Centrosomes. Regulated assembly of a supramolecular centrosome scaffold in vitro

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...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2015-05, Vol.348 (6236), p.808-812
Main Authors: Woodruff, Jeffrey B, Wueseke, Oliver, Viscardi, Valeria, Mahamid, Julia, Ochoa, Stacy D, Bunkenborg, Jakob, Widlund, Per O, Pozniakovsky, Andrei, Zanin, Esther, Bahmanyar, Shirin, Zinke, Andrea, Hong, Sun Hae, Decker, Marcus, Baumeister, Wolfgang, Andersen, Jens S, Oegema, Karen, Hyman, Anthony A
Format: Article
Language:English
Subjects:
Animals
Caenorhabditis elegans - genetics
Caenorhabditis elegans - metabolism
Caenorhabditis elegans Proteins - chemistry
Caenorhabditis elegans Proteins - genetics
Caenorhabditis elegans Proteins - metabolism
Cell Cycle Proteins - chemistry
Cell Cycle Proteins - genetics
Cell Cycle Proteins - metabolism
Centrosome - diagnostic imaging
Centrosome - metabolism
Metabolic Networks and Pathways
Phosphorylation
Polo-Like Kinase 1
Polymerization
Protein Binding
Protein Serine-Threonine Kinases - metabolism
Protein Structure, Tertiary
Proto-Oncogene Proteins - metabolism
Ultrasonography
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Summary: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.
ISSN:1095-9203
DOI:10.1126/science.aaa3923