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Science 22 July 1994:
Vol. 265. no. 5171, pp. 533 - 535
DOI: 10.1126/science.8036497

Articles

Science, Vol 265, Issue 5171, 533-535
Copyright © 1994 by American Association for the Advancement of Science


articles

14-3-3 protein homologs required for the DNA damage checkpoint in fission yeast

JC Ford, F al-Khodairy, E Fotou, KS Sheldrick, DJ Griffiths, and AM Carr

Research Centre, King Faisal Specialist Hospital, Riyadh, Saudi Arabia.

During the cell cycle, DNA is replicated and segregated equally into two daughter cells. The DNA damage checkpoint ensures that DNA damage is repaired before mitosis is attempted. Genetic studies of the fission yeast Schizosaccharomyces pombe have identified two genes, rad24 and rad25, that are required for this checkpoint. These genes encode 14-3-3 protein homologs that together provide a function that is essential for cell proliferation. In addition, S. pombe rad24 null mutants, and to a lesser extent rad25 null mutants, enter mitosis prematurely, which indicates that 14-3-3 proteins have a role in determining the timing of mitosis.


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14-3-3zeta Binds a Phosphorylated Raf Peptide and an Unphosphorylated Peptide via Its Conserved Amphipathic Groove.
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   Abstract »    Full Text »    PDF »
14-3-3 Proteins Interact with Specific MEK Kinases.
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   Abstract »    Full Text »    PDF »
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   Abstract »    Full Text »
Damage and replication checkpoint control in fission yeast is ensured by interactions of Crb2, a protein with BRCT motif, with Cut5 and Chk1.
Y. Saka, F. Esashi, T. Matsusaka, S. Mochida, and M. Yanagida (1997)
Genes & Dev. 11, 3387-3400
   Abstract »    Full Text »    PDF »
14-3-3 Is Phosphorylated by Casein Kinase I on Residue 233. PHOSPHORYLATION AT THIS SITE IN VIVO REGULATES Raf/14-3-3 INTERACTION.
T. Dubois, C. Rommel, S. Howell, U. Steinhussen, Y. Soneji, N. Morrice, K. Moelling, and A. Aitken (1997)
J. Biol. Chem. 272, 28882-28888
   Abstract »    Full Text »    PDF »
Interference of BAD (Bcl-xL/Bcl-2-Associated Death Promoter)-Induced Apoptosis in Mammalian Cells by 14-3-3 Isoforms and P11.
S. Y. Hsu, A. Kaipia, L. Zhu, and A. J. W. Hsueh (1997)
Mol. Endocrinol. 11, 1858-1867
   Abstract »    Full Text »
Interaction of Phosphorylated Tryptophan Hydroxylase with 14-3-3 Proteins.
U. Banik, G.-A. Wang, P. D. Wagner, and S. Kaufman (1997)
J. Biol. Chem. 272, 26219-26225
   Abstract »    Full Text »    PDF »
14-3-3 Protein Binds to Insulin Receptor Substrate-1, One of the Binding Sites of Which Is in the Phosphotyrosine Binding Domain.
T. Ogihara, T. Isobe, T. Ichimura, M. Taoka, M. Funaki, H. Sakoda, Y. Onishi, K. Inukai, M. Anai, Y. Fukushima, et al. (1997)
J. Biol. Chem. 272, 25267-25274
   Abstract »    Full Text »    PDF »
14-3-3 Inhibits the Dictyostelium Myosin II Heavy-Chain-specific Protein Kinase C Activity by a Direct Interaction: Identification of the 14-3-3 Binding Domain.
M. Matto-Yelin, A. Aitken, and S. Ravid (1997)
Mol. Biol. Cell 8, 1889-1899
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Raf-1 Kinase and Exoenzyme S Interact with 14-3-3zeta through a Common Site Involving Lysine 49.
L. Zhang, H. Wang, D. Liu, R. Liddington, and H. Fu (1997)
J. Biol. Chem. 272, 13717-13724
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Interaction of the Ligand-activated Glucocorticoid Receptor with the 14-3-3eta Protein.
H. Wakui, A. P.H. Wright, J.-A. Gustafsson, and J. Zilliacus (1997)
J. Biol. Chem. 272, 8153-8156
   Abstract »    Full Text »    PDF »
Cdc2 tyrosine phosphorylation is required for the DNA damage checkpoint in fission yeast..
N Rhind, B Furnari, and P Russell (1997)
Genes & Dev. 11, 504-511
