A decade of Cdc14--a personal perspective. Delivered on 9 July 2007 at the 32nd FEBS Congress in Vienna, Austria.
In budding yeast, the protein phosphatase Cdc14 is a key regulator of late mitotic events. Research over the last decade has revealed many of its functions and today we know that this protein phosphatase orchestrates several aspects of chromosome segregation and is the key trigger of exit from mitosis. Elucidation of the mechanisms controlling Cdc14 activity through nucleolar sequestration now serves as a paradigm for how regulation of the subcellular localization of proteins regulates protein function. Here I review these findings focusing on how discoveries in my laboratory helped elucidate the function and regulation of Cdc14.
Amon
Angelika
A
David H. Koch Institute for Integrative Cancer Research, Cambridge, MA, USA. angelika@mit.edu
D000705:Anaphase / Q000502:physiology; D018797:Cell Cycle Proteins / Q000378:metabolism*; D002466:Cell Nucleolus / Q000378:metabolism / Q000502:physiology; D020090:Chromosome Segregation / Q000502:physiology; D019926:Cyclin B / Q000378:metabolism; D018844:Cyclin-Dependent Kinases / Q000378:metabolism; D008677:Metaphase / Q000502:physiology; D008938:Mitosis / Q000502:physiology*; D008954:Models, Biological; D017027:Protein Tyrosine Phosphatases / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*
C074860:CDC14 protein, S cerevisiae; C093749:CLB2 protein, S cerevisiae; D018797:Cell Cycle Proteins; D019926:Cyclin B; D029701:Saccharomyces cerevisiae Proteins; D018844:Cyclin-Dependent Kinases; D017027:Protein Tyrosine Phosphatases