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Substrate specificity analysis of protein kinase complex Dbf2-Mob1 by peptide library and proteome array screening |
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| Authors: | Angie?S?Mah Andrew?EH?Elia Geeta?Devgan Jason?Ptacek Mike?Schutkowski Michael?Snyder Michael?B?Yaffe |
| Institution: | (1) Department of Biology, California Institute of Technology, Pasadena, CA 91125, USA;(2) Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA;(3) Center for Cancer Research, Massachusetts Institute of Technology, Cambridge, MA 02139, USA;(4) Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA;(5) Division of Biological Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USA;(6) Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520, USA;(7) Department of Molecular Biophysics & Biochemistry, Yale University, New Haven, CT 06520, USA;(8) JPT Peptide Technologies GmbH, Invalidenstrasse 130, 10115 Berlin, Germany, USA |
| Abstract: | BackgroundThe mitotic exit network (MEN) is a group of proteins that form a signaling cascade that is essential for cells to exit mitosis in Saccharomyces cerevisiae. The MEN has also been implicated in playing a role in cytokinesis. Two components of this signaling pathway are the protein kinase Dbf2 and its binding partner essential for its kinase activity, Mob1. The components of MEN that act upstream of Dbf2-Mob1 have been characterized, but physiological substrates for Dbf2-Mob1 have yet to be identified. |
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