JCB logo
PeproTech: Your source for Cell Biology Research Reagents
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published online 28 December 2004. doi:10.1083/jcb.200405073
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 168, Number 1, 127-139
This Article
Right arrow Full Text
Right arrow PDF (Full Text)
Right arrow PPT slides of all figures
Right arrow Supplemental Material Index
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Bodrikov, V.
Right arrow Articles by Schachner, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bodrikov, V.
Right arrow Articles by Schachner, M.
Right arrowPubmed/NCBI databases
*Gene*GEO Profiles
*HomoloGene*UniGene
*Compound via MeSH
*Substance via MeSH
Hazardous Substances DB
*CALCIUM COMPOUNDS
*CALCIUM, ELEMENTAL
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Article

 RPTP{alpha} is essential for NCAM-mediated p59fyn activation and neurite elongation

Vsevolod Bodrikov1, Iryna Leshchyns'ka1, Vladimir Sytnyk1, John Overvoorde2, Jeroen den Hertog2, and Melitta Schachner1

1 Zentrum für Molekulare Neurobiologie, Universität Hamburg, 20246 Hamburg, Germany
2 Hubrecht Laboratory, Netherlands Institute for Developmental Biology, 3584 CT Utrecht, Netherlands

Correspondence to Melitta Schachner: melitta.schachner{at}zmnh.uni-hamburg.de

The neural cell adhesion molecule (NCAM) forms a complex with p59fyn kinase and activates it via a mechanism that has remained unknown. We show that the NCAM140 isoform directly interacts with the intracellular domain of the receptor-like protein tyrosine phosphatase RPTP{alpha}, a known activator of p59fyn. Whereas this direct interaction is Ca2+ independent, formation of the complex is enhanced by Ca2+-dependent spectrin cytoskeleton–mediated cross-linking of NCAM and RPTP{alpha} in response to NCAM activation and is accompanied by redistribution of the complex to lipid rafts. Association between NCAM and p59fyn is lost in RPTP{alpha}-deficient brains and is disrupted by dominant-negative RPTP{alpha} mutants, demonstrating that RPTP{alpha} is a link between NCAM and p59fyn. NCAM-mediated p59fyn activation is abolished in RPTP{alpha}-deficient neurons, and disruption of the NCAM–p59fyn complex in RPTP{alpha}-deficient neurons or with dominant-negative RPTP{alpha} mutants blocks NCAM-dependent neurite outgrowth, implicating RPTP{alpha} as a major phosphatase involved in NCAM-mediated signaling.

V. Bodrikov, I. Leshchyns'ka, and V. Sytnyk contributed equally to this paper.

Abbreviations used in this paper: FGFR, FGF receptor; NCAM, neural cell adhesion molecule.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:



  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents