Key result
Yeast actin cytoskeleton studies substantially define universal mechanisms regulating actin assembly.
Yeast models have contributed substantially to defining the universal mechanisms regulating actin assembly and disassembly in eukaryotes.
Yeast models advance eukaryotic actin understanding; leaves open validation and cardiac cell applications.
The actin cytoskeleton is a complex network of dynamic polymers, which plays an important role in various fundamental cellular processes, including maintenance of cell shape, polarity, cell division, cell migration, endocytosis, vesicular trafficking, and mechanosensation. Precise spatiotemporal assembly and disassembly of actin structures is regulated by the coordinated activity of about 100 highly conserved accessory proteins, which nucleate, elongate, cross-link, and sever actin filaments. Both in vivo studies in a wide range of organisms from yeast to metazoans and in vitro studies of purified proteins have helped shape the current understanding of actin dynamics and function. Molecular genetics, genome-wide functional analysis, sophisticated real-time imaging, and ultrastructural studies in concert with biochemical analysis have made yeast an attractive model to understand the actin cytoskeleton, its molecular dynamics, and physiological function. Studies of the yeast actin cytoskeleton have contributed substantially in defining the universal mechanism regulating actin assembly and disassembly in eukaryotes. Here, we review some of the important insights generated by the study of actin cytoskeleton in two important yeast models the budding yeast Saccharomyces cerevisiae and the fission yeast Schizosaccharomyces pombe.
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Mishra et al. (2014) conducted a review in Yeast actin cytoskeleton. Studies of the yeast actin cytoskeleton in Saccharomyces cerevisiae and Schizosaccharomyces pombe have contributed substantially to defining the universal mechanisms regulating actin assembly.
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