Phosphorylation is the enzymatic process through which a phosphate group is added via an ester bond, generally by a kinase, to either a small molecule or a protein. Protein phosphorylation is important in regulating signal transduction systems, as it affects the activity of its target, for instance in turning an enzyme ‘on’ or ‘off’.

Latest Research and Reviews

News and Comment

  • News and Views |

    Under steady-state conditions, the E3 ubiquitin ligase Parkin is localized to the cytosol in an autoinhibited state. Two recent studies describe the mechanism of Parkin activation by phosphorylation via structural rearrangement of the Ubl and RING2 domains, explaining how the RING2 domain is released from the core of Parkin to allow for ubiquitination of its substrates.

    • François Le Guerroué
    •  & Richard J. Youle
  • Research Highlights |

    A set of 80 (mostly synaptic) proteins show hyperphosphorylation in sleep-deprived mice and genetically ‘sleepy’ mice, suggesting that increased phosphorylation of such proteins may be associated with sleep need.

    • Natasha Bray
  • News and Views |

    Activation signals from GPCRs, the largest receptor family, are transmitted to heterotrimeric G proteins and arrestins, and can be differentially modulated by GPCR phosphorylation. In a recent article, available data, including multiple arrestin structures, are analyzed to decipher common and state-specific conformational changes in arrestins and how these depend on patterns of receptor phosphorylation.

    • Christopher J. Draper-Joyce
    •  & Arthur Christopoulos