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Science 3 June 1994:
Vol. 264. no. 5164, pp. 1452 - 1455
DOI: 10.1126/science.8197457

Articles

Science, Vol 264, Issue 5164, 1452-1455
Copyright © 1994 by American Association for the Advancement of Science


articles

A protein phosphatase 2C involved in ABA signal transduction in Arabidopsis thaliana

K Meyer, MP Leube, and E Grill

Institute of Plant Sciences, Swiss Federal Institute of Technology, Zurich.

The plant hormone abscisic acid (ABA) mediates various responses such as stomatal closure, the maintenance of seed dormancy, and the inhibition of plant growth. All three responses are affected in the ABA-insensitive mutant abi1 of Arabidopsis thaliana, suggesting that an early step in the signaling of ABA is controlled by the ABI1 locus. The ABI1 gene was cloned by chromosome walking, and a missense mutation was identified in the structural gene of the abi1 mutant. The ABI1 gene encodes a protein with high similarity to protein serine or threonine phosphatases of type 2C with the novel feature of a putative Ca2+ binding site. Thus, the control of the phosphorylation state of cell signaling components by the ABI1 product could mediate pleiotropic hormone responses.


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PNAS 95, 6619-6623
   Abstract »    Full Text »    PDF »
Isolation of the GA-Response Mutant sly1 as a Suppressor of ABI1-1 in Arabidopsis thaliana.
C. M. Steber, S. E. Cooney, and P. McCourt (1998)
Genetics 149, 509-521
   Abstract »    Full Text »    PDF »
The Arabidopsis Abscisic Acid Response Locus ABI4 Encodes an APETALA 2 Domain Protein.
R. R. Finkelstein, M. L. Wang, T. J. Lynch, S. Rao, and H. M. Goodman (1998)
PLANT CELL 10, 1043-1054
   Abstract »    Full Text »
Spalten, a protein containing Galpha -protein-like and PP2C domains, is essential for cell-type differentiation in Dictyostelium.
L. Aubry and R. A. Firtel (1998)
Genes & Dev. 12, 1525-1538
   Abstract »    Full Text »
Identification and Characterization of an Unusual Double Serine/Threonine Protein Phosphatase 2C in the Malaria Parasite Plasmodium falciparum.
C. B. Mamoun, D. J. Sullivan Jr., R. Banerjee, and D. E. Goldberg (1998)
J. Biol. Chem. 273, 11241-11247
   Abstract »    Full Text »    PDF »
14-3-3 Proteins Are Part of an Abscisic Acid–VIVIPAROUS1 (VP1) Response Complex in the Em Promoter and Interact with VP1 and EmBP1.
T. F. Schultz, J. Medina, A. Hill, and R. S. Quatrano (1998)
PLANT CELL 10, 837-848
   Abstract »    Full Text »    PDF »
Protein Serine/Threonine Phosphatase Ptc2p Negatively Regulates the Unfolded-Protein Response by Dephosphorylating Ire1p Kinase.
A. A. Welihinda, W. Tirasophon, S. R. Green, and R. J. Kaufman (1998)
Mol. Cell. Biol. 18, 1967-1977
   Abstract »    Full Text »
MP2C, a plant protein phosphatase 2C, functions as a negative regulator of mitogen-activated protein kinase pathways in yeast and plants.
I. Meskiene, L. Bogre, W. Glaser, J. Balog, M. Brandstotter, K. Zwerger, G. Ammerer, and H. Hirt (1998)
PNAS 95, 1938-1943
   Abstract »    Full Text »    PDF »
Mutational analysis of protein phosphatase 2C involved in abscisic acid signal transduction in higher plants.
J. Sheen (1998)
PNAS 95, 975-980
   Abstract »    Full Text »    PDF »
Calcium-Dependent Protein Phosphorylation May Mediate the Gibberellic Acid Response in Barley Aleurone.
S. Ritchie and S. Gilroy (1998)
Plant Physiology 116, 765-776
   Abstract »    Full Text »    PDF »
Inhibition of the Iron-induced ZmFer1 Maize Ferritin Gene Expression by Antioxidants and Serine/Threonine Phosphatase Inhibitors.
G. Savino, J.-F. Briat, and S. Lobreaux (1997)
J. Biol. Chem. 272, 33319-33326
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Arabidopsis NPH1: A Protein Kinase with a Putative Redox-Sensing Domain.
E. Huala, P. W. Oeller, E. Liscum, I. Han, E. Larsen, and W. R. Briggs (1997)
Science 278, 2120-2123
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Identification and characterization of a conserved family of protein serine/threonine phosphatases homologous to Drosophila retinal degeneration C (rdgC).
P. M. Sherman, H. Sun, J. P. Macke, J. Williams, P. M. Smallwood, and J. Nathans (1997)
PNAS 94, 11639-11644
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Protein Phosphatase 2C Acts Independently of Stress-activated Kinase Cascade to Regulate the Stress Response in Fission Yeast.
F. Gaits, K. Shiozaki, and P. Russell (1997)
J. Biol. Chem. 272, 17873-17879
   Abstract »    Full Text »    PDF »



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