Kyaw Aung

Iowa State University

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Shinji Tsukahara

Saitama University

Jianping Hu

Michigan State University

Zhongpeng Li

Chinese Academy of Medical Sciences & Peking Union Medical College

Fumihiko Maekawa

National Institute for Environmental Studies

Keiko Nohara

National Institute for Environmental Studies

Kazuaki Nakamura

National Center For Child Health and Development

Sheng Yang He

Michigan State University

Tzyy‐Jen Chiou

Agricultural Biotechnology Research Center, Academia Sinica

Akito Tanoue

National Center For Child Health and Development

Shu-I Lin

National Taiwan University

Cooperative Institutions

Michigan State University

Saitama University

Iowa State University

The University of Tokyo

University of Tsukuba

National Institute for Environmental Studies

Nagoya University

Agricultural Biotechnology Research Center, Academia Sinica

Howard Hughes Medical Institute

National Center For Child Health and Development

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Role of Environmental Chemical Insult in Neuronal Cell Death and Cytoskeleton Damage

Biological and Pharmaceutical Bulletin (2015)

Kyaw Aung Shinji Tsukahara Fumihiko Maekawa Keiko Nohara Kazuaki Nakamura

Environmental influences, such as chemical exposure, have long been considered potential risk factors for neurodegenerative disorders, including neuromuscular diseases. However, no definitive links between environmental chemical exposure and a pathogenic mechanism of neurodegenerative disease has yet been established. In this study, we describe that exposure to arsenic, an environmental pollutant naturally found in drinking water, induces neuronal cell death and alteration of morphology, particularly neurite outgrowth and in the cytoskeleton of neurons. Since progressive cell loss accompanied by the alteration of neuronal structures and cytoskeleton is considered the major pathologic feature of neurodegenerative disorders, arsenic-induced neurotoxicity might contribute to an etiologic mechanism of some neurodegenerative diseases. Further, we discuss the importance of in vitro assay, particularly an embryonic toxicity test, for assessing the neurotoxicity of chemicals, because most of chemicals found in our environment remain to be evaluated regarding their neurotoxicity risk for neurodegenerative diseases.

Neurotoxicity

Neurite

10.1248/bpb.b14-00890

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Citations (15)

Effects of aromatase or estrogen receptor gene deletion on the formation of sexually dimorphic nuclei in mice

Neuroscience Research (2011)

Ryohei Kurihara Mumeko C. Tsuda Kyaw Aung M. Nakata Kota Okoshi

Hindbrain

10.1016/j.neures.2011.07.1149

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Citations (1)

Plasmodesmata-dependent intercellular movement of bacterial effectors

bioRxiv (Cold Spring Harbor Laboratory) (2020)

Zhongpeng Li Haris Variz Yani Chen Suling Liu Kyaw Aung

Abstract Pathogenic microorganisms deliver protein effectors into host cells to suppress host immune responses. Recent findings reveal that phytopathogens manipulate the function of plant cell-to-cell communication channels plasmodesmata (PD) to promote diseases. Several bacterial and filamentous pathogen effectors have been shown to regulate PD in their host cells. A few effectors of filamentous pathogens have been reported to move from the infected cells to neighboring plant cells through PD; however, it is unclear whether bacterial effectors can traffic through PD in plants. In this study, we systemically determined the intercellular movement of Pseudomonas syringae pv. tomato ( Pst ) DC3000 effectors between adjoining plant cells in Nicotiana benthamiana . We observed that at least 16 Pst DC3000 effectors move from transformed cells to the surrounding plant cells. The movement of the effectors is largely dependent on their molecular weights. The expression of PD regulators, Arabidopsis PD-located protein PDLP5 and PDLP7, lead to PD closure and inhibits the PD-dependent movement of a bacterial effector in N. benthamiana . Similarly, a 22-amino acid peptide of bacterial flagellin (flg22) treatment induces PD closure and suppresses the movement of a bacterial effector in N. benthamiana . Together, our findings demonstrated that bacterial effectors are able to move intercellularly through PD in plants.

Plasmodesma

Pseudomonas syringae

Movement protein

Plant cell

Xanthomonas

10.1101/2020.12.10.420240

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Citations (3)

Plasmodesmata-Dependent Intercellular Movement of Bacterial Effectors

Frontiers in Plant Science (2021)

