Mechanism of redox-mediated guanine nucleotide exchange on redox-active Rho GTPases.
Rho GTPases regulate multiple cellular processes including actin cytoskeletal rearrangements, transcriptional regulation, and oxidant production. The studies described herein demonstrate that small molecule redox agents, in addition to protein regulatory factors, can regulate the activity of redox-active Rho GTPases. A novel (GXXXXGK(S/T)C) motif, conserved in a number of Rho GTPases, appears critical for redox-mediated guanine nucleotide dissociation in vitro. A detailed molecular mechanism for redox regulation of GXXXXGK(S/T)C motif-containing Rho GTPases is proposed.
Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599-7260, USA.
Jongyun
J
Heo
Sharon L
SL
Campbell
D020816:Amino Acid Motifs; D006150:Guanine Nucleotides / Q000737:chemistry / Q000378:metabolism*; D015394:Molecular Structure; D008970:Molecular Weight; D010084:Oxidation-Reduction; D026361:Reactive Nitrogen Species; D017382:Reactive Oxygen Species / Q000737:chemistry / Q000378:metabolism; D020741:rho GTP-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
D006150:Guanine Nucleotides; D026361:Reactive Nitrogen Species; D017382:Reactive Oxygen Species; D020741:rho GTP-Binding Proteins