Open AccessA molecular assembly phase transition and kinetic proofreading modulate Ras activation by SOS
Author(s) -
William Y. C. Huang,
Steven Alvarez,
Yasushi Kondo,
Young Kwang Lee,
Jean K. Chung,
Hiu Yue Monatrice Lam,
Kabir H. Biswas,
John Kuriyan,
Jay T. Groves
Publication year - 2019
Publication title -
science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 12.556
H-Index - 1186
eISSN - 1095-9203
pISSN - 0036-8075
DOI - 10.1126/science.aau5721
Subject(s) - guanine nucleotide exchange factor , proofreading , chemistry , activator (genetics) , biophysics , membrane , microbiology and biotechnology , cytosol , enzyme activator , exonuclease , receptor , gtpase , biochemistry , biology , enzyme , polymerase
Organized for action It is becoming increasingly clear that biomolecular condensates, which are concentrations of macromolecules not surrounded by a membrane, are a key organizational structure in eukaryotic cells (see the Perspective by Martin and Mittag). Now, two papers show how such condensates function in actin assembly or in a Ras signaling pathway. In both cases, the condensates form at the plasma membrane and increase the activity of signaling proteins by increasing their membrane dwell times. Caseet al. show that the dwell time is dependent on cluster stoichiometry, so that stoichiometry of regulatory proteins can control actin assembly. Huanget al. demonstrate that the longer dwell time allows kinetic proofreading in receptor-mediated activation of Ras.Science , this issue p.1093 , p.1098 ; see also p.1036
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