Controlling the cortical actin motor

• Published in: Protoplasma Vol. 249; no. 4; pp. 1001 - 1015
• Main Authors: Grantham, Julie, Lassing, Ingrid, Karlsson, Roger
• Format: Journal Article
• Language: English
• Published: Vienna Springer-Verlag 01.10.2012; Springer Vienna; Springer Nature B.V
• Subjects: actin; Actin Cytoskeleton - metabolism; Actin dynamics; Actin folding; Actin-binding proteins; Actins - metabolism; Animals; arp2/3 complex; beta-actin; Biochemistry and Molecular Biology; Biokemi och molekylärbiologi; Biomedical and Life Sciences; CCT; Cell Biology; Cell motility; Cell Movement - physiology; cross-linked profilin; crystal-structure; electron tomography; end; eukaryotic cells; eukaryotic cytosolic chaperonin; f-actin; fast-growing; Humans; Life Sciences; Microfilament Proteins - metabolism; microfilament system; microfilaments; Molecular chaperone; Molecular Chaperones - metabolism; Plant Sciences; polymerization; Review; Review Article; saccharomyces-cerevisiae; signal transduction; Zoology; Cell motility; Actin-binding proteins; Actin folding; CCT; Actin dynamics; Molecular chaperone
• ISSN: 0033-183X; 1615-6102; 1615-6102
• DOI: 10.1007/s00709-012-0403-9

Actin is the essential force-generating component of the microfilament system, which powers numerous motile processes in eukaryotic cells and undergoes dynamic remodeling in response to different internal and external signaling. The ability of actin to polymerize into asymmetric filaments is the inherent property behind the site-directed force-generating capacity that operates during various intracellular movements and in surface protrusions. Not surprisingly, a broad variety of signaling pathways and components are involved in controlling and coordinating the activities of the actin microfilament system in a myriad of different interactions. The characterization of these processes has stimulated cell biologists for decades and has, as a consequence, resulted in a huge body of data. The purpose here is to present a cellular perspective on recent advances in our understanding of the microfilament system with respect to actin polymerization, filament structure and specific folding requirements.