Activation of Rac and Cdc42 Video Imaged by Fluorescent Resonance Energy Transfer-Based Single-Molecule Probes in the Membrane of Living Cells

By Reina E. Itoh, K. Kurokawa, Y. Ohba, H. Yoshizaki, N. Mochizuki, M. Matsuda. Molecular and Cellular Biology, 2002

621 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/b7137d98ec417b744c24067f15faf3b05a1f3f72

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Citations in the corpus

Fluorescent proteins and their applications in imaging living cells and tissues. (2010, background): “The universality and relative simplicity of such a design have led to the development of numerous FRETbased sensors of this type, including GES for monitoring changes in the concentration of Ca(2) (130, 153, 262, 263, 291, 292, 295, 304, 307, 327, 434), cyclic nucleotides (174, 317, 318, 375, 445, 5”
Rho GTPases: biochemistry and biology. (2005, background): “GTP-bound active Rac accumulates at the front of migrating cells, and in chemotaxing neutrophils this is sustained through a positive feedback loop with PI 3-kinase and its lipid product PIP3 (Gardiner et al. 2002, Itoh et al. 2002, Kraynov et al. 2000).”
Development of an optimized backbone of FRET biosensors for kinases and GTPases (2011, methodology): “pRaichu-Ras and Raichu-Rac1 containing an EV linker were constructed by replacing the linker region of the original biosensors with an EV linker (Mochizuki et al., 2001; Itoh et al., 2002).”
Conserved microtubule–actin interactions in cell movement and morphogenesis (2003, background): “In support of this hypothesis, FRET-based visualization of Rac1 activity has revealed a gradient from the leading edg”
Adhesion-dependent cell mechanosensitivity. (2003, background): “…visualization of active Rho has not been reported yet, there are some interesting data concerning the distribution of activated Rac and Cdc42 based on various modifications of the fluorescence resonance energy transfer (FRET) technique (Gardiner et al. 2002, Itoh et al. 2002, Kraynov et al. 2000).”
Multiphoton time-domain fluorescence lifetime imaging microscopy: practical application to protein–protein interactions using global analysis (2009, methodology): “…(FLIM) as opposed to intensity based methods (Jares-Erijman & Jovin 2006) are the independence of the measurement to fluorophore concentration and light path as well as removing the need to make numerous normalizing measurements to obtain a quantitative result (Jares-Erijman & Jovin 2006).”
Interferon-α induction through Toll-like receptors involves a direct interaction of IRF7 with MyD88 and TRAF6 (2004, methodology): “Human MyD88, IRF3 or IRF7 obtained by PCR was inserted into the Xho I- Not I sites of pCAG and pCAGGS vectors encoding YFP and CFP at the N and C termini of the inserted protei”
Amiloride inhibits macropinocytosis by lowering submembranous pH and preventing Rac1 and Cdc42 signaling (2010, methodology): “The Cdc42 biosensor uses an intermolecular design as reported by several groups (Itoh et al., 2002; Seth et al., 2003; Tzima et al., 2003; Hoppe and Swanson, 2004), but here is further optimized by the use of different fluorescent proteins and of a Cdc42-binding domain from WASP, a fragment shown…”