Dephosphorylation of NCAM1 bound pFyn

Stable Identifier
R-NUL-420388
Type
Reaction [transition]
Species
Homo sapiens
Compartment
General
SVG |   | PPTX  | SBGN
Dephosphorylation of NCAM1 bound pFyn

The homophilic NCAM1:NCAM1 interaction redistributes these molecules and leads to the formation of clusters within lipid rafts. Spectrin, an NCAM1 binding cytoskeletal protein, colocalizes with NCAM1 and codistribute to lipid rafts. Spectrin associates with RPTP-alpha, linking it to the cytoplasmic NCAM1 domain and causing its coredistribution to lipid rafts on NCAM1 clustering. The receptor tyrosine phosphatase RPTP-alpha is an activator of all kinases of the Src family, including Fyn kinase.

The interaction of RPTP-alpha and the SH2 domain of Fyn induces an interaction of Fyn Tyr531 with the D1 domain of RPTP-alpha. This induces dephosphorylation of Tyr531 and activates Fyn.

Literature References
PubMed ID Title Journal Year
15623578 RPTPalpha is essential for NCAM-mediated p59fyn activation and neurite elongation

Bodrikov, V, Leshchyns'ka, I, Sytnyk, V, Overvoorde, J, den Hertog, J, Schachner, M

J Cell Biol 2005
12743109 Neural cell adhesion molecule (NCAM) association with PKCbeta2 via betaI spectrin is implicated in NCAM-mediated neurite outgrowth

Leshchyns'ka, I, Sytnyk, V, Morrow, JS, Schachner, M

J Cell Biol 2003
Participants
Catalyst Activity
Catalyst Activity
Title
protein tyrosine phosphatase activity of Receptor-type tyrosine-protein phosphatase T [plasma membrane]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed
Created
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