Zhongpeng Li Haris Variz Yani Chen Suling Liu Kyaw Aung

Pathogenic microorganisms deliver protein effectors into host cells to suppress host immune responses. Recent findings reveal that phytopathogens manipulate the function of plant cell-to-cell communication channels known as plasmodesmata (PD) to promote diseases. Several bacterial and filamentous pathogen effectors have been shown to regulate PD in their host cells. A few effectors of filamentous pathogens have been reported to move from the infected cells to neighboring plant cells through PD; however, it is unclear whether bacterial effectors can traffic through PD in plants. In this study, we determined the intercellular movement of Pseudomonas syringae pv. tomato ( Pst ) DC3000 effectors between adjoining plant cells in Nicotiana benthamiana . We observed that at least 16 Pst DC3000 effectors have the capacity to move from transformed cells to the surrounding plant cells. The movement of the effectors is largely dependent on their molecular weights. The expression of PD regulators, Arabidopsis PD-located protein PDLP5 and PDLP7, leads to PD closure and inhibits the PD-dependent movement of a bacterial effector in N. benthamiana . Similarly, a 22-amino acid peptide of bacterial flagellin (flg22) treatment induces PD closure and suppresses the movement of a bacterial effector in N. benthamiana . Among the mobile effectors, HopAF1 and HopA1 are localized to the plasma membrane (PM) in plant cells. Interestingly, the PM association of HopAF1 does not negatively affect the PD-dependent movement. Together, our findings demonstrate that bacterial effectors are able to move intercellularly through PD in plants.

Plasmodesma

Pseudomonas syringae

Movement protein

Plant cell

Xanthomonas

10.3389/fpls.2021.640277

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Citations (33)

Involvement of hemeoxygenase-1 in di(2-ethylhexyl) phthalate (DEHP)-induced apoptosis of Neuro-2a cells

The Journal of Toxicological Sciences (2014)

Kyaw Aung Tin‐Tin Win‐Shwe Moeko Kanaya Hirohisa Takano Shinji Tsukahara

A widely-used plasticizer di(2-ethylhexyl) phthalate (DEHP) is known to induce apoptosis in neurons, although the mechanisms responsible for DEHP-induced apoptosis is not well explored yet. We recently showed that exposure to DEHP increases the expression of hemeoxygenase (HO)-1, an oxidative stress related enzyme, in the mice brain. In this study, we investigated whether HO-1 is involved in DEHP-induced apoptosis using a mouse neuroblastoma cell line Neuro-2a, which forcibly express SCAT3, a fluorescent indicator of caspase-3 activity. The doses of DEHP at 1, 10 or 100 µM were used in the present study to mimic the level of human exposure to DEHP. Live image analysis of SCAT3-expressing Neuro-2a cells revealed that caspase-3 activity in the cells was significantly increased by DEHP at 100 µM but not 1 or 10 µM. We measured HO-1 mRNA level in Neuro-2a cells exposed to DEHP and found significant increase in HO-1 mRNA level by DEHP at 100 µM but not 1 or 10 µM. Live image analysis of SCAT3-expresisng Neuro-2a cells was further performed to determine the effects of HO-1 siRNA in DEHP-induced apoptosis via caspase-3 activation. We found that knockdown of HO-1 gene nullifies the effects of DEHP to activate caspase-3. These results suggest that HO-1 is involved in DEHP-induced apoptosis. Moreover, this study demonstrates that high-dose DEHP exposure induces caspase-3-dependent apoptosis, which is at least partially mediated by the up-regulation of HO-1 gene, in Neuro-2a cells.

10.2131/jts.39.217

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Citations (19)

The Arabidopsis peroxisome division mutantpdd2is defective in theDYNAMIN-RELATED PROTEIN3A(DRP3A) gene

Plant Signaling & Behavior (2009)

Kyaw Aung Jianping Hu

In plants, the division of peroxisomes is mediated by several classes of proteins, including PEROXIN11 (PEX11), FISSION1 (FIS1), and DYNAMIN-RELATED PROTEIN3 (DRP3). DRP3A and DRP3B are two homologous dynamin-related proteins playing overlapping roles in the division of both peroxisomes and mitochondria, with DRP3A performing a stronger function than DRP3B in peroxisomal fission. Here, we report the identification and characterization of the peroxisome division defective 2 (pdd2) mutant, which was later proven to be another drp3A allele. The pdd2 mutant generates a truncated DRP3A protein and exhibits pale green and retarded growth phenotypes. Intriguingly, this mutant displays much stronger peroxisome division deficiency in root cells than in leaf mesophyll cells. Our data suggest that the partial GTPase effector domain retained in pdd2 may have contributed to the distinct mutant phenotype of this mutant.

FIS1

10.4161/psb.4.6.8699

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Citations (9)

Regulation of plasmodesmata at specific cell-cell interfaces

bioRxiv (Cold Spring Harbor Laboratory) (2021)

Zhongpeng Li Kyaw Aung

Abstract Precise exchange of information and resources among cells is essential for multicellular organisms. Intercellular communication among diverse cell types requires differential mechanisms to achieve the specific regulation. Despite the significance of intercellular communication, it is largely unknown how the communication between different cells is regulated. Here, we report that two members of plasmodesmata-located proteins modulate plasmodesmata at two distinct cell-cell interfaces.

