N-terminal acetylation can occur on actin, as it does on more than 80 percent of human proteins, and appears to help regulate actin's ability to form filaments.

Actin filaments are protein fibers that make up the internal skeleton of the cell. As active elements of our cells, actin filaments support the cell’s fusion, movement and are involved in many other ...

Researchers have raised the curtain on how actin maintains just the right filament length to keep the cell healthy and happily dividing.

They provide experimental evidence supporting the “proof of principle” that the flexible and specific helical twists of actin filaments regulate the functions of actin binding proteins.

Cofilin severing activity can generate free actin filament ends that are accessible for F-actin polymerization and depolymerization. The combination of structural data for filament severing with ...

Actin has several functions in cancer propagation Actin filaments are part of the cell skeleton and essential for stability and motility. They form a network that dynamically builds up and gets ...

Microtubule guidance along actin bundles may use either static (probably in neurons or tissue cells) or dynamic motor-mediated (as in yeast) links between microtubules and actin filaments.

An artificial cytoskeleton imitating cells’ internal scaffold provides evidence of a controversial concept called ...

Actin is found in all living cells where it has a range of important functions – from muscle contraction to cell signaling and cell shape.

In turn, the cytoskeleton relies on a type of actin protein, called filamentous or F-actin. It forms networks of thin, flexible filaments that affect the shape, stiffness, and movement of cells.

The delay in the α-actin switch coincided with the onset of motor function deficits and histopathological changes including a high frequency of type IIB ring fibers. Our data suggest that subtle ...