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Actin is one of the most abundant proteins in eukaryotic cells. It is a 43-kDa protein that was originally identified and purified from skeletal muscle. Once thought to be simply a component of muscle cells, actin has later been shown to be a highly conserved and ubiquitiously distributed protein in eukaryotic cells. It has been extensively studied as a cytoplasmic cytoskeletal protein that is involved in a wide range of cellular processes, including cell motility, growth and cytokinesis; endocytosis, exocytosis and secretion; signal transduction, synaptic transmission as well as intracellular trafficking (Ascough, 2004;Brakebusch and Fassler, 2003;Suetsugu and Takenawa, 2003). In the cytoplasm, actin exists in equilibrium between monomers (globularor G-actin) and polymers (filamentousor F-actin). The dynamics of actin, the coordinated assembly and disassembly of actin filaments in response to cellular and extracellular signaling, is critical for the diverse functions of actin and is tightly regulated by a plethora of actin-binding proteins (ABPs) in the cytoplasm (dos Remedios et al., 2003). To date, over 70 distinct classes of ABPs have being identified and the inventory is still far from been completed (Pollard and Borisy, 2003).

Exploring Secrets of Nuclear Actin Involvement in the Regulation of Gene Transcription and Genome Organization