Monitoring SHP2 phosphoproteome dynamics identifies new substrate sites and sites protected from dephosphorylation by its SH2 domains, highlighting distinct scaffolding and catalytic activities in effecting a transmembrane signaling response.
Global phosphoproteomic analysis in nerve terminal during exocytosis reveals 252 uniquely regulated phosphosites, highlighting complex regulation of active zone proteins at multiple sites and the role of specific kinases/phosphatases.
A detailed analysis of protein abundance and phosphorylation changes across mitotic subphases and interphase in asynchronously growing human cells has been enabled by combining FACS with quantitative MS-based proteomics.
Quantitative phosphoproteomics defines the substrates for Cyclin A/Cdk1 kinase during early mitosis and follow up studies validate that one identified substrate, MYPT1, influences the stability of k-MT attachments by regulating Plk1.
Inhibition of ITGA2-mediated cancer cell-collagen interaction or targeting focal adhesion kinase activity may present an opportunity for therapeutic intervention of metastatic spread in ovarian cancer.
A comprehensive whole cell proteomic map describing expression time courses of >6,500 viral and cellular proteins during HIV infection identifies Vif-dependent antagonism of key cellular phosphatase PP2A.