorylated on the Reelin-regulated site, Y220, or on Y232. Nckbeta is coexpressed with Dahl in the developing brain and in cultured neurons, where Reelin stimulation leads to the redistribution of Nckbeta from the cell soma into neuronal processes. We found that tyrosine-phosphorylated Dah1 in synergy with Nckbeta disrupts the actin cytoskeleton in transfected cells. In Drosophila melanogaster, exogenous expression of mouse Dahl causes tyrosine phosphorylation site-dependent morphological changes in the compound eye. This phenotype is enhanced by overexpression of the Drosophila Nck protein Dock, suggesting a conserved interaction between the Disabled and Nck family members. We suggest a model in which Dab1 phosphorylation leads to the recruitment of Nckbeta to the membrane, where it acts to remodel the actin cytoskeleton.
URI
Go to Link
DOI
http://dx.doi.org/10.1128/MCB.23.20.7210-7221.2003
ISSN
0270-7306
Appears in Collections:
SLS_Journal Papers
Files in This Item:
2-s2.0-0141640850.pdfDownload

find_unist can give you direct access to the published full text of this article. (UNISTARs only)

Show full item record

qr_code

  • mendeley

    citeulike

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

MENU