Special Issue "Protein Intrinsic Disorder: Role in Signaling, Regulation and Membrane-Less Organelle Formation"
Deadline for manuscript submissions: 30 June 2021.
Interests: intrinsically disordered proteins (IDPs); post-translational modifications (PTMs); signaling; nuclear magnetic resonance (NMR); small-angle X-ray scattering (SAXS)
Interests: intrinsically disordered proteins; folding copuled to binding; protein-protein interactions; structural transitions; paramyxoviruses
Special Issues and Collections in MDPI journals
Dr. Nathalie Sibille
Dr. Sonia Longhi
Dr. Carine Van Heijenoort
Manuscript Submission Information
Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.
Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Biomolecules is an international peer-reviewed open access monthly journal published by MDPI.
Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2000 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.
- intrinsically disordered proteins (IDPs)
- post-translational modification (PTM)
- membrane-less organelle formation (MLOs)
- liquid–liquid phase separation (LLPS)
- nuclear magnetic resonance (NMR)
- integrative structural biology
The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.
Title: Intrinsic disorder in BRCA2 facilitates tight regulation of multiple conserved binding events
Authors: Julien Manon; Petitalot Ambre; Ghouil Rania; Sandrine Caputo; Carreira Aura; Zinn-Justin Sophie
Affiliation: Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Univ Paris-Sud, Université Paris-Saclay, Gif-sur-Yvette Cedex, France Department of Biology, École Normale Supérieure, 94230 Cachan, France Service de génétique, unité de génétique constitutionnelle, Institut Curie, 26 rue d'Ulm, Paris, France Paris Sciences Lettres Research University, Paris, France Institut Curie, PSL Research University, CNRS, UMR3348, F-91405, Orsay, France Paris Sud University, Paris-Saclay University CNRS, UMR3348, F-91405 Orsay, France
Abstract: The maintenance of genome integrity in the cell is an essential process for the accurate transmission of the genetic material. BRCA2 participates in this process at several levels, including DNA repair by homologous recombination, protection of stalled replication forks and cell division. These activities are regulated and coordinated via cell-cycle dependent modifications. Mutations in BRCA2 cause genome instability and are associated with breast and ovarian cancers. BRCA2 is a very large protein of 3418 amino acids. Most well-characterized mutations causing a strong predisposition to cancer are located in the C-terminal 700 amino acids DNA binding domain of BRCA2. The rest of the BRCA2 protein is predicted to be disordered. Interactions involving intrinsically disordered regions (IDRs) remain difficult to identify both using bioinformatics tools and performing experimental assays. Yet, the lack of well-structured binding sites provides unique functional opportunities for BRCA2 to bind to a large set of partners in a tightly regulated manner. We here summarize the predictive and experimental arguments that support the presence of disorder in BRCA2. We describe how BRCA2 IDRs mediate self-assembly and binding to partners during DNA double-strand break repair, mitosis and meiosis. We highlight how phosphorylation by cell-cycle and DNA repair kinases regulates these interactions.