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.
Phosphoproteomics identifies β-arrestin 2 phosphorylation at Thr383 by MEK as a key step of GPCR-induced Erk½ activation, thus providing new insight into the molecular mechanism underlying β-arrestin-dependent GPCR-operated signaling.
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.