title: Kinetic characterization of apoptotic Ras signaling through Nore1-MST1 complex formation.
abstract: Ras-mediated apoptotic signaling is expected to be mediated via Rassf-MST complexes, but the system has been poorly characterized in vitro until now. Here we demonstrate that active H-Ras, Nore1A and MST1 form a stable ternary complex in vitro without other external factors, Nore1A interacting simultaneously with H-Ras and MST1 via its RBD and SARAH domain, respectively. Moreover, our data show for the first time that the SARAH domain of Nore1A plays a role in the Nore1A binding to H-Ras. Finally, we analyze the relation between the electrostatic and hydrophobic forces and kinetic constants of the Nore1A - H-Ras complex.
authors.affiliation: Department of Physical Chemistry I, Ruhr University Bochum, Universitätsstraße 150, D-44780 Bochum.
authors.forename: Agne
authors.initials: A
authors.lastname: Koturenkiene
authors.affiliation: Department of Physical Chemistry I, Ruhr University Bochum, Universitätsstraße 150, D-44780 Bochum.
authors.forename: Cihan
authors.initials: C
authors.lastname: Makbul
authors.affiliation: Department of Physical Chemistry I, Ruhr University Bochum, Universitätsstraße 150, D-44780 Bochum.
authors.forename: Christian
authors.initials: C
authors.lastname: Herrmann
authors.affiliation: Department of Physical Chemistry I, Ruhr University Bochum, Universitätsstraße 150, D-44780 Bochum.
authors.forename: Diana
authors.initials: D
authors.lastname: Constantinescu-Aruxandei
mesh_terms: D017209:Apoptosis; D007700:Kinetics; D020559:Monomeric GTP-Binding Proteins / Q000378:metabolism*; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D015398:Signal Transduction; D018631:ras Proteins / Q000378:metabolism*
chemical_list: D017346:Protein Serine-Threonine Kinases; D020559:Monomeric GTP-Binding Proteins; D018631:ras Proteins
keywords: Hippo; RBD; SARAH; affinity; hetero dimer; kinetics