Myosin-actin interaction in Dictyostelium cells revealed by GFP-based strain sensor and validated linear spectral unmixing

Cytometry. Part a : the Journal of the International Society for Analytical Cytology
Sosuke Iwai, Taro Q P Uyeda

Abstract

Myosin is an actin-based motor protein that is involved in a wide range of cellular motile processes. Although in vitro properties of the myosin-actin interaction have been extensively studied, the interaction in vivo remains poorly understood. Recently, we developed a GFP-based strain sensor termed PriSSM (PRIM-based strain sensor module), by using the proximity imaging (PRIM) technique, which detects spectral changes of two GFP molecules that are in direct contact. Using PriSSM-myosin II fusion proteins, the interaction between myosin II and F-actin can be detected in Dictyostelium cells. In the spectroscopic measurements of PriSSM, to decompose the measured spectra of the cells expressing the sensor proteins into the contributions from the sensor and the background autofluorescence, we applied the linear spectral unmixing approach, which was based on the assumption that the errors at each wavelength were independent. Cellular autofluorescence, however, often includes systematic errors, so that the unmixing procedures might lead to biased estimates. Here, to validate our spectral unmixing procedures, we estimate the possible maximum errors in the fluorescence ratio values that are obtained by unmixing spectra including such s...Continue Reading

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Citations

Jun 3, 2015·Molecular and Cellular Biology·Carol Jurchenko, Khalid S Salaita
Jul 4, 2012·Chemical Communications : Chem Comm·Taro IchimuraTomonobu M Watanabe

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