Faculty Profiles - MUNEMASA Shintaro

Reactive Carbonyl Species Mediate ABA Signaling in Guard Cells Reviewed International coauthorship International journal

Md. Moshiul Islam, Wenxiu Ye, Daiki Matsushima, Shintaro Munemasa, Eiji Okuma, Yoshimasa Nakamura, Sanaullah Biswas, Jun’ichi Mano, Yoshiyuki Murata

Plant and Cell Physiology 57 ( 12 ) 2552 - 2563 2016.12

L-Met Activates Arabidopsis GLR Ca2+ Channels Upstream of ROS Production and Regulates Stomatal Movement Reviewed International coauthorship International journal

Dongdong Kong, Heng-Cheng Hu, Eiji Okuma, Yuree Lee, Hui Sun Lee, Shintaro Munemasa, Daeshik Cho, Chuanli Ju, Leah Pedoeim, Barbara Rodriguez, Juan Wang, Wonpil Im, Yoshiyuki Murata, Zhen-Ming Pei, June M. Kwak

Cell Reports 17 ( 10 ) 2553 - 2561 2016.12

Calcium and EGTA Alleviate Cadmium Toxicity in Germinating Chickpea Seeds Reviewed International coauthorship International journal

Lamia Sakouhi, Sondès Rahoui, Marouane Ben Massoud, Shintaro Munemasa, Ezzeddine EL Ferjani, Yoshiyuki Murata, Abdelilah Chaoui

Journal of Plant Growth Regulation 35 ( 4 ) 1064 - 1073 2016.12

A novel tag-free probe for targeting molecules interacting with a flavonoid catabolite Reviewed International coauthorship International journal

Sayaka Nakashima, Zhe Liu, Yuya Yamaguchi, Shunya Saiki, Shintaro Munemasa, Toshiyuki Nakamura, Yoshiyuki Murata, Yoshimasa Nakamura

Biochemistry and Biophysics Reports 7 240 - 245 2016.9

Involvement of OST1 Protein Kinase and PYR/PYL/RCAR Receptors in Methyl Jasmonate-Induced Stomatal Closure in Arabidopsis Guard Cells Reviewed International coauthorship International journal

Ye Yin, Yuji Adachi, Yoshimasa Nakamura, Shintaro Munemasa, Izumi C. Mori, Yoshiyuki Murata

Plant and Cell Physiology 57 ( 8 ) 1779 - 1790 2016.8

Galloylated Catechins as Potent Inhibitors of Angiotensin Converting Enzyme Reviewed International coauthorship International journal

Zhe Liu, Toshiyuki Nakamura, Shintaro Munemasa, Yoshiyuki Murata, Yoshimasa Nakamura

Food Science and Technology Research 22 ( 6 ) 847 - 851 2016

Mechanisms of abscisic acid-mediated control of stomatal aperture Invited Reviewed International coauthorship International journal

Shintaro Munemasa, Felix Hauser, Jiyoung Park, Rainer Waadt, Benjamin Brandt, Julian I Schroeder

Current Opinion in Plant Biology 28 154 - 162 2015.12

Identification of Open Stomata1-Interacting Proteins Reveals Interactions with Sucrose Non-fermenting1-Related Protein Kinases2 and with Type 2A Protein Phosphatases That Function in Abscisic Acid Responses Reviewed International coauthorship International journal

Rainer Waadt, Bianca Manalansan, Navin Rauniyar, Shintaro Munemasa, Matthew A. Booker, Benjamin Brandt, Christian Waadt, Dmitri A. Nusinow, Steve A. Kay, Hans-Henning Kunz, Karin Schumacher, Alison DeLong, John R. Yates, Julian I. Schroeder

Plant Physiology 169 ( 1 ) 760 - 779 2015.9

Calcium specificity signaling mechanisms in abscisic acid signal transduction in Arabidopsis guard cells Reviewed International coauthorship International journal

Benjamin Brandt, Shintaro Munemasa, Cun Wang, Desiree Nguyen, Taiming Yong, Paul G Yang, Elly Poretsky, Thomas F Belknap, Rainer Waadt, Fernando Alemán, Julian I Schroeder

eLife 4 e03599 2015.7

Authorship：Lead author Language：English Publishing type：Research paper (scientific journal) Publisher：eLife Sciences Publications, Ltd

A central question is how specificity in cellular responses to the eukaryotic second messenger Ca2+ is achieved. Plant guard cells, that form stomatal pores for gas exchange, provide a powerful system for in depth investigation of Ca2+-signaling specificity in plants. In intact guard cells, abscisic acid (ABA) enhances (primes) the Ca2+-sensitivity of downstream signaling events that result in activation of S-type anion channels during stomatal closure, providing a specificity mechanism in Ca2+-signaling. However, the underlying genetic and biochemical mechanisms remain unknown. Here we show impairment of ABA signal transduction in stomata of calcium-dependent protein kinase quadruple mutant plants. Interestingly, protein phosphatase 2Cs prevent non-specific Ca2+-signaling. Moreover, we demonstrate an unexpected interdependence of the Ca2+-dependent and Ca2+-independent ABA-signaling branches and the in planta requirement of simultaneous phosphorylation at two key phosphorylation sites in SLAC1. We identify novel mechanisms ensuring specificity and robustness within stomatal Ca2+-signaling on a cellular, genetic, and biochemical level.

