Identification of Two Novel Endoplasmic Reticulum Body-Specific Integral Membrane Proteins

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  • Kenji Yamada
    Department of Cell Biology, National Institute for Basic Biology, Okazaki 444–8585, Aichi, Japan (K.Y., Mo.N., Mi.N.); School of Life Science, Graduate University for Advanced Studies (Sokendai), Okazaki 444–8585, Aichi, Japan (K.Y., Mi.N.); and Department of Botany, Graduate School of Science, Kyoto University, Kyoto 606–8502, Kyoto, Japan (A.J.N., I.H.-N.)
  • Atsushi J. Nagano
    Department of Cell Biology, National Institute for Basic Biology, Okazaki 444–8585, Aichi, Japan (K.Y., Mo.N., Mi.N.); School of Life Science, Graduate University for Advanced Studies (Sokendai), Okazaki 444–8585, Aichi, Japan (K.Y., Mi.N.); and Department of Botany, Graduate School of Science, Kyoto University, Kyoto 606–8502, Kyoto, Japan (A.J.N., I.H.-N.)
  • Momoko Nishina
    Department of Cell Biology, National Institute for Basic Biology, Okazaki 444–8585, Aichi, Japan (K.Y., Mo.N., Mi.N.); School of Life Science, Graduate University for Advanced Studies (Sokendai), Okazaki 444–8585, Aichi, Japan (K.Y., Mi.N.); and Department of Botany, Graduate School of Science, Kyoto University, Kyoto 606–8502, Kyoto, Japan (A.J.N., I.H.-N.)
  • Ikuko Hara-Nishimura
    Department of Cell Biology, National Institute for Basic Biology, Okazaki 444–8585, Aichi, Japan (K.Y., Mo.N., Mi.N.); School of Life Science, Graduate University for Advanced Studies (Sokendai), Okazaki 444–8585, Aichi, Japan (K.Y., Mi.N.); and Department of Botany, Graduate School of Science, Kyoto University, Kyoto 606–8502, Kyoto, Japan (A.J.N., I.H.-N.)
  • Mikio Nishimura
    Department of Cell Biology, National Institute for Basic Biology, Okazaki 444–8585, Aichi, Japan (K.Y., Mo.N., Mi.N.); School of Life Science, Graduate University for Advanced Studies (Sokendai), Okazaki 444–8585, Aichi, Japan (K.Y., Mi.N.); and Department of Botany, Graduate School of Science, Kyoto University, Kyoto 606–8502, Kyoto, Japan (A.J.N., I.H.-N.)

Description

<jats:title>Abstract</jats:title> <jats:p>The endoplasmic reticulum (ER) body, a large compartment specific to the Brassicales, accumulates β-glucosidase and possibly plays a role in the defense against pathogens and herbivores. Although the ER body is a subdomain of the ER, it is unclear whether any ER body-specific membrane protein exists. In this study, we identified two integral membrane proteins of the ER body in Arabidopsis (Arabidopsis thaliana) and termed them MEMBRANE PROTEIN OF ENDOPLASMIC RETICULUM BODY1 (MEB1) and MEB2. In Arabidopsis, a basic helix-loop-helix transcription factor, NAI1, and an ER body component, NAI2, regulate ER body formation. The expression profiles of MEB1 and MEB2 are similar to those of NAI1, NAI2, and ER body β-glucosidase PYK10 in Arabidopsis. The expression of MEB1 and MEB2 was reduced in the nai1 mutant, indicating that NAI1 regulates the expression of MEB1 and MEB2 genes. MEB1 and MEB2 proteins localize to the ER body membrane but not to the ER network, suggesting that these proteins are specifically recruited to the ER body membrane. MEB1 and MEB2 physically interacted with ER body component NAI2, and they were diffused throughout the ER network in the nai2 mutant, which has no ER body. Heterologous expression of MEB1 and MEB2 in yeast (Saccharomyces cerevisiae) suppresses iron and manganese toxicity, suggesting that MEB1 and MEB2 are metal transporters. These results indicate that the membrane of ER bodies has specific membrane proteins and suggest that the ER body is involved in defense against metal stress as well as pathogens and herbivores.</jats:p>

Journal

  • Plant Physiology

    Plant Physiology 161 (1), 108-120, 2012-11-19

    Oxford University Press (OUP)

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