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Mol. Cells 2012; 34(3): 271-278

Published online September 30, 2012

https://doi.org/10.1007/s10059-012-0092-4

© The Korean Society for Molecular and Cellular Biology

Soybean MAPK, GMK1 Is Dually Regulated by Phosphatidic Acid and Hydrogen Peroxide and Translocated to Nucleus during Salt Stress

Jong Hee Im1, Hyoungseok Lee1,2, Jitae Kim1,3, Ho Bang Kim1,4, and Chung Sun An1,*

1School of Biological Sciences, College of Natural Sciences, Seoul National University, Seoul 151-747, Korea, 2Present address: Division of Life Sciences, Korea Polar Research Institute (KOPRI), Songdo Techno Park, Incheon 406-840, Korea, 3Present address: Department of Plant Biology, Cornell University, Ithaca, New York, 14853, USA, 4Present address: Life Sciences Research Institute, Biomedic Co. Ltd., Bucheon 420-852, Korea

Correspondence to : *Correspondence: ancs@snu.ac.kr

Received: March 26, 2012; Revised: May 7, 2012; Accepted: June 19, 2012

Abstract

Mitogen-activated protein kinase (MAPK) is activated by various biotic and abiotic stresses. Salt stress induces two well-characterized MAPK activating signaling molecules, phosphatidic acid (PA) via phospholipase D and phospholipase C, and reactive oxygen species (ROS) via nicotinamide adenine dinucleotide phosphate (NADPH)-oxidase. In our previous study, the activity of soybean MAPK, GMK1 was strongly induced within 5 min of 300 mM NaCl treatment and this early activity was regulated by PA. In this study, we focused on the regulation of GMK1 at the later stage of the salt stress, because its activity was strongly persistent for up to 30 min. H2O2 activated GMK1 even in the presence of PA generation inhibitors, but GMK1 activity was greatly decreased in the presence of diphenyleneiodonium, an inhibitor of NADPH-oxidase after 5 min of the treatment. On the contrary, the n-butanol and neomycin reduced GMK1 activity within 5 min of the treatment. Thus, GMK1 activity may be sustained by H2O2 10 min after the treatment. Further, GMK1 was translocated into the nucleus 60 min after NaCl treatment. In the relationship between GMK1 and ROS generation, ROS generation was reduced by SB202190, a MAPK inhibitor, but was increased in protoplast overexpressing TESD-GMKK1. However, these effects were occurred at prolonged time of NaCl treatment. These data suggest that GMK1 indirectly regulates ROS generation. Taken together, we propose that soybean GMK1 is dually regulated by PA and H2O2 at a time dependant manner and translocated to the nucleus by the salt stress signal.

Keywords GMK1, hydrogen peroxide, phosphatidic acid, salt stress, soybean

Article

Research Article

Mol. Cells 2012; 34(3): 271-278

Published online September 30, 2012 https://doi.org/10.1007/s10059-012-0092-4

Copyright © The Korean Society for Molecular and Cellular Biology.

Soybean MAPK, GMK1 Is Dually Regulated by Phosphatidic Acid and Hydrogen Peroxide and Translocated to Nucleus during Salt Stress

Jong Hee Im1, Hyoungseok Lee1,2, Jitae Kim1,3, Ho Bang Kim1,4, and Chung Sun An1,*

1School of Biological Sciences, College of Natural Sciences, Seoul National University, Seoul 151-747, Korea, 2Present address: Division of Life Sciences, Korea Polar Research Institute (KOPRI), Songdo Techno Park, Incheon 406-840, Korea, 3Present address: Department of Plant Biology, Cornell University, Ithaca, New York, 14853, USA, 4Present address: Life Sciences Research Institute, Biomedic Co. Ltd., Bucheon 420-852, Korea

Correspondence to:*Correspondence: ancs@snu.ac.kr

Received: March 26, 2012; Revised: May 7, 2012; Accepted: June 19, 2012

Abstract

Mitogen-activated protein kinase (MAPK) is activated by various biotic and abiotic stresses. Salt stress induces two well-characterized MAPK activating signaling molecules, phosphatidic acid (PA) via phospholipase D and phospholipase C, and reactive oxygen species (ROS) via nicotinamide adenine dinucleotide phosphate (NADPH)-oxidase. In our previous study, the activity of soybean MAPK, GMK1 was strongly induced within 5 min of 300 mM NaCl treatment and this early activity was regulated by PA. In this study, we focused on the regulation of GMK1 at the later stage of the salt stress, because its activity was strongly persistent for up to 30 min. H2O2 activated GMK1 even in the presence of PA generation inhibitors, but GMK1 activity was greatly decreased in the presence of diphenyleneiodonium, an inhibitor of NADPH-oxidase after 5 min of the treatment. On the contrary, the n-butanol and neomycin reduced GMK1 activity within 5 min of the treatment. Thus, GMK1 activity may be sustained by H2O2 10 min after the treatment. Further, GMK1 was translocated into the nucleus 60 min after NaCl treatment. In the relationship between GMK1 and ROS generation, ROS generation was reduced by SB202190, a MAPK inhibitor, but was increased in protoplast overexpressing TESD-GMKK1. However, these effects were occurred at prolonged time of NaCl treatment. These data suggest that GMK1 indirectly regulates ROS generation. Taken together, we propose that soybean GMK1 is dually regulated by PA and H2O2 at a time dependant manner and translocated to the nucleus by the salt stress signal.

Keywords: GMK1, hydrogen peroxide, phosphatidic acid, salt stress, soybean

Mol. Cells
Aug 31, 2022 Vol.45 No.8, pp. 513~602
COVER PICTURE
Cryo-EM structure of human porphyrin transporter ABCB6 (main figure) shows that binding of hemin (inset, magenta) in concert with two glutathione molecules (cyan) primes ABCB6 for high ATP turnover (Kim et al., pp. 575-587).

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