DOI： 10.7554/elife.03599

Other Link： https://cdn.elifesciences.org/articles/03599/elife-03599-v1.pdf

Open Stomata 1 Kinase is Essential for Yeast Elicitor-Induced Stomatal Closure in Arabidopsis Reviewed International coauthorship International journal

Wenxiu Ye, Yuji Adachi, Shintaro Munemasa, Yoshimasa Nakamura, Izumi C. Mori, Yoshiyuki Murata

Plant and Cell Physiology 56 ( 6 ) 1239 - 1248 2015.6

Language：English Publishing type：Research paper (scientific journal) Publisher：Oxford University Press (OUP)

We recently demonstrated that yeast elicitor (YEL)-induced stomatal closure requires a Ca2+-dependent kinase, CPK6. A Ca2+-independent kinase, Open Stomata 1 (OST1), is involved in stomatal closure induced by various stimuli including ABA. In the present study, we investigated the role of OST1 in YEL-induced stomatal closure in Arabidopsis using a knock-out mutant, ost1-3, and a kinase-deficient mutant, ost1-2. YEL did not induce stomatal closure or activation of guard cell S-type anion channels in the ost1 mutants unlike in wild-type plants. However, YEL did not increase OST1 kinase activity in wild-type guard cells. The YEL-induced stomatal closure and activation of S-type anion channels were also impaired in a gain-of-function mutant of a clade A type 2C protein phosphatase (ABA INSENSITIVE 1), abi1-1C. In the ost1 mutants like in the wild type, YEL induced H2O2 accumulation, activation of non-selective Ca2+-permeable cation (I-Ca) channels and transient elevations in cytosolic free Ca2+ concentration ([Ca2+](cyt)) in guard cells. These results suggest that OST1 kinase is essential for stomatal closure and activation of S-type anion channels induced by YEL and that OST1 is not involved in H2O2 accumulation, I-Ca channel activation or [Ca2+](cyt) elevations in guard cells induced by YEL.

DOI： 10.1093/pcp/pcv051

Diverse Stomatal Signaling and the Signal Integration Mechanism Invited Reviewed International journal

Yoshiyuki Murata, Izumi C. Mori, Shintaro Munemasa

Annual Review of Plant Biology 66 ( 1 ) 369 - 392 2015.4

Authorship：Last author,　Corresponding author Language：English Publishing type：Research paper (scientific journal) Publisher：Annual Reviews

Guard cells perceive a variety of chemicals produced metabolically in response to abiotic and biotic stresses, integrate the signals into reactive oxygen species and calcium signatures, and convert these signatures into stomatal movements by regulating turgor pressure. Guard cell behaviors in response to such complex signals are critical for plant growth and sustenance in stressful, ever-changing environments. The key open question is how guard cells achieve the signal integration to optimize stomatal aperture. Abscisic acid is responsible for stomatal closure in plants in response to drought, and its signal transduction has been well studied. Other plant hormones and low-molecular-weight compounds function as inducers of stomatal closure and mediators of signaling in guard cells. In this review, we summarize recent advances in research on the diverse stomatal signaling pathways, with specific emphasis on signal integration and signal interaction in guard cell movement.

DOI： 10.1146/annurev-arplant-043014-114707

Inhibition by acrolein of light-induced stomatal opening through inhibition of inward-rectifying potassium channels in Arabidopsis thaliana Reviewed International coauthorship International journal

Md Moshiul Islam, Wenxiu Ye, Daiki Matsushima, Md Atiqur Rahman Khokon, Shintaro Munemasa, Yoshimasa Nakamura, Yoshiyuki Murata

Bioscience, Biotechnology, and Biochemistry 79 ( 1 ) 59 - 62 2015.1

Language：English Publishing type：Research paper (scientific journal) Publisher：Oxford University Press (OUP)

<title>Abstract</title>
Acrolein is a reactive α,β-unsaturated aldehyde derived from lipid peroxides, which are produced in plants under a variety of stress. We investigated effects of acrolein on light-induced stomatal opening using Arabidopsis thaliana. Acrolein inhibited light-induced stomatal opening in a dose-dependent manner. Acrolein at 100 μM inhibited plasma membrane inward-rectifying potassium (Kin) channels in guard cells. Acrolein at 100 μM inhibited Kin channel KAT1 expressed in a heterologous system using Xenopus leaves oocytes. These results suggest that acrolein inhibits light-induced stomatal opening through inhibition of Kin channels in guard cells.

