BiomedExperts: Identification of tyrosine 620 as the major phosphorylation site of myelin-associated glycoprotein and its implication in interacting with signaling molecules.

Username

Password

Preview

Sign-in free and Explore the Exciting World of BiomedExperts:

Over 1.500.000 Profiles
More than 1.800 Organizations worldwide
State of the Art Network Visualizations

Manage your own Profile
Locate Experts in your Country/Region
Locate Experts in your 1. and 2. Level Network
Connect to Experts Worldwide

find experts for

Sign-in to see more

1994: Jaramillo M L; Afar D E; Almazan G; Bell J C
Identification of tyrosine 620 as the major phosphorylation site of myelin-associated glycoprotein and its implication in interacting with signaling molecules.
The Journal of biological chemistry 1994;269(44):27240-5.

Myelin-associated glycoprotein (MAG) is a myelin-specific cell adhesion molecule of the immunoglobulin supergene family and is tyrosine-phosphorylated in the developing brain. To define the role of MAG in signal transduction, the tyrosine phosphorylation sites were analyzed. The major tyrosine phosphorylation residue was identified as Tyr-620, which was found to interact specifically with the SH2 domains of phospholipase C (PLC gamma). This domain may represent a novel protein binding motif that can be regulated by tyrosine phosphorylation. MAG also specifically bound the Fyn tyrosine kinase, suggesting that MAG serves as a docking protein that allows the interaction between different signaling molecules.

Post to CiteULike

Sign in free and see...

Visualized networks:

See your personal network in
sophisticated graphical views

GeoTargeted Searches:

Locate experts around the world
and connect with global collaborators

Research Profiles:

See the visualized research activity
of experts around the globe

Sign-in to see more