   Abstract »    PDF »
The Drosophila 14-3-3 protein Leonardo enhances Torso signaling through D-Raf in a Ras 1-dependent manner.
W Li, E. Skoulakis, R. Davis, and N Perrimon (1997)
Development 124, 4163-4171
   Abstract »    PDF »
RAD9 and DNA polymerase epsilon form parallel sensory branches for transducing the DNA damage checkpoint signal in Saccharomyces cerevisiae..
T A Navas, Y Sanchez, and S J Elledge (1996)
Genes & Dev. 10, 2632-2643
   Abstract »    PDF »
14-3-3 Proteins Associate with A20 in an Isoform-specific Manner and Function Both as Chaperone and Adapter Molecules.
C. Vincenz and V. M. Dixit (1996)
J. Biol. Chem. 271, 20029-20034
   Abstract »    Full Text »    PDF »
14-3-3 epsilon has no homology to LIS1 and lies telomeric to it on chromosome 17p13.3 outside the Miller-Dieker syndrome chromosome region..
S S Chong, A Tanigami, A V Roschke, and D H Ledbetter (1996)
Genome Res. 6, 735-741
   Abstract »    PDF »
Identification of a Binding Sequence for the 14-3-3 Protein within the Cytoplasmic Domain of the Adhesion Receptor, Platelet Glycoprotein Ibalpha.
X. Du, J. E. Fox, and S. Pei (1996)
J. Biol. Chem. 271, 7362-7367
   Abstract »    Full Text »    PDF »
Raf-1 Is Activated during Mitosis.
A. D. Laird, S. J. Taylor, M. Oberst, and D. Shalloway (1995)
J. Biol. Chem. 270, 26742-26745
   Abstract »    Full Text »    PDF »
14-3-3 alpha and [IMAGE] Are the Phosphorylated Forms of Raf-activating 14-3-3 beta and [IMAGE].
A. Aitken, S. Howell, D. Jones, J. Madrazo, and Y. Patel (1995)
J. Biol. Chem. 270, 5706-5709
   Abstract »    Full Text »    PDF »
The Schizosaccharomyces pombe hus5 gene encodes a ubiquitin conjugating enzyme required for normal mitosis.
F al-Khodairy, T Enoch, I. Hagan, and A. Carr (1995)
J. Cell Sci. 108, 475-486
   Abstract »    PDF »
14-3-3: modulators of signaling proteins?.
D Morrison (1994)
Science 266, 56-57
   PDF »
Interaction of the protein kinase Raf-1 with 14-3-3 proteins.
H Fu, K Xia, D. Pallas, C Cui, K Conroy, R. Narsimhan, H Mamon, R. Collier, and T. Roberts (1994)
Science 266, 126-129
   Abstract »    PDF »
Association of the protein kinases c-Bcr and Bcr-Abl with proteins of the 14-3-3 family.
G. Reuther, H Fu, L. Cripe, R. Collier, and A. Pendergast (1994)
Science 266, 129-133
   Abstract »    PDF »
Association of polyomavirus middle tumor antigen with 14-3-3 proteins.
D. Pallas, H Fu, L. Haehnel, W Weller, R. Collier, and T. Roberts (1994)
Science 265, 535-537
   Abstract »    PDF »
Proteins of the 14-3-3 Family Associate with Raf and Contribute to Its Activation.
E. Freed, F. McCormick, and R. Ruggieri (1994)
Cold Spring Harb Symp Quant Biol 59, 187-193
   Abstract »    PDF »
Calyculin A-induced Vimentin Phosphorylation Sequesters 14-3-3 and Displaces Other 14-3-3 Partners in Vivo.
G. Tzivion, Z.-J. Luo, and J. Avruch (2000)
J. Biol. Chem. 275, 29772-29778
   Abstract »    Full Text »    PDF »
Signal Transduction by the CEACAM1 Tumor Suppressor. PHOSPHORYLATION OF SERINE 503 IS REQUIRED FOR GROWTH-INHIBITORY ACTIVITY.
V. T. Estrera, D.-T. Chen, W. Luo, D. C. Hixson, and S.-H. Lin (2001)
J. Biol. Chem. 276, 15547-15553
   Abstract »    Full Text »    PDF »
14-3-3 Proteins Mediate an Essential Anti-apoptotic Signal.
S. C. Masters and H. Fu (2001)
J. Biol. Chem. 276, 45193-45200
   Abstract »    Full Text »    PDF »
Association of the Cyclin-dependent Kinases and 14-3-3 Sigma Negatively Regulates Cell Cycle Progression.
C. Laronga, H.-Y. Yang, C. Neal, and M.-H. Lee (2000)
J. Biol. Chem. 275, 23106-23112
   Abstract »    Full Text »    PDF »
Serine-345 is required for Rad3-dependent phosphorylation and function of checkpoint kinase Chk1 in fission yeast.
A. Lopez-Girona, K. Tanaka, X.-B. Chen, B. A. Baber, C. H. McGowan, and P. Russell (2001)
PNAS 98, 11289-11294
   Abstract »    Full Text »    PDF »



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