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Verfasst von:Meitinger, Franz [VerfasserIn]   i
 Pereira, Gislene [VerfasserIn]   i
Titel:Dual function of the NDR-kinase Dbf2 in the regulation of the F-BAR protein Hof1 during cytokinesis
Verf.angabe:Franz Meitinger, Saravanan Palani, Birgit Hub, and Gislene Pereira
E-Jahr:2013
Jahr:February 27, 2013
Umfang:15 S.
Fussnoten:Gesehen am 15.05.2017
Titel Quelle:Enthalten in: Molecular biology of the cell
Ort Quelle:Bethesda, Md. : American Society for Cell Biology, 1992
Jahr Quelle:2013
Band/Heft Quelle:24(2013), 9, Seite 1290-1304
ISSN Quelle:1939-4586
Abstract:The conserved NDR-kinase Dbf2 plays a critical role in cytokinesis in budding yeast. Among its cytokinesis-related substrates is the F-BAR protein Hof1. Hof1 colocalizes at the cell division site with the septin complex and, as mitotic exit progresses, moves to the actomyosin ring (AMR). Neither the function of Hof1 at the septin complex nor the mechanism by which Hof1 supports AMR constriction is understood. Here we establish that Dbf2 has a dual function in Hof1 regulation. First, we show that the coiled-coil region, which is adjacent to the conserved F-BAR domain, is required for the binding of Hof1 to septins. The Dbf2-dependent phosphorylation of Hof1 at a single serine residue (serine 313) in this region diminishes the recruitment of Hof1 to septins both in vitro and in vivo. Genetic and functional analysis indicates that the binding of Hof1 to septins is important for septin rearrangement and integrity during cytokinesis. Furthermore, Dbf2 phosphorylation of Hof1 at serines 533 and 563 promotes AMR constriction most likely by inhibiting the SH3-domain-dependent interactions of Hof1. Thus our data show that Dbf2 coordinates septin and AMR functions during cytokinesis through the regulation/control of Hof1.
DOI:doi:10.1091/mbc.E12-08-0608
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

kostenfrei: Volltext: http://dx.doi.org/10.1091/mbc.E12-08-0608
 kostenfrei: Volltext: http://www.molbiolcell.org/content/24/9/1290
 DOI: https://doi.org/10.1091/mbc.E12-08-0608
Datenträger:Online-Ressource
Sprache:eng
K10plus-PPN:1558605118
Verknüpfungen:→ Zeitschrift

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