title: Detection of Phosphorylation Status of Cytokinetic Components.
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.
authors.affiliation: DKFZ-ZMBH Alliance, German Cancer Research Center (DKFZ), University of Heidelberg, Im Neuenheimer Feld 581, Heidelberg, 69120, Germany.|Ludwig Institute for Cancer Research, 9500 Gilman Drive, CMM East, La Jolla, CA, 92093, USA.
authors.forename: Franz
authors.initials: F
authors.lastname: Meitinger
authors.affiliation: Division of Biomedical Cell Biology, Warwick Medical School, University of Warwick, Gibbet Hill Road, Coventry, CV4 7AL, UK.
authors.forename: Saravanan
authors.initials: S
authors.lastname: Palani
authors.affiliation: DKFZ-ZMBH Alliance, German Cancer Research Center (DKFZ), University of Heidelberg, Im Neuenheimer Feld 581, Heidelberg, 69120, Germany. g.pereira@dkfz-heidelberg.de.
authors.forename: Gislene
authors.initials: G
authors.lastname: Pereira
mesh_terms: D015153:Blotting, Western; D002453:Cell Cycle; D048749:Cytokinesis; D004591:Electrophoresis, Polyacrylamide Gel; D005656:Fungal Proteins / Q000378:metabolism*; D010766:Phosphorylation
chemical_list: D005656:Fungal Proteins
keywords: Cdc5; Cdk1; Cell cycle synchronization; Cytokinesis; Dbf2; Kinase; Mitotic exit network (MEN); Phosphatase; Phosphorylation; SDS-PAGE; Yeast