Post-translational modifications articles from across Nature Portfolio

Understanding the role of pyrophosphorylation requires specific analytical strategies to discriminate it from protein phosphorylation. A custom workflow reveals that nucleolar protein pyrophosphorylation in human cells regulates the transcription of ribosomal DNA.

Cryo-electron microscopy (cryo-EM), kinetic analysis and single-molecule biochemistry reveal how the tubulin tyrosine ligase-like 6 (TTLL6) glutamylase binds reads microtubule geometry and modification state of neighboring tubulins, enabling a spatial positive feedback loop for microtubule modification.

Coactivator-associated arginine methyltransferase 1 (CARM1) is an important target in hematologic malignancies. In this work, the authors show that the hyperactivation of Janus kinase 2 (JAK2) by the V617F mutation phosphorylates CARM1 which regulates its methyltransferase activity and alters its target specificity.

Liu et al. reveal that human TOPORS is a SUMO1-selective SUMO-targeted ubiquitin ligase (STUbL). The parallel action of TOPORS and the STUbL RNF4 defines a general mechanistic principle governing pathways driven by direct SUMO–ubiquitin crosstalk.

Here the authors show that anti-phage signalling in the CBASS immune system is activated by a ubiquitination-like poly-cGASylation mechanism.

Reversible S-palmitoylation regulates gasdermin D cleavage, membrane translocation and pore formation to control pyroptosis following bacterial infection.

Thomas Arnesen and colleagues discuss an emerging major role of one of the most common protein modifications, N-terminal acetylation, in shielding the proteome from degradation.

The microbiome is implicated in a study that involves the metabolism of dietary fibre into short-chain fatty acids, which provides a biochemical link to the poorly understood histone butyrylation.

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.

O-linked N-acetylglucosamine (O-GlcNAc) is an endogenous form of glycosylation that alters the structure of α-synuclein amyloid fibrils and attenuates their pathogenetic properties. The modified fibrils have a significantly reduced ability to seed the aggregation of endogenous α-synuclein in cultured neurons and in mice brains in vivo, which results in reduced pathology.