N-terminus-mediated dimerization of ROCK-I is required for RhoE binding and actin reorganization

The Biochemical Journal
Ritu GargAnne J Ridley

Abstract

ROCK-I (Rho-associated kinase 1) is a serine/threonine kinase that can be activated by RhoA and inhibited by RhoE. ROCK-I has an N-terminal kinase domain, a central coiled-coil region and a RhoA-binding domain near the C-terminus. We have previously shown that RhoE binds to the N-terminal 420 amino acids of ROCK-I, which includes the kinase domain as well as N-terminal and C-terminal extensions. In the present study, we show that N-terminus-mediated dimerization of ROCK-I is required for RhoE binding. The central coiled-coil domain can also dimerize ROCK-I in cells, but this is insufficient in the absence of the N-terminus to allow RhoE binding. The kinase activity of ROCK-I(1-420) is required for dimerization and RhoE binding; however, inclusion of part of the coiled-coil domain compensates for lack of kinase activity, allowing RhoE to bind. N-terminus-mediated dimerization is also required for ROCK-I to induce the formation of stellate actin stress fibres in cells. These results indicate that dimerization via the N-terminus is critical for ROCK-I function in cells and for its regulation by RhoE.

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Citations

Nov 13, 2009·Cellular and Molecular Life Sciences : CMLS·C Hahmann, T Schroeter
Jan 5, 2016·Archivum Immunologiae Et Therapiae Experimentalis·Lei WeiJianjian Shi
Oct 24, 2008·The EMBO Journal·David KomanderDavid Barford
Sep 15, 2012·Cellular Signalling·Andrzej MleczakEdmond Y W Chan
Apr 23, 2013·Critical Reviews in Biochemistry and Molecular Biology·Alice V Schofield, Ora Bernard
Nov 12, 2013·European Journal of Medicinal Chemistry·Ronggui GuanRongbiao Pi
Jan 8, 2015·Frontiers in Endocrinology·Janina Müller-Deile, Mario Schiffer
Aug 23, 2019·The Biochemical Journal·Raquel B HagaAnne J Ridley
Oct 24, 2017·Expert Review of Neurotherapeutics·Nikola SladojevicJames K Liao
Apr 3, 2013·International Journal of Molecular Medicine·Hongwei XiaFeng Bi

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