Regulated assembly of a supramolecular centrosome scaffold in vitro

Jeffrey B. Woodruff; Oliver Wueseke; Valeria Viscardi; Julia Mahamid; Stacy D. Ochoa; Jakob Bunkenborg; Per O. Widlund; Andrei Pozniakovsky; Esther Zanin; Shirin Bahmanyar; Andrea Zinke; Sun Hae Hong; Marcus Decker; Wolfgang Baumeister; Jens S. Andersen; Karen Oegema; Anthony A. Hyman

doi:10.1126/science.aaa3923

Regulated assembly of a supramolecular centrosome scaffold in vitro

Jeffrey B. Woodruff, Oliver Wueseke, Valeria Viscardi, Julia Mahamid, Stacy D. Ochoa, Jakob Bunkenborg, Per O. Widlund, Andrei Pozniakovsky, Esther Zanin, Shirin Bahmanyar, Andrea Zinke, Sun Hae Hong, Marcus Decker, Wolfgang Baumeister, Jens S. Andersen, Karen Oegema, Anthony A. Hyman

Research output: Contribution to journal › Article › peer-review

127 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	808-812
Number of pages	5
Journal	Science
Volume	348
Issue number	6236
DOIs	https://doi.org/10.1126/science.aaa3923
State	Published - May 15 2015
Externally published	Yes

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Woodruff, J. B., Wueseke, O., Viscardi, V., Mahamid, J., Ochoa, S. D., Bunkenborg, J., Widlund, P. O., Pozniakovsky, A., Zanin, E., Bahmanyar, S., Zinke, A., Hong, S. H., Decker, M., Baumeister, W., Andersen, J. S., Oegema, K., & Hyman, A. A. (2015). Regulated assembly of a supramolecular centrosome scaffold in vitro. Science, 348(6236), 808-812. https://doi.org/10.1126/science.aaa3923

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 2015, 'Regulated assembly of a supramolecular centrosome scaffold in vitro', Science, vol. 348, no. 6236, pp. 808-812. https://doi.org/10.1126/science.aaa3923

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title = "Regulated assembly of a supramolecular centrosome scaffold in vitro",

abstract = "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.",

author = "Woodruff, {Jeffrey B.} and Oliver Wueseke and Valeria Viscardi and Julia Mahamid and Ochoa, {Stacy D.} and Jakob Bunkenborg and Widlund, {Per O.} and Andrei Pozniakovsky and Esther Zanin and Shirin Bahmanyar and Andrea Zinke and Hong, {Sun Hae} and Marcus Decker and Wolfgang Baumeister and Andersen, {Jens S.} and Karen Oegema and Hyman, {Anthony A.}",

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AU - Woodruff, Jeffrey B.

AU - Wueseke, Oliver

AU - Viscardi, Valeria

AU - Mahamid, Julia

AU - Ochoa, Stacy D.

AU - Bunkenborg, Jakob

AU - Widlund, Per O.

AU - Pozniakovsky, Andrei

AU - Zanin, Esther

AU - Bahmanyar, Shirin

AU - Zinke, Andrea

AU - Hong, Sun Hae

AU - Decker, Marcus

AU - Baumeister, Wolfgang

AU - Andersen, Jens S.

AU - Oegema, Karen

AU - Hyman, Anthony A.

PY - 2015/5/15

Y1 - 2015/5/15

N2 - 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.

AB - 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.

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Regulated assembly of a supramolecular centrosome scaffold in vitro

Abstract

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