Reentrant liquid condensate phase of proteins is stabilized by hydrophobic and non-ionic interactions

Autor: Georg Krainer, Timothy J. Welsh, Jerelle A. Joseph, Jorge R. Espinosa, Sina Wittmann, Ella de Csilléry, Akshay Sridhar, Zenon Toprakcioglu, Giedre Gudiškytė, Magdalena A. Czekalska, William E. Arter, Jordina Guillén-Boixet, Titus M. Franzmann, Seema Qamar, Peter St George-Hyslop, Anthony A. Hyman, Rosana Collepardo-Guevara, Simon Alberti, Tuomas P. J. Knowles

Publikováno v: Nature Communications, Vol 12, Iss 1, Pp 1-14 (2021)

Elucidating the molecular driving forces underlying liquid–liquid phase separation is a key objective for understanding biological function and malfunction. Here the authors show that a wide range of cellular proteins, including FUS, TDP-43, Brd4,

Externí odkaz: https://doaj.org/article/f1a7c13511ed46d3b7d48b9f4017a81c

CAPRIN1

Autor: Andrea, Delle Vedove, Janani, Natarajan, Ginevra, Zanni, Matthias, Eckenweiler, Anixa, Muiños-Bühl, Markus, Storbeck, Jordina, Guillén Boixet, Sabina, Barresi, Simone, Pizzi, Irmgard, Hölker, Friederike, Körber, Titus M, Franzmann, Enrico S, Bertini, Janbernd, Kirschner, Simon, Alberti, Marco, Tartaglia, Brunhilde, Wirth

Publikováno v: Cellular and molecular life sciences : CMLS. 79(10)

CAPRIN1 is a ubiquitously expressed protein, abundant in the brain, where it regulates the transport and translation of mRNAs of genes involved in synaptic plasticity. Here we describe two unrelated children, who developed early-onset ataxia, dysarth

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::fde2003976f29e9d8503ae63f764e036
https://pubmed.ncbi.nlm.nih.gov/36136249

Reentrant liquid condensate phase of proteins is stabilized by hydrophobic and non-ionic interactions

Autor: Jordina Guillén-Boixet, Peter St George-Hyslop, Giedre Gudiškytė, Akshay Sridhar, Sina Wittmann, William E. Arter, Georg Krainer, Jerelle A. Joseph, Magdalena A. Czekalska, Tuomas P. J. Knowles, Simon Alberti, Seema Qamar, Titus M. Franzmann, Jorge R. Espinosa, Rosana Collepardo-Guevara, Timothy J. Welsh, Ella de Csillery, Anthony A. Hyman, Zenon Toprakcioglu

Publikováno v: Nature Communications
Nature Communications, Vol 12, Iss 1, Pp 1-14 (2021)

Liquid–liquid phase separation of proteins underpins the formation of membraneless compartments in living cells. Elucidating the molecular driving forces underlying protein phase transitions is therefore a key objective for understanding biological

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e76508f1c7f77c9dfa6f04a1b46d6ff
https://www.repository.cam.ac.uk/handle/1810/317798

Defective ribosomal products challenge nuclear function by impairing nuclear condensate dynamics and immobilizing ubiquitin

Autor: Arianna Dorotea Carrà, Titus M. Franzmann, Laura Mediani, Simon Alberti, Daniel Mateju, Jonathan Vinet, Ina Poser, Jordina Guillén-Boixet, Federica Francesca Morelli, Ilaria Bigi, Serena Carra, Tatiana Tiago

Publikováno v: The EMBO Journal

Nuclear protein aggregation has been linked to genome instability and disease. The main source of aggregation‐prone proteins in cells is defective ribosomal products (DRiPs), which are generated by translating ribosomes in the cytoplasm. Here, we r

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::917d61afe440d1187e89fe250bc35a04

RNA buffers the phase separation behavior of prion-like RNA binding proteins

Autor: Jie Wang, Lara Marrone, Andrey Pozniakovsky, Simon Alberti, Jordina Guillén-Boixet, Pavel Tomancak, Sandra Rizk, Titus M. Franzmann, Young-Tae Chang, Shovamayee Maharana, Dimitrios K. Papadopoulos, Anthony A. Hyman, Marc Bickle, Ina Poser, Jared Sterneckert, Doris Richter, Marcus Jahnel

Publikováno v: Maharana, S, Wang, J, Papadopoulos, D K, Richter, D, Pozniakovsky, A, Poser, I, Bickle, M, Rizk, S, Guillén-Boixet, J, Franzmann, T M, Jahnel, M, Marrone, L, Chang, Y-T, Sterneckert, J, Tomancak, P, Hyman, A A & Alberti, S 2018, ' RNA buffers the phase separation behavior of prion-like RNA binding proteins ', Science, vol. 360, no. 6391, pp. 918-921 . https://doi.org/10.1126/science.aar7366
Science

RNA and membraneless organelles Membraneless compartments can form in cells through liquidliquid phase separation (see the Perspective by Polymenidou). But what prevents these cellular condensates from randomly fusing together? Using the RNA-binding

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::686247c724dbe64ee5fd740abaf80917
https://hdl.handle.net/20.500.11820/fd5ed633-bb65-441b-a53a-867cf43027b7