Studies of the cytoskeleton of Schizosaccharomyces pombe and Saccharomyces cerevisiae

Anabelle Aranda, University of Texas at El Paso

Abstract

It has been suggested that components of the cytoskeleton contribute to the signal transduction process in association with one or more members of the G protein family. In animal cells, relatively high-affinity binding between dimeric tubulin and the alpha subunits of Gs and Gi1 has also been reported (Wang and Rasenick, 1991). Tubulin has binding domains for microtubule-associated proteins and modifies G-protein signaling. According to Chen et al., (2003) heterotrimeric G-proteins regulate microtubule assembly in mammalian cells. G alpha inhibits microtubule assembly and increases microtubule disassembly by activating the intrinsic GTPase of tubulin while G βγ promotes microtubule assembly (Roychowdhury and Rasenick, 1997; 1999). A Saccharomyces cerevisiae gene (GPR1) for the G-protein coupled receptor has been isolated. The receptor is localized at the plasma membrane and monitors extracellular signals such as neurotransmitters (Yun et al., 1997). In the present study, the interaction between α and βγ subunits of G proteins and tubulin were analyzed by immunofluorescence in two distantly related yeasts, Saccharomyces cerevisiae, a budding yeast, and Schizosaccharomyces pombe, a fission yeast, by immunofluorescence (Hagan and Hyams, 1988) and electron microscopy. The visualization of the γ and α tubulin is most evident in Saccharomyces cerevisiae. (Abstract shortened by UMI.) ^

Subject Area

Biology, Cell

Recommended Citation

Aranda, Anabelle, "Studies of the cytoskeleton of Schizosaccharomyces pombe and Saccharomyces cerevisiae" (2005). ETD Collection for University of Texas, El Paso. AAI1430266.
http://digitalcommons.utep.edu/dissertations/AAI1430266

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