Actin Structure and Function
By R. Dominguez, K. Holmes. Annual Review of Biophysics, 2011
1,164 citations recorded by the source corpus.
Actin is the most abundant protein in most eukaryotic cells. It is highly conserved and participates in more protein-protein interactions than any known protein. These properties, along with its ability to transition between monomeric (G-actin) and filamentous (F-actin) states under the control of nucleotide hydrolysis, ions, and a large number of actin-binding proteins, make actin a critical player in many cellular functions, ranging from cell motility and the maintenance of cell shape and polarity to the regulation of transcription. Moreover, the interaction of filamentous actin with myosin forms the basis of muscle contraction. Owing to its central role in the cell, the actin cytoskeleton is also disrupted or taken over by numerous pathogens. Here we review structures of G- and F-actin and discuss some of the interactions that control the polymerization and disassembly of actin.
Subfields: Atomic and Molecular Physics, and Optics, Cardiology and Cardiovascular Medicine, Cell Biology
View Paper: https://www.semanticscholar.org/paper/2eddc48ba2945bd24a9b7d73c194d53c5f35ae19
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Citations in the corpus
- Structure of Actin-related protein 8 and its contribution to nucleosome binding (2012, background): “It is likely that these insertions in part evolved to mediate contacts with other subunits of the INO80 complex, suggesting that Arp8 uses the same filament facing side as actin for protein–protein contacts (Supplementary Figure S2).”