Series |

Post-translational modifications

The diversity of modifications that a nascent peptide acquires as it is transported to its target cellular location is long established, as is the ability of tags such as phosphorylation and ubiquitylation to regulate signalling and protein turnover. But recently we have seen a renaissance of interest in the ability of additional modifications — from ubiquitin-like proteins to moieties such as sugars or methyl, acetyl and prenyl groups — to target specific sites in proteins and to coordinately exert dynamic control over protein function in diverse cell biological contexts. The articles in this series discuss new insights that have been gained into how ‘old and new’ modifications are regulated and recognized, and how they crosstalk with one another to control fundamental biological processes.


  • Nature Reviews Molecular Cell Biology | Review Article

    Ubiquitylation is a post-translational modification that modulates protein stability and regulates various cellular signalling pathways and cellular processes, including cell differentiation, proliferation and migration. Recent insights highlight its crucial role in development and how its deregulation is associated with several diseases.

    • Michael Rape
  • Nature Reviews Molecular Cell Biology | Timeline

    Protein methylation was discovered over 50 years ago, but only with the advent of genomic and proteomic technologies could its mechanisms and cellular functions be studied in detail. Shi and Murn discuss the seminal discoveries in protein methylation research and highlight future directions for this field.

    • Jernej Murn
    •  &  Yang Shi
  • Nature Reviews Molecular Cell Biology | Review Article

    Many cellular proteins are reversibly modified by O-linked N-acetylglucosamine (O-GlcNAc) moieties on Ser and Thr residues. Studies on the mechanisms and functions of O-GlcNAcylation and its links to metabolism reveal the importance of this modification in the maintenance of cellular and organismal homeostasis.

    • Xiaoyong Yang
    •  &  Kevin Qian
  • Nature Reviews Molecular Cell Biology | Review Article

    In addition to acetylation, eight types of structurally and functionally different short-chain acylations have recently been identified as important histone Lys modifications: propionylation, butyrylation, 2-hydroxyisobutyrylation, succinylation, malonylation, glutarylation, crotonylation and β-hydroxybutyrylation. These modifications are regulated by enzymatic and metabolic mechanisms and have physiological functions, which include signal-dependent gene activation and metabolic stress.

    • Benjamin R. Sabari
    • , Di Zhang
    • , C. David Allis
    •  &  Yingming Zhao
  • Nature Reviews Molecular Cell Biology | Analysis

    Analysis of the available human small ubiquitin-like modifier (SUMO) proteomics data provided evidence for the sumoylation of thousands of proteins and residues, and clustered the sumoylated proteins into functional networks. Sumoylation is a frequent modification, occurring mostly on nuclear proteins, with functions including transcription, mRNA processing and the DNA-damage response.

    • Ivo A. Hendriks
    •  &  Alfred C. O. Vertegaal
  • Nature Reviews Molecular Cell Biology | Review Article

    Learning more about the biochemistry of protein prenylation (modification by isoprenoid lipids) and its functional effects on target CAAX proteins has provided opportunities for therapeutic intervention in a range of human diseases.

    • Mei Wang
    •  &  Patrick J. Casey