Regulated assembly of a supramolecular centrosome scaffold in vitro

J. B. Woodruff; O. Wueseke; V. Viscardi; J. Mahamid; S. D. Ochoa; J. Bunkenborg; P. O. Widlund; A. Pozniakovsky; E. Zanin; S. Bahmanyar; A. Zinke; S. H. Hong; M. Decker; W. Baumeister; J. S. Andersen; K. Oegema; A. A. Hyman

doi:10.1126/science.aaa3923

Regulated assembly of a supramolecular centrosome scaffold in vitro

J. B. Woodruff, O. Wueseke, V. Viscardi, J. Mahamid, S. D. Ochoa, J. Bunkenborg, P. O. Widlund, A. Pozniakovsky, E. Zanin, S. Bahmanyar, A. Zinke, S. H. Hong, M. Decker, W. Baumeister, J. S. Andersen, K. Oegema, A. A. Hyman

Department of Biochemistry and Molecular Biology

Copenhagen University Hospital

Research output: Contribution to journal › Journal article › Research › peer-review

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
Journal	Science
Volume	348
Issue number	6236
Pages (from-to)	808-812
ISSN	0036-8075
DOIs	https://doi.org/10.1126/science.aaa3923
Publication status	Published - 2015

Keywords

Animals
Caenorhabditis elegans Proteins/chemistry
Caenorhabditis elegans/genetics
Cell Cycle Proteins/chemistry
Centrosome/diagnostic imaging
Metabolic Networks and Pathways
Phosphorylation
Polymerization
Protein Binding
Protein Serine-Threonine Kinases/metabolism
Protein Structure, Tertiary
Proto-Oncogene Proteins/metabolism
Ultrasonography

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10.1126/science.aaa3923

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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

@article{090bda81e7e84a73bf80b5b963b238e3,

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.",

keywords = "Animals, Caenorhabditis elegans Proteins/chemistry, Caenorhabditis elegans/genetics, Cell Cycle Proteins/chemistry, Centrosome/diagnostic imaging, Metabolic Networks and Pathways, Phosphorylation, Polymerization, Protein Binding, Protein Serine-Threonine Kinases/metabolism, Protein Structure, Tertiary, Proto-Oncogene Proteins/metabolism, Ultrasonography",

author = "Woodruff, {J. B.} and O. Wueseke and V. Viscardi and J. Mahamid and Ochoa, {S. D.} and J. Bunkenborg and Widlund, {P. O.} and A. Pozniakovsky and E. Zanin and S. Bahmanyar and A. Zinke and Hong, {S. H.} and M. Decker and W. Baumeister and Andersen, {J. S.} and K. Oegema and Hyman, {A. A.}",

year = "2015",

doi = "10.1126/science.aaa3923",

language = "English",

volume = "348",

pages = "808--812",

journal = "Science",

issn = "0036-8075",

publisher = "American Association for the Advancement of Science",

number = "6236",

}

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

TY - JOUR

T1 - Regulated assembly of a supramolecular centrosome scaffold in vitro

AU - Woodruff, J. B.

AU - Wueseke, O.

AU - Viscardi, V.

AU - Mahamid, J.

AU - Ochoa, S. D.

AU - Bunkenborg, J.

AU - Widlund, P. O.

AU - Pozniakovsky, A.

AU - Zanin, E.

AU - Bahmanyar, S.

AU - Zinke, A.

AU - Hong, S. H.

AU - Decker, M.

AU - Baumeister, W.

AU - Andersen, J. S.

AU - Oegema, K.

AU - Hyman, A. A.

PY - 2015

Y1 - 2015

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.

KW - Animals

KW - Caenorhabditis elegans Proteins/chemistry

KW - Caenorhabditis elegans/genetics

KW - Cell Cycle Proteins/chemistry

KW - Centrosome/diagnostic imaging

KW - Metabolic Networks and Pathways

KW - Phosphorylation

KW - Polymerization

KW - Protein Binding

KW - Protein Serine-Threonine Kinases/metabolism

KW - Protein Structure, Tertiary

KW - Proto-Oncogene Proteins/metabolism

KW - Ultrasonography

U2 - 10.1126/science.aaa3923

DO - 10.1126/science.aaa3923

M3 - Journal article

C2 - 25977552

SN - 0036-8075

VL - 348

SP - 808

EP - 812

JO - Science

JF - Science

IS - 6236

ER -

Regulated assembly of a supramolecular centrosome scaffold in vitro

Abstract

Keywords

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