Strings of beads, in different colours.

Advancing the mechanistic understanding of writers and readers of ubiquitylation

In this issue, we feature studies progressing our understanding of writers and readers of ubiquitylation, and several pieces reflecting on the ever-expanding roles of this critical modification.

Editorial

Announcements

  • NSMB cover

    January 2024 marks 30 years since we published the first volume of NSMB. We will be celebrating this milestone throughout 2024, reflecting on the road covered and looking towards the future.

  • NSMB cover first issue

    In January 2024, NSMB will celebrate the 30th anniversary of publishing its first issue. To celebrate, we would like to give our readers, center stage and invite you to send us your comments and letters to the editors, reflecting both on the past and the upcoming years. Details: https://rdcu.be/doiBQ

Nature Structural & Molecular Biology is a Transformative Journal; authors can publish using the traditional publishing route OR via immediate gold Open Access.

Our Open Access option complies with funder and institutional requirements.

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  • First discovered more than five decades ago, protein ubiquitylation has proven to be an omnipresent post-translational modification regulating virtually every eukaryotic cellular process. With novel clinical applications and recent studies demonstrating ubiquitylation of biomolecules other than proteins, the interest in ubiquitin will not waver any time soon.

    Editorial
  • In addition to its role in proteasomal degradation, ubiquitin has multiple roles in autophagy. It can mark proteins for autophagic degradation and actively drive autophagosome formation. Recent work shows that ubiquitin can also be conjugated to phospholipids and other biomolecules.

    • Noboru Mizushima
    Comment
  • Ubiquitination is an essential process that curtails cellular levels of damaged and redundant proteins. Chemical biologists have harnessed this natural system to induce the degradation of disease-relevant proteins. We reflect here on the potential of ‘degraders’ for targeted selectivity, and discuss the role of computer-aided drug design in shaping future advances.

    • Rory Whelan
    • Cristina Mayor-Ruiz
    Comment
  • The modification of proteins with the small protein ubiquitin constitutes a Daedalian system of posttranslational modifications in every eukaryotic cell, which is often referred to as the ubiquitin code1. Here we consider the scale and complexity of the ubiquitin system in light of recent developments.

    • Bernhard C. Lechtenberg
    • David Komander
    Comment