DOI： 10.1080/09168451.2014.951028

Nuclear factor-kappaB sensitizes to benzyl isothiocyanate-induced antiproliferation in p53-deficient colorectal cancer cells Reviewed International coauthorship International journal

N Abe, D-X Hou, S Munemasa, Y Murata, Y Nakamura

Cell Death & Disease 5 ( 11 ) e1534 2014.11

Identification of Cyclic GMP-Activated Nonselective Ca2+-Permeable Cation Channels and Associated CNGC5 and CNGC6 Genes in Arabidopsis Guard Cells Reviewed International coauthorship International journal

Yong-Fei Wang, Shintaro Munemasa, Noriyuki Nishimura, Hui-Min Ren, Nadia Robert, Michelle Han, Irina Puzõrjova, Hannes Kollist, Stephen Lee, Izumi Mori, Julian I. Schroeder

Plant Physiology 163 ( 2 ) 578 - 590 2013.10

Language：English Publishing type：Research paper (scientific journal) Publisher：Oxford University Press (OUP)

<title>Abstract</title>
Cytosolic Ca2+ in guard cells plays an important role in stomatal movement responses to environmental stimuli. These cytosolic Ca2+ increases result from Ca2+ influx through Ca2+-permeable channels in the plasma membrane and Ca2+ release from intracellular organelles in guard cells. However, the genes encoding defined plasma membrane Ca2+-permeable channel activity remain unknown in guard cells and, with some exceptions, largely unknown in higher plant cells. Here, we report the identification of two Arabidopsis (Arabidopsis thaliana) cation channel genes, CNGC5 and CNGC6, that are highly expressed in guard cells. Cytosolic application of cyclic GMP (cGMP) and extracellularly applied membrane-permeable 8-Bromoguanosine 3′,5′-cyclic monophosphate-cGMP both activated hyperpolarization-induced inward-conducting currents in wild-type guard cells using Mg2+ as the main charge carrier. The cGMP-activated currents were strongly blocked by lanthanum and gadolinium and also conducted Ba2+, Ca2+, and Na+ ions. cngc5 cngc6 double mutant guard cells exhibited dramatically impaired cGMP-activated currents. In contrast, mutations in CNGC1, CNGC2, and CNGC20 did not disrupt these cGMP-activated currents. The yellow fluorescent protein-CNGC5 and yellow fluorescent protein-CNGC6 proteins localize in the cell periphery. Cyclic AMP activated modest inward currents in both wild-type and cngc5cngc6 mutant guard cells. Moreover, cngc5 cngc6 double mutant guard cells exhibited functional abscisic acid (ABA)-activated hyperpolarization-dependent Ca2+-permeable cation channel currents, intact ABA-induced stomatal closing responses, and whole-plant stomatal conductance responses to darkness and changes in CO2 concentration. Furthermore, cGMP-activated currents remained intact in the growth controlled by abscisic acid2 and abscisic acid insensitive1 mutants. This research demonstrates that the CNGC5 and CNGC6 genes encode unique cGMP-activated nonselective Ca2+-permeable cation channels in the plasma membrane of Arabidopsis guard cells.

DOI： 10.1104/pp.113.225045

Calcium-dependent protein Kinase CPK6 positively functions in induction by yeast elicitor of stomatal closure and inhibition by yeast elicitor of light-induced stomatal opening in Arabidopsis Reviewed International coauthorship International journal

Wenxiu Ye, Daichi Muroyama, Shintaro Munemasa, Yoshimasa Nakamura, Izumi C. Mori, Yoshiyuki Murata

Plant Physiology 163 ( 2 ) 591 - 599 2013.10

Language：English Publishing type：Research paper (scientific journal)

Yeast elicitor (YEL) induces stomatal closure that is mediated by a Ca2+-dependent signaling pathway. A Ca2+-dependent protein kinase, CPK6, positively regulates activation of ion channels in abscisic acid and methyl jasmonate signaling, leading to stomatal closure in Arabidopsis (Arabidopsis thaliana). YEL also inhibits light-induced stomatal opening. However, it remains unknown whether CPK6 is involved in induction by YEL of stomatal closure or in inhibition by YEL of light-induced stomatal opening. In this study, we investigated the roles of CPK6 in induction by YEL of stomatal closure and inhibition by YEL of light-induced stomatal opening in Arabidopsis. Disruption of CPK6 gene impaired induction by YEL of stomatal closure and inhibition by YEL of light-induced stomatal opening. Activation by YEL of nonselective Ca2+-permeable cation channels was impaired in cpk6-2 guard cells, and transient elevations elicited by YEL in cytosolic-free Ca2+ concentration were suppressed in cpk6-2 and cpk6-1 guard cells. YEL activated slow anion channels in wild-type guard cells but not in cpk6-2 or cpk6-1 and inhibited inward-rectifying K+ channels in wild-type guard cells but not in cpk6-2 or cpk6-1. The cpk6-2 and cpk6-1 mutations inhibited YEL-induced hydrogen peroxide accumulation in guard cells and apoplast of rosette leaves but did not affect YEL-induced hydrogen peroxide production in the apoplast of rosette leaves. These results suggest that CPK6 positively functions in induction by YEL of stomatal closure and inhibition by YEL of light-induced stomatal opening in Arabidopsis and is a convergent point of signaling pathways for stomatal closure in response to abiotic and biotic stress. © 2013 American Society of Plant Biologists. All Rights Reserved.

DOI： 10.1104/pp.113.224055

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