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10.1126/science.aaa3923

http://scihub22266oqcxt.onion/10.1126/science.aaa3923
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C5039038!5039038!25977552
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suck abstract from ncbi


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pmid25977552      Science 2015 ; 348 (6236): 808-12
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  • Regulated assembly of a supramolecular centrosome scaffold in vitro #MMPMID25977552
  • Woodruff JB; Wueseke O; Viscardi V; Mahamid J; Ochoa SD; Bunkenborg J; Widlund PO; Pozniakovsky A; Zanin E; Bahmanyar S; Zinke A; Hong SH; Decker M; Baumeister W; Andersen JS; Oegema K; Hyman AA
  • Science 2015[May]; 348 (6236): 808-12 PMID25977552show ga
  • The centrosome organizes microtubule arrays within animal cells and comprises two centrioles surrounded by an amorphous protein mass called the pericentriolar material (PCM). Despite the importance of centrosomes as microtubule-organizing centers, the mechanism and regulation of PCM assembly are not well understood. In C. elegans, PCM assembly requires the coiled-coil protein SPD-5. Here we found that recombinant SPD-5 could polymerize to form micrometer-sized porous networks in vitro. Network assembly was accelerated by two conserved regulators that control PCM assembly in vivo, Polo-like kinase-1 and SPD-2/Cep192. Only the assembled SPD-5 networks, and not unassembled SPD-5 protein, functioned as a scaffold for other PCM proteins. Thus, PCM size and binding capacity emerge from the regulated polymerization of one coiled-coil protein to form a porous network.
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