Regulation of synaptojanin 2 5′-phosphatase activity by Src

• Published in: Cell adhesion & migration Vol. 6; no. 6; pp. 518 - 525
• Main Authors: Chuang, Yayu, Xu, Xiaonan, Kwiatkowska, Aneta, Tsapraillis, George, Hwang, Hyonson, Petritis, Konstantinos, Flynn, Dan, Symons, Marc
• Format: Journal Article
• Language: English
• Published: United States Taylor & Francis 01.11.2012; Landes Bioscience
• Subjects: Blotting, Western; Cell Membrane - metabolism; Clathrin-Coated Vesicles - metabolism; clathrin-mediated endocytosis; Cortactin - genetics; Cortactin - metabolism; Endocytosis; Enzyme Activation; HEK293 Cells; Humans; Immunoprecipitation; invadopodia; Phosphoric Monoester Hydrolases - genetics; Phosphoric Monoester Hydrolases - metabolism; Phosphorylation; Plasmids - genetics; Plasmids - metabolism; podosome; Protein Binding; Protein Interaction Mapping; Proto-Oncogene Proteins c-fyn - genetics; Proto-Oncogene Proteins c-fyn - metabolism; Recombinant Proteins - genetics; Recombinant Proteins - metabolism; Research Paper; RNA, Small Interfering - genetics; RNA, Small Interfering - metabolism; Src; src Homology Domains; src-Family Kinases - genetics; src-Family Kinases - metabolism; synaptojanin 2; Transfection; Tyrosine - metabolism
• ISSN: 1933-6918; 1933-6926
• DOI: 10.4161/cam.22139

Synaptojanin 2 (SYNJ2) is a phosphatidylinositol (PI) phosphatase that controls two distinct functions, clathrin-mediated endocytosis and tumor cell invadopodia formation and invasion. Here, we identify a number of novel SYNJ2 binding partners, several of which have previously been shown to be necessary for invadopodia formation or clathrin-mediated endocytosis. We focus on Src family kinases. We found that Src phosphorylates SYNJ2 on Tyr 490 , thereby stimulating SYNJ2 5′-phosphatase activity in vitro. We also provide evidence that Src-mediated phosphorylation of SYNJ2 contributes to invadopodia formation.