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Regulated assembly of a supramolecular centrosome scaffold in vitro

Woodruff, J. B. (author)
Wueseke, O. (author)
Viscardi, V. (author)
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Mahamid, J. (author)
Ochoa, S. D. (author)
Bunkenborg, J. (author)
Widlund, Per O (author)
Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology
Pozniakovsky, A. (author)
Zanin, E. (author)
Bahmanyar, S. (author)
Zinke, A. (author)
Hong, S. H. (author)
Decker, M. (author)
Baumeister, W. (author)
Andersen, J. S. (author)
Oegema, K. (author)
Hyman, A. A. (author)
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 (creator_code:org_t)
2015-05-14
2015
English.
In: Science. - : American Association for the Advancement of Science (AAAS). - 0036-8075 .- 1095-9203. ; 348:6236, s. 808-812
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • 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 Caenorhabditis elegans, PCM assembly requires the coiled-coil protein SPD-5.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.

Subject headings

MEDICIN OCH HÄLSOVETENSKAP  -- Medicinska och farmaceutiska grundvetenskaper -- Andra medicinska och farmaceutiska grundvetenskaper (hsv//swe)
MEDICAL AND HEALTH SCIENCES  -- Basic Medicine -- Other Basic Medicine (hsv//eng)

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