Role of Schwannomin and Paxillin in Cell Growth Control
Abstract
Preliminary results indicate that phosphorylation of serine 518 is not required for localization of schwannomin to the plasma membrane and filopodia and lameliapodia. This indicates that schwannomin binding to paxillin does not require phosphorylation of serine 518 by Pak, a racactivated serine/threonine kinase. It suggests that schwannomin firsts binds paxillin and targets to the membrane where local activation of p21 activated kinase by cdc42 or rac stimulates phosphorylation of serine 518 on schwannomin and the ensuing change in morphology.
Document Details
- Document Type
- Technical Report
- Publication Date
- May 01, 2004
- Accession Number
- ADA425669
Entities
People
- Cristina Fernandez-valle
Organizations
- University of Central Florida