ERMO3/MVP1/GOLD36 Is Involved in a Cell Type-Specific Mechanism for Maintaining ER Morphology in Arabidopsis thaliana

Ryohei Thomas Nakano, Ryo Matsushima, Atsushi J. Nagano, Yoichiro Fukao, Masayuki Fujiwara, Maki Kondo, Mikio Nishimura, Ikuko Hara-Nishimura

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

The endoplasmic reticulum (ER) has a unique, network-like morphology. The ER structures are composed of tubules, cisternae, and three-way junctions. This morphology is highly conserved among eukaryotes, but the molecular mechanism that maintains ER morphology has not yet been elucidated. In addition, certain Brassicaceae plants develop a unique ER-derived organelle called the ER body. This organelle accumulates large amounts of PYK10, a β-glucosidase, but its physiological functions are still obscure. We aimed to identify a novel factor required for maintaining the morphology of the ER, including ER bodies, and employed a forward-genetic approach using transgenic Arabidopsis thaliana (GFP-h) with fluorescently-labeled ER. We isolated and investigated a mutant (designated endoplasmic reticulum morphology3, ermo3) with huge aggregates and abnormal punctate structures of ER. ERMO3 encodes a GDSL-lipase/esterase family protein, also known as MVP1. Here, we showed that, although ERMO3/MVP1/GOLD36 was expressed ubiquitously, the morphological defects of ermo3 were specifically seen in a certain type of cells where ER bodies developed. Coimmunoprecipitation analysis combined with mass spectrometry revealed that ERMO3/MVP1/GOLD36 interacts with the PYK10 complex, a huge protein complex that is thought to be important for ER body-related defense systems. We also found that the depletion of transcription factor NAI1, a master regulator for ER body formation, suppressed the formation of ER-aggregates in ermo3 cells, suggesting that NAI1 expression plays an important role in the abnormal aggregation of ER. Our results suggest that ERMO3/MVP1/GOLD36 is required for preventing ER and other organelles from abnormal aggregation and for maintaining proper ER morphology in a coordinated manner with NAI1.

Original languageEnglish
Article numbere49103
JournalPLoS One
Volume7
Issue number11
DOIs
Publication statusPublished - Nov 14 2012

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Arabidopsis
Endoplasmic Reticulum
endoplasmic reticulum
Arabidopsis thaliana
cells
Agglomeration
Glucosidases
Esterases
Lipase
Mass spectrometry
Proteins
Transcription Factors
Organelles
organelles
Defects
protein aggregates
Brassicaceae
glucosidases
Eukaryota
esterases

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Medicine(all)

Cite this

ERMO3/MVP1/GOLD36 Is Involved in a Cell Type-Specific Mechanism for Maintaining ER Morphology in Arabidopsis thaliana. / Nakano, Ryohei Thomas; Matsushima, Ryo; Nagano, Atsushi J.; Fukao, Yoichiro; Fujiwara, Masayuki; Kondo, Maki; Nishimura, Mikio; Hara-Nishimura, Ikuko.

In: PLoS One, Vol. 7, No. 11, e49103, 14.11.2012.

Research output: Contribution to journalArticle

Nakano, RT, Matsushima, R, Nagano, AJ, Fukao, Y, Fujiwara, M, Kondo, M, Nishimura, M & Hara-Nishimura, I 2012, 'ERMO3/MVP1/GOLD36 Is Involved in a Cell Type-Specific Mechanism for Maintaining ER Morphology in Arabidopsis thaliana', PLoS One, vol. 7, no. 11, e49103. https://doi.org/10.1371/journal.pone.0049103
Nakano, Ryohei Thomas ; Matsushima, Ryo ; Nagano, Atsushi J. ; Fukao, Yoichiro ; Fujiwara, Masayuki ; Kondo, Maki ; Nishimura, Mikio ; Hara-Nishimura, Ikuko. / ERMO3/MVP1/GOLD36 Is Involved in a Cell Type-Specific Mechanism for Maintaining ER Morphology in Arabidopsis thaliana. In: PLoS One. 2012 ; Vol. 7, No. 11.
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