References
- Etienne-Manneville S, Hall A. Rho GTPases in cell biology. Nature. 2002;420(6916):629–635.
- Mosaddeghzadeh N, Ahmadian MR. The RHO family GTPases: mechanisms of regulation and signaling. Cells. 2021;10(7):1831.
- Ren XD, Kiosses WB, Schwartz MA. Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton. EMBO J. 1999;18(3):578–585.
- Bros M, et al. RhoA as a key regulator of innate and adaptive immunity. Cells. 2019;8(7):733.
- Lessey EC, Guilluy C, Burridge K. From mechanical force to RhoA activation. Biochemistry. 2012;51(38):7420–7432.
- Dvorsky R, Ahmadian MR. Always look on the bright site of Rho: structural implications for a conserved intermolecular interface. EMBO Rep. 2004;5(12):1130–1136.
- Sahai E, Alberts AS, Treisman R. RhoA effector mutants reveal distinct effector pathways for cytoskeletal reorganization, SRF activation and transformation. EMBO J. 1998;17(5):1350–1361.
- Kataoka K, Ogawa S. Variegated RHOA mutations in human cancers. Exp Hematol. 2016;44(12):1123–1129.
- Hodge RG, Ridley AJ. Regulating Rho GTPases and their regulators. Nat Rev Mol Cell Biol. 2016;17(8):496–510.
- Bagci H, Sriskandarajah N, Robert A, et al. Mapping the proximity interaction network of the Rho-family GTPases reveals signalling pathways and regulatory mechanisms. Nat Cell Biol. 2020;22(1):120–134.
- Pertz O, Hodgson L, Klemke RL, et al. Spatiotemporal dynamics of RhoA activity in migrating cells. Nature. 2006;440(7087):1069–1072.
- Tong J, et al. Phosphorylation and activation of RhoA by ERK in response to epidermal growth factor stimulation. PLoS One. 2016;11(1):e0147103.
- Rolli-Derkinderen M, Toumaniantz G, Pacaud P, et al. RhoA phosphorylation induces Rac1 release from guanine dissociation inhibitor alpha and stimulation of vascular smooth muscle cell migration. Mol Cell Biol. 2010;30(20):4786–4796.
- Fujisawa K, Madaule P, Ishizaki T, et al. Different regions of Rho determine Rho-selective binding of different classes of Rho target molecules. J Biol Chem. 1998;273(30):18943–18949.
- Lammers M, et al. Specificity of interactions between mDia isoforms and Rho proteins. J Biol Chem. 2008;283(50):35236–35246.
- Rose R, Weyand M, Lammers M, et al. Structural and mechanistic insights into the interaction between Rho and mammalian Dia. Nature. 2005;435(7041):513–518.
- Maesaki R, Ihara K, Shimizu T, et al. The structural basis of Rho effector recognition revealed by the crystal structure of human RhoA complexed with the effector domain of PKN/PRK1. Mol Cell. 1999;4(5):793–803.
- Reid T, Furuyashiki T, Ishizaki T, et al. Rhotekin, a new putative target for Rho bearing homology to a serine/threonine kinase, PKN, and rhophilin in the rho-binding domain. J Biol Chem. 1996;271(23):13556–13560.
- Watanabe G, et al. Protein kinase N (PKN) and PKN-related protein rhophilin as targets of small GTPase Rho. Science. 1996;271(5249):645–648.
- Fritz RD, Letzelter M, Reimann A, et al. A versatile toolkit to produce sensitive FRET biosensors to visualize signaling in time and space. Sci Signal. 2013;6(285):rs12.
- Kim JG, Islam R, Cho JY, et al. Regulation of RhoA GTPase and various transcription factors in the RhoA pathway. J Cell Physiol. 2018;233(9):6381–6392.
- Fine N, Gracey E, Dimitriou I, et al. GEF-H1 is required for colchicine inhibition of neutrophil rolling and recruitment in mouse models of gout. J Immunol. 2020;205(12):3300–3310.
- Kobayashi H, Picard L-P, Schönegge A-M, et al. Bioluminescence resonance energy transfer-based imaging of protein-protein interactions in living cells. Nat Protoc. 2019;14(4):1084–1107.
- Dale NC, Johnstone EKM, White CW, et al. NanoBRET: the bright future of proximity-based assays. Front Bioeng Biotechnol. 2019;7:56.
- Laschet C, Dupuis N, Hanson J. A dynamic and screening-compatible nanoluciferase-based complementation assay enables profiling of individual GPCR-G protein interactions. J Biol Chem. 2019;294(11):4079–4090.
- Leung T, et al. A novel serine/threonine kinase binding the Ras-related RhoA GTPase which translocates the kinase to peripheral membranes. J Biol Chem. 1995;270(49):29051–29054.
- Nagai T, et al. A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications. Nat Biotechnol. 2002;20(1):87–90.