Intrinsically disordered proteins

Intrinsically disordered proteins are isolated polypeptide chains with no stable tertiary structure under physiological conditions in vitro. They remain functional despite the lack of a well-defined structure, contradicting the notion that structure defines the function of a protein.

Latest Research and Reviews

News and Comment

  • News & Views |

    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.

    • Tanja Mittag
    •  & Aseem Z. Ansari
  • Comments & Opinion |

    The long non-coding RNA Xist induces heterochromatinization of the X chromosome by recruiting repressive protein complexes to chromatin. Here we gather evidence, from the literature and from computational analyses, showing that Xist assemblies are similar in size, shape and composition to phase-separated condensates, such as paraspeckles and stress granules. Given the progressive sequestration of Xist’s binding partners during X-chromosome inactivation, we formulate the hypothesis that Xist uses phase separation to perform its function.

    • Andrea Cerase
    • , Alexandros Armaos
    •  & Gian Gaetano Tartaglia
  • Research Highlights |

    Many eukaryotic proteins, including key transcription regulators, contain intrinsically disordered regions (IDRs), which serve as flexible interaction platforms. The molecular understanding of IDR-based interactions is now emerging, providing new insights into how IDRs promote protein compartmentalization and/or phase separation and how these processes regulate gene expression.

    • Paulina Strzyz