Phosphorylation by cyclin B-Cdk underlies release of mitotic exit activator Cdc14 from the nucleolus

Science

Volumn 305, Issue 5683, 2004, Pages 516-519

  Azzam, Ramzi ^a   Chen, Susan L ^b   Shou, Wenying ^a   Mah, Angie S ^a   Alexandru, Gabriela ^a,c   Nasmyth, Kim ^c   Annan, Roland S ^b   Carr, Steven A ^b,d   Deshaies, Raymond J ^a  

^a CALIFORNIA INSTITUTE OF TECHNOLOGY   (United States)

^b GLAXOSMITHKLINE   (United States)

^c RESEARCH INSTITUTE OF MOLECULAR PATHOLOGY   (Austria)

^d BROAD INSTITUTE OF MIT AND HARVARD   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; CHROMOSOMES; GROWTH KINETICS; MICROBIOLOGY; PROTEINS;

CELL DIVISIONS; MITOSIS; PHOSPHORYLATION;

YEAST;

CELL CYCLE PROTEIN; CELL CYCLE PROTEIN 14; CYCLIN B; CYCLIN B1; CYCLIN B2; CYCLIN DEPENDENT KINASE; NET1 PROTEIN; PHOSPHOPROTEIN PHOSPHATASE; PROTEIN; UNCLASSIFIED DRUG;

BIOLOGY;

ANAPHASE; ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; ENZYME PHOSPHORYLATION; INTERPHASE; MITOSIS; NONHUMAN; NUCLEOLUS; PRIORITY JOURNAL; PROTEIN SECRETION; REGULATORY MECHANISM; YEAST;

ANAPHASE; CELL CYCLE PROTEINS; CELL NUCLEOLUS; CYCLIN B; CYCLIN-DEPENDENT KINASES; DNA, RIBOSOMAL; MEIOSIS; METAPHASE; MITOSIS; MUTATION; NUCLEAR PROTEINS; PHOSPHORYLATION; PROTEIN KINASES; PROTEIN-TYROSINE-PHOSPHATASE; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

SACCHAROMYCETALES;

EID: 3242760516     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1099402     Document Type: Article

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24. We thank J. Huangh for the Net1 1-621 construct; I. Lesur for help with elutriation; D. Kellogg for antibody to Clb2; K. Shokat for NaPP1 analog; the Morgan, Amon, and Holloway labs for various strains and GAL1p-CLB2 mutant constructs; M. Olson, for the Clb2-MBP bacterial construct; R. Verma for preparing the Baculo (GST-Cdc28-HA) virus; M. Petroski for purified Clb5-Cdk; J. Sanders for mugenesis efforts; and members of the Deshaies lab for critical comments during the course of this work. Supported by NIH grant GM59940 (R.J.D.) and by fellowships from the Norris and Baxter foundations (R.A.). R.J.D. is an Assistant Investigator of the Howard Hughes Medical Institute. Molecular interaction data have been deposited in the Biomolecular interaction Network Database with accession codes 145590 and 145624.