Actin

Supporting information

Actin is a ubiquitous globular protein that is one of the most highly-conserved proteins known. It is found in two main states: G-actin is the globular monomeric form, whereas F-actin forms helical polymers. Both G- and F-actin are intrinsically flexible structures - a feature vital in actin's role as a dynamic filament network.

Actin has four major functions. Firstly, F-actin polymers form microfilaments - polar intracellular 'tracks' for kinesin motor proteins, allowing the transport of vesicles, organelles and other cargo. Actin is a component of the cytoskeleton and links to α-actinin, E-cadherin and β-catenin at adherens junctions. This gives mechanical support to cells and attaches them to each other and the extracellular matrix. In muscle cells, actin-rich thin filaments associate with myosin-rich thick filaments to form actomyosin myofibrils. Using energy from the hydrolysis of ATP, myofibrils undergo cyclic shortening through actin-myosin head interactions, which represents the mechanics of muscle contraction. Finally, actin has a role in cell motility through polymerization and depolymerization of fibrils.

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Gene Species Gene Symbol Gene Accession No. Protein Accession No.
α1 actin Human ACTA1 NM_001100 P68133
Mouse Acta1 NM_009606 P68134
Rat Acta1 NM_019212 NP_062085
α2 actin Human ACTA2 NM_001613 P62736
Mouse Acta2 NM_007392 P62737
Rat Acta2 NM_031004 P62738
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Literature for Actin

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