Plasmodesma

Multicellular organism

Cell type

10.1101/2021.02.25.432931

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Citations (1)

The role of water in plant–microbe interactions

The Plant Journal (2017)

Kyaw Aung Yanjuan Jiang Sheng Yang He

Throughout their life plants are associated with various microorganisms, including commensal, symbiotic and pathogenic microorganisms. Pathogens are genetically adapted to aggressively colonize and proliferate in host plants to cause disease. However, disease outbreaks occur only under permissive environmental conditions. The interplay between host, pathogen and environment is famously known as the 'disease triangle'. Among the environmental factors, rainfall events, which often create a period of high atmospheric humidity, have repeatedly been shown to promote disease outbreaks in plants, suggesting that the availability of water is crucial for pathogenesis. During pathogen infection, water-soaking spots are frequently observed on infected leaves as an early symptom of disease. Recent studies have shown that pathogenic bacteria dedicate specialized virulence proteins to create an aqueous habitat inside the leaf apoplast under high humidity. Water availability in the apoplastic environment, and probably other associated changes, can determine the success of potentially pathogenic microbes. These new findings reinforce the notion that the fight over water may be a major battleground between plants and pathogens. In this article, we will discuss the role of water availability in host-microbe interactions, with a focus on plant-bacterial interactions.

10.1111/tpj.13795

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Citations (170)

PLASMODESMATA-LOCATED PROTEIN 6 regulates plasmodesmal function in Arabidopsis vasculature

The Plant Cell (2024)

Zhongpeng Li Su-Ling Liu Christian Montes Justin W. Walley Kyaw Aung

Plasmodesmata connect adjoining plant cells, allowing molecules to move between the connected cells for communication and sharing resources. It has been well established that the plant polysaccharide callose is deposited at plasmodesmata, regulating their aperture and function. Among proteins involved in maintaining callose homeostasis, PLASMODESMATA-LOCATED PROTEINSs (PDLPs) promote callose deposition at plasmodesmata. This study explored the function of PDLP5 and PDLP6 in different cell types. We discovered that PDLP5 and PDLP6 are expressed in nonoverlapping cell types in Arabidopsis (Arabidopsis thaliana). The overexpression of PDLP5 and PDLP6 results in the overaccumulation of plasmodesmal callose at different cell interfaces, indicating that PDLP5 and PDLP6 are active in different cell types. We also observed 2 distinct patterns of starch accumulation in mature leaves of PDLP5 and PDLP6 overexpressors. An enzyme-catalyzed proximity labeling approach was used to identify putative functional partners of the PDLPs. We identified SUCROSE SYNTHASE 6 (SUS6) as a functional partner of PDLP6 in the vasculature. We further demonstrated that PDLP6 physically and genetically interacts with SUS6. In addition, CALLOSE SYNTHASE 7 (CALS7) physically interacts with SUS6 and PDLP6. Genetic interaction studies showed that CALS7 is required for PDLP6 function. We propose that PDLP6 functions with SUS6 and CALS7 in the vasculature to regulate plasmodesmal function.

Plasmodesma

10.1093/plcell/koae166

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Citations (5)

In-Depth Proteome Analysis of Arabidopsis Leaf Peroxisomes Combined with in Vivo Subcellular Targeting Verification Indicates Novel Metabolic and Regulatory Functions of Peroxisomes

PLANT PHYSIOLOGY (2009)

Sigrun Reumann Sheng Quan Kyaw Aung Pingfang Yang Kalpana Manandhar-Shrestha

Peroxisomes are metabolically diverse organelles with essential roles in plant development. The major protein constituents of plant peroxisomes are well characterized, whereas only a few low-abundance and regulatory proteins have been reported to date. We performed an in-depth proteome analysis of Arabidopsis (Arabidopsis thaliana) leaf peroxisomes using one-dimensional gel electrophoresis followed by liquid chromatography and tandem mass spectrometry. We detected 65 established plant peroxisomal proteins, 30 proteins whose association with Arabidopsis peroxisomes had been previously demonstrated only by proteomic data, and 55 putative novel proteins of peroxisomes. We subsequently tested the subcellular targeting of yellow fluorescent protein fusions for selected proteins and confirmed the peroxisomal localization for 12 proteins containing predicted peroxisome targeting signals type 1 or 2 (PTS1/2), three proteins carrying PTS-related peptides, and four proteins that lack conventional targeting signals. We thereby established the tripeptides SLM> and SKV> (where > indicates the stop codon) as new PTS1s and the nonapeptide RVx(5)HF as a putative new PTS2. The 19 peroxisomal proteins conclusively identified from this study potentially carry out novel metabolic and regulatory functions of peroxisomes. Thus, this study represents an important step toward defining the complete plant peroxisomal proteome.

Proteome

Peroxisomal targeting signal

Organelle

10.1104/pp.109.137703

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Citations (258)