Cadherins and catenins bind to it via vinculin, and ATP binding causes this protein to transition between its globular and fibrous forms.
The Wiskott-Aldrich protein activates another protein that binds to this protein, and on the cell membrane these proteins complex with archvillin and supervillin. Prokaryotic analogues of this protein include MreB and ParM, and another protein that binds to it is mutated in Finnish-type amyloidosis, known as gelsolin. A common method of viewing this protein in cell culture involves using fluorescently-tagged phalloidin, and they tend to collect when nucleated by the Arp2/3 complex. Cadherins and catenins bind to it via vinculin, and ATP binding causes this protein to transition between its globular and fibrous forms. Polymers of it are surrounded by nebulin in one structure, and this protein forms lamellopodia and the contractile ring in cytokinesis. It also binds to troponin and tropomyosin in sarcomeres. For 10 points, name this protein that when arranged in a helix and polymerized forms microfilaments, and which pairs with the motor protein myosin.
The Wiskott-Aldrich protein activates another protein that binds to this protein, and on the cell membrane these proteins complex with archvillin and supervillin.
{Actin}