Detection of phosphorylation status of cytokinetic components

• Verfasst von: Meitinger, Franz [VerfasserIn]
• Verfasst von: Palani, Saravanan [VerfasserIn]
• Verfasst von: Pereira, Gislene [VerfasserIn]
• Titel: Detection of phosphorylation status of cytokinetic components
• Verf.angabe: Franz Meitinger, Saravanan Palani, and Gislene Pereira
• Jahr: 2016
• Umfang: 19 S.
• Teil: year:2016
• Teil: pages:219-237
• Teil: extent:19
• Fussnoten: Gesehen am 22.05.2017
• Titel Quelle: Enthalten in: Yeast Cytokinesis
• Ausgabe Quelle: 1st ed. 2016
• Ort Quelle: New York, NY : Humana Press, 2016
• Jahr Quelle: 2016
• Band/Heft Quelle: (2016), Seite 219-237
• ISBN Quelle: 978-1-4939-3145-3
• DOI: doi:10.1007/978-1-4939-3145-3_16
• Datenträger: Online-Ressource
• Sprache: eng
• Sach-SW: Cdc5
• Sach-SW: Cdk1
• Sach-SW: Cell cycle synchronization
• Sach-SW: Cytokinesis
• Sach-SW: Dbf2
• Sach-SW: Kinase
• Sach-SW: Mitotic exit network (MEN)
• Sach-SW: Phosphatase
• Sach-SW: Phosphorylation
• Sach-SW: SDS-PAGE
• Sach-SW: Yeast
• K10plus-PPN: 1558842330

Abstract

Yeast cells can be easily cultured, synchronized, and genetically modified making them a convenient model system to study molecular mechanisms underlying cytokinesis. Here, we describe simple methods that allow the analysis of the phosphorylation profile of cytokinetic proteins, both in vivo and in vitro, using standard laboratory equipment. In addition, we compare the ability of three different, standard, and optimized acrylamide gel conditions to separate phosphorylated forms, using the protein Inn1 as an example.