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Actin-based Motility pp 213–235Cite as

Regulation of the Cytoplasmic Actin Monomer Pool in Actin-based Motility

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Abstract

Actin-based motility is driven by spatially and temporally coordinated rapid actin polymerization. This relies on the precise regulation of the size, localization and dynamics of the cytoplasmic actin monomer pool by proteins that control different aspects of actin dynamics. In dynamic actin filament arrays, the “old” actin filaments are severed and depolymerized by ADF/cofilin and gelsolin family proteins, and the newly depolymerized actin monomers are subsequently recycled for new rounds of polymerization with the aid of actin monomer-binding proteins such as profilin and cyclase-associated protein. Furthermore, actin monomer sequestering proteins, such as twinfilin and β-thymosins control the size, nucleotide status, and dynamics of the actin monomer pool in cells. Actin polymerization at filament barbed ends is also controlled by capping proteins that “funnel” polymerization-competent actin monomers to a subset of filament ends at the sites of rapid actin assembly. In this chapter, we discuss the mechanisms by which these proteins control the cytoplasmic actin monomer pool and how their activities are regulated in cells to promote various actin-based motile processes.

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Authors and Affiliations

  1. Institute of Biotechnology, University of Helsinki, P.O. Box 56, 00014, Helsinki, Finland

    Pekka Lappalainen

  2. Institute of Biotechnology, University of Helsinki, Helsinki, Finland

    Maarit Makkonen & Hongxia Zhao

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  1. Pekka Lappalainen
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  2. Maarit Makkonen
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  1. , Laboratory of Structural Enzymology and, CNRS, Gif-sur-Yvette Cedex, 91198, France

    Marie-France Carlier

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Lappalainen, P., Makkonen, M., Zhao, H. (2010). Regulation of the Cytoplasmic Actin Monomer Pool in Actin-based Motility. In: Carlier, MF. (eds) Actin-based Motility. Springer, Dordrecht. https://doi.org/10.1007/978-90-481-9301-1_9

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