Intrinsically disordered proteins articles from across Nature Portfolio

Here, the authors show that biomolecular condensates can enhance enzymatic rates by creating distinct solvent environments compared to the surrounding solution, and this emergent property can manifest within assemblies as small as nanometers.

Cells must respond to environmental changes. In three fungal species adapted to different temperatures, cellular responses are conserved yet tuned to each organism’s thermal niche, including the formation of adaptive biomolecular condensates.

Here the authors characterise the impact of phosphorylation site mutations in intrinsically disordered regions (IDRs) on protein-protein interactions, highlighting the critical role of phosphorylation of IDRs in health and disease.

Here, the authors dissect the fuzzy interaction between the prokaryote transcription factor HigA2 and its DNA target and show that specific, transient interactions drive specificity despite HigA2 remaining mostly disordered.

Modulating amyloid protein phase separation and fibrilization may help in addressing neurodegenerative diseases. This study demonstrates that halogen-doped graphene quantum dots can modulate these processes in TDP-43 in both nucleus and cytoplasm.

The androgen receptor forms nuclear condensates associated with gene transcription. Investigating the molecular basis of condensate formation led us to discover an approach for optimizing small molecules that inhibit the receptor in a currently untreatable form of prostate cancer.

Leveraging the underlying mechanism of phase-separating biomolecular condensates could prove a great asset for developing designer condensates in bioengineering applications.

Self-assembly of replication protein A (RPA) into dynamic condensates after binding of single-stranded DNA promotes telomere maintenance in cancer cells.

Biomolecular condensates grow in busy cellular environments. Statistical image analysis of heterogeneous structures now enables quantification of macromolecular interactions between condensates and cytoskeletal filaments.

A spectrum of high-risk leukemias is caused by recurrent chromosomal translocations that result in the expression of fusion proteins. In a recent article in Nature, it has been demonstrated that the oncogenic properties of one such fusion, NUP98–HOXA9, are linked to its ability to self-associate and function through aberrantly phase-separated “onco-condensates.”