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10.1073/pnas.1413397111

http://scihub22266oqcxt.onion/10.1073/pnas.1413397111
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C4273407!4273407!25468977
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suck abstract from ncbi


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pmid25468977      Proc+Natl+Acad+Sci+U+S+A 2014 ; 111 (50): 17821-6
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  • Site-specific cation release drives actin filament severing by vertebrate cofilin #MMPMID25468977
  • Kang H; Bradley MJ; Cao W; Zhou K; Grintsevich EE; Michelot A; Sindelar CV; Hochstrasser M; De La Cruz EM
  • Proc Natl Acad Sci U S A 2014[Dec]; 111 (50): 17821-6 PMID25468977show ga
  • Cofilin is an essential actin regulatory protein that severs filaments, which accelerates network remodeling by increasing the concentration of filament ends available for elongation and subunit exchange. The molecular basis of how cofilin binding interactions fragment filaments, which have stiffness comparable to commercial laboratory plastics, remains a central and unresolved mystery of cellular actin cytoskeleton reorganization. In this study we demonstrate that actin filament severing by vertebrate cofilin is driven by the linked dissociation of a single, site-specific cation that controls filament structure and mechanical properties, and that filament severing is an essential function of cofilin in cells. This work establishes that discrete interactions with cations serve a central regulatory function in mediating actin filament fragmentation by certain classes of severing proteins.
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