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 novel regulatory step in the endocytic pathway, which occurs post-internalization, takes place at the trans-Golgi network and involves the arrestin-related protein Rod1 and the ubiquitin ligase Rsp5.
PTEN organizes multicellular architecture by non-catalytic scaffolding of spatially localized β-Arrestin1/ARHGAP21/Cdc42 protein complexes to control mitotic spindle orientation, multicellular configuration and lumen formation.
Ablation of the Cdkn1c cell cycle inhibitor leads to defective muscle stem cell dynamics and myogenic potential, while progressive cytoplasmic to nuclear cellular localization of the Cdkn1c protein regulates growth arrest.
Building on previous work (Ly et al., 2014), we show that elutriated cells and arrested cells have similar patterns of DNA content and cyclin expression: however, a large fraction of the proteome changes detected in arrested cells are found to reflect arrest-specific responses rather than physiological cell cycle regulation.