- HIF-2α phosphorylation by CK1δ promotes erythropoietin secretion in liver cancer cells under hypoxia
Summary: Phosphorylation of hypoxia inducible factor 2α mediated by casein kinase 1δ increases erythropoietin production by impairing a CRM1-dependent nuclear export mechanism in liver cancer cells.
- ELYS regulates the localization of LBR by modulating its phosphorylation state
Highlighted Article: The nuclear envelope localization of LBR is regulated through a phosphorylation network governed by ELYS, and defects in this phosphorylation network induce the aberrant phosphorylation and mislocalization of LBR.
- The centrosomal deubiquitylase USP21 regulates Gli1 transcriptional activity and stability
Summary: We identify a Hedgehog-pathway-associated ubiquitin ligase adapter as a direct interaction partner of the deubiquitylase USP21 and discover a close interplay between USP21 and protein kinase A in regulating Gli1.
- MEKK1-dependent phosphorylation of calponin-3 tunes cell contractility
Summary: Phosphorylation of calponin-3 by MEKK1, which is regulated by actomyosin contraction, leads to an increase in cell-generated traction stress, forming a new positive-feedback loop in the cellular contractile machinery.
- Clathrin-mediated endocytosis in budding yeast at a glance
Summary: A review of the current knowledge of the timeline of clathrin-mediated endocytosis in the budding yeast S. cerevisiae, including discussion of recent works that focus on how this process is regulated.
- A dual phosphorylation switch controls 14-3-3-dependent cell surface expression of TASK-1
Summary: Phosphorylation of a previously neglected serine residue in the trafficking control region of TASK-1 interferes with the binding of trafficking machinery and enables complex regulation by physiological stimuli.
- Phosphorylation of C-terminal tyrosine residue 526 in FUS impairs its nuclear import
Highlighted Article: The C-terminal Tyr residue of FUS can be phosphorylated by members of the Src kinase family. Phosphorylated Tyr526 impairs the interaction of FUS with transportin 1 and, potentially, its nuclear import.
- Phosphorylation of PACSIN2 by protein kinase C triggers the removal of caveolae from the plasma membrane
Highlighted Article: Decreased membrane binding of PACSIN2 upon its PKC-mediated phosphorylation at serine 313 is shown to trigger the removal of caveolae from the plasma membrane.