Protein Kinase and Phosphatase Regulation During Abscisic Acid Signaling and Ion Channel Regulation in Guard Cells

1998 ◽  
pp. 59-69 ◽  
Author(s):  
Julian I. Schroeder ◽  
Martin Schwarz ◽  
Zhen-Ming Pei
Keyword(s):  
Abscisic Acid ◽  
Protein Kinase ◽  
Ion Channel ◽  
Guard Cells ◽  
Ion Channel Regulation ◽  
Abscisic Acid Signaling ◽  
Channel Regulation ◽  
Phosphatase Regulation

Dual ion-channel regulation by cyclic GMP and cyclic GMP-dependent protein kinase

Nature ◽  
1990 ◽  
Vol 344 (6264) ◽  
pp. 336-339 ◽  
Author(s):  
Douglas B. Light ◽  
Jackie D. Corbin ◽  
Bruce A. Stanton
Keyword(s):  
Protein Kinase ◽  
Ion Channel ◽  
Cyclic Gmp ◽  
Dependent Protein Kinase ◽  
Ion Channel Regulation ◽  
Channel Regulation ◽  
Dependent Protein

scholarly journals Nitric oxide negatively regulates abscisic acid signaling in guard cells by S-nitrosylation of OST1

2014 ◽  
Vol 112 (2) ◽  
pp. 613-618 ◽  
Author(s):  
Pengcheng Wang ◽  
Yanyan Du ◽  
Yueh-Ju Hou ◽  
Yang Zhao ◽  
Chuan-Chih Hsu ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Abscisic Acid ◽  
Protein Kinase ◽  
Stomatal Closure ◽  
Guard Cells ◽  
Cysteine Residue ◽  
Aba Signaling ◽  
Related Protein ◽  
Abscisic Acid Signaling ◽  
Evolutionarily Conserved

The phytohormone abscisic acid (ABA) plays important roles in plant development and adaptation to environmental stress. ABA induces the production of nitric oxide (NO) in guard cells, but how NO regulates ABA signaling is not understood. Here, we show that NO negatively regulates ABA signaling in guard cells by inhibiting open stomata 1 (OST1)/sucrose nonfermenting 1 (SNF1)-related protein kinase 2.6 (SnRK2.6) through S-nitrosylation. We found that SnRK2.6 is S-nitrosylated at cysteine 137, a residue adjacent to the kinase catalytic site. Dysfunction in the S-nitrosoglutathione (GSNO) reductase (GSNOR) gene in the gsnor1-3 mutant causes NO overaccumulation in guard cells, constitutive S-nitrosylation of SnRK2.6, and impairment of ABA-induced stomatal closure. Introduction of the Cys137 to Ser mutated SnRK2.6 into the gsnor1-3/ost1-3 double-mutant partially suppressed the effect of gsnor1-3 on ABA-induced stomatal closure. A cysteine residue corresponding to Cys137 of SnRK2.6 is present in several yeast and human protein kinases and can be S-nitrosylated, suggesting that the S-nitrosylation may be an evolutionarily conserved mechanism for protein kinase regulation.

scholarly journals Assessing the Impact of Calmodulinopathic Mutations on Neuronal Ion Channel Regulation

2021 ◽  
Vol 120 (3) ◽  
pp. 155a
Author(s):  
John W. Hussey ◽  
Emily DeMarco ◽  
Deborah DiSilvestre ◽  
Helene H. Jensen ◽  
Mette Nyegaard ◽  
...  
Keyword(s):  
Ion Channel ◽  
Ion Channel Regulation ◽  
Channel Regulation ◽  
The Impact

scholarly journals Roles of intracellular hydrogen peroxide accumulation in abscisic acid signaling in Arabidopsis guard cells

2011 ◽  
Vol 168 (16) ◽  
pp. 1919-1926 ◽  
Author(s):  
Rayhanur Jannat ◽  
Misugi Uraji ◽  
Miho Morofuji ◽  
Mohammad Muzahidul Islam ◽  
Rachel E. Bloom ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Abscisic Acid ◽  
Guard Cells ◽  
Abscisic Acid Signaling ◽  
Hydrogen Peroxide Accumulation ◽  
Intracellular Hydrogen Peroxide
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