Ontology highlight
ABSTRACT:
SUBMITTER: Akbulut S
PROVIDER: S-EPMC2947483 | biostudies-literature | 2010 Oct
REPOSITORIES: biostudies-literature
Akbulut Simge S Reddi Alagarsamy L AL Aggarwal Priya P Ambardekar Charuta C Canciani Barbara B Kim Marianne K H MK Hix Laura L Vilimas Tomas T Mason Jacqueline J Basson M Albert MA Lovatt Matthew M Powell Jonathan J Collins Samuel S Quatela Steven S Phillips Mark M Licht Jonathan D JD
Molecular biology of the cell 20100818 19
Sprouty (Spry) proteins are negative regulators of receptor tyrosine kinase signaling; however, their exact mechanism of action remains incompletely understood. We identified phosphatidylinositol-specific phospholipase C (PLC)-γ as a partner of the Spry1 and Spry2 proteins. Spry-PLCγ interaction was dependent on the Src homology 2 domain of PLCγ and a conserved N-terminal tyrosine residue in Spry1 and Spry2. Overexpression of Spry1 and Spry2 was associated with decreased PLCγ phosphorylation and ...[more]