Increased amounts of the 47-kD protein are associated with neutrophil disorders involving this protein, whose depolymerization often involves cofilin.
Increased amounts of the 47-kD protein are associated with neutrophil disorders involving this protein, whose depolymerization often involves cofilin. Adducin, Cap(G), and members of the gelsolin family are all used to disassemble this protein, and it shares genetic characteristics with the prokaryotic MreB, which adjusts cell width in rod-shaped bacteria. The seven-unit Arp2/3 complex regulates the polymerization of this protein, whose signal transduction involves WASp, named for a syndrome in which T cells fail to reorganize (*) structures composed of this protein. Prolifin is one of the major "binding proteins" associated with this protein, which is held in place by nebulin. A double helix of this highly-conserved protein forms the polymers comprising microfilaments in the cytoskeleton, and it binds to the globular heads of its counterpart when forming thin filaments in the sarcomere. For 10 points, identify this motor protein that drives muscle contraction along with myosin.
Increased amounts of the 47-kD protein are associated with neutrophil disorders involving this protein, whose depolymerization often involves cofilin.
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