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  Regulated assembly of a supramolecular centrosome scaffold in vitro

Woodruff, J. B., Wueseke, O., Viscardi, V., Mahamid, J., Ochoa, S. D., Bunkenborg, J., et al. (2015). Regulated assembly of a supramolecular centrosome scaffold in vitro. SCIENCE, 348(6236), 808-812. doi:10.1126/science.aaa3923.

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Woodruff, Jeffrey B.1, Autor
Wueseke, Oliver1, Autor
Viscardi, Valeria1, Autor
Mahamid, Julia2, Autor           
Ochoa, Stacy D.1, Autor
Bunkenborg, Jakob1, Autor
Widlund, Per O.1, Autor
Pozniakovsky, Andrei1, Autor
Zanin, Esther1, Autor
Bahmanyar, Shirin1, Autor
Zinke, Andrea1, Autor
Hong, Sun Hae1, Autor
Decker, Marcus1, Autor
Baumeister, Wolfgang2, Autor           
Andersen, Jens S.1, Autor
Oegema, Karen1, Autor
Hyman, Anthony A.1, Autor
Affiliations:
1external, ou_persistent22              
2Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              

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Schlagwörter: GAMMA-TUBULIN COMPLEXES; COILED-COIL DOMAINS; CENTRIOLE DUPLICATION; MITOTIC CENTROSOMES; DROSOPHILA SPD-2; ELEGANS REQUIRE; PROTEIN SPD-2; PERICENTRIN; MATURATION; PCM
 Zusammenfassung: 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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Sprache(n): eng - English
 Datum: 2015
 Publikationsstatus: Erschienen
 Seiten: 5
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: ISI: 000354428700046
DOI: 10.1126/science.aaa3923
 Art des Abschluß: -

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Titel: SCIENCE
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: 1200 NEW YORK AVE, NW, WASHINGTON, DC 20005 USA : AMER ASSOC ADVANCEMENT SCIENCE
Seiten: - Band / Heft: 348 (6236) Artikelnummer: - Start- / Endseite: 808 - 812 Identifikator: ISSN: 0036-8075