A guanine nucleotide exchange factor for Rab5 proteins is essential for intracellular transport of the proglutelin from the golgi apparatus to the protein storage vacuole in rice endosperm

Masako Fukuda, Liuying Wen, Mio Satoh-Cruz, Yasushi Kawagoe, Yoshiaki Nagamura, Thomas W. Okita, Haruhiko Washida, Aya Sugino, Sonoko Ishino, Yoshizumi Ishino, Masahiro Ogawa, Mariko Sunada, Takashi Ueda, Toshihiro Kumamaru

研究成果: ジャーナルへの寄稿記事

28 引用 (Scopus)

抄録

Rice (Oryza sativa) glutelins are synthesized on the endoplasmic reticulum as a precursor, which are then transported via the Golgi to protein storage vacuoles (PSVs), where they are proteolytically processed into acidic and basic subunits. The glutelin precursor mutant6 (glup6) accumulates abnormally large amounts of proglutelin. Map-base cloning studies showed that glup6 was a loss-of-function mutant of guanine nucleotide exchange factor (GEF), which activates Rab GTPase, a key regulator of membrane trafficking. Immunofluorescence studies showed that the transport of proglutelins and a-globulins to PSV was disrupted in glup6 endosperm. Secreted granules of glutelin and a-globulin were readily observed in young glup6 endosperm, followed by the formation of large dilated paramural bodies (PMBs) containing both proteins as the endosperm matures. The PMBs also contained membrane biomarkers for the Golgi and prevacuolar compartment as well as the cell wall component, b-glucan. Direct evidence was gathered showing that GLUP6/GEF activated in vitro GLUP4/Rab5 as well as several Arabidopsis (Arabidopsis thaliana) Rab5 isoforms to the GTP-bound form. Therefore, loss-of-function mutations in GEF or Rab5 disrupt the normal transport of proglutelin from the Golgi to PSVs, resulting in the initial extracellular secretion of these proteins followed, in turn, by the formation of PMBs. Overall, our results indicate that GLUP6/GEF is the activator of Rab5 GTPase and that the cycling of GTP- and GDP-bound forms of this regulatory protein is essential for the intracellular transport of proglutelin and a-globulin from the Golgi to PSVs and in the maintenance of the general structural organization of the endomembrane system in rice seeds.

元の言語英語
ページ(範囲)663-674
ページ数12
ジャーナルPlant physiology
162
発行部数2
DOI
出版物ステータス出版済み - 6 1 2013

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rab5 GTP-Binding Proteins
Guanine Nucleotide Exchange Factors
Endosperm
glutelins
Golgi Apparatus
storage proteins
Vacuoles
Golgi apparatus
Glutens
endosperm
vacuoles
rice
globulins
Globulins
Proteins
proteins
guanosinetriphosphatase
Guanosine Triphosphate
Arabidopsis
GTP Phosphohydrolase Activators

All Science Journal Classification (ASJC) codes

  • Physiology
  • Genetics
  • Plant Science

これを引用

A guanine nucleotide exchange factor for Rab5 proteins is essential for intracellular transport of the proglutelin from the golgi apparatus to the protein storage vacuole in rice endosperm. / Fukuda, Masako; Wen, Liuying; Satoh-Cruz, Mio; Kawagoe, Yasushi; Nagamura, Yoshiaki; Okita, Thomas W.; Washida, Haruhiko; Sugino, Aya; Ishino, Sonoko; Ishino, Yoshizumi; Ogawa, Masahiro; Sunada, Mariko; Ueda, Takashi; Kumamaru, Toshihiro.

:: Plant physiology, 巻 162, 番号 2, 01.06.2013, p. 663-674.

研究成果: ジャーナルへの寄稿記事

Fukuda, Masako ; Wen, Liuying ; Satoh-Cruz, Mio ; Kawagoe, Yasushi ; Nagamura, Yoshiaki ; Okita, Thomas W. ; Washida, Haruhiko ; Sugino, Aya ; Ishino, Sonoko ; Ishino, Yoshizumi ; Ogawa, Masahiro ; Sunada, Mariko ; Ueda, Takashi ; Kumamaru, Toshihiro. / A guanine nucleotide exchange factor for Rab5 proteins is essential for intracellular transport of the proglutelin from the golgi apparatus to the protein storage vacuole in rice endosperm. :: Plant physiology. 2013 ; 巻 162, 番号 2. pp. 663-674.
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abstract = "Rice (Oryza sativa) glutelins are synthesized on the endoplasmic reticulum as a precursor, which are then transported via the Golgi to protein storage vacuoles (PSVs), where they are proteolytically processed into acidic and basic subunits. The glutelin precursor mutant6 (glup6) accumulates abnormally large amounts of proglutelin. Map-base cloning studies showed that glup6 was a loss-of-function mutant of guanine nucleotide exchange factor (GEF), which activates Rab GTPase, a key regulator of membrane trafficking. Immunofluorescence studies showed that the transport of proglutelins and a-globulins to PSV was disrupted in glup6 endosperm. Secreted granules of glutelin and a-globulin were readily observed in young glup6 endosperm, followed by the formation of large dilated paramural bodies (PMBs) containing both proteins as the endosperm matures. The PMBs also contained membrane biomarkers for the Golgi and prevacuolar compartment as well as the cell wall component, b-glucan. Direct evidence was gathered showing that GLUP6/GEF activated in vitro GLUP4/Rab5 as well as several Arabidopsis (Arabidopsis thaliana) Rab5 isoforms to the GTP-bound form. Therefore, loss-of-function mutations in GEF or Rab5 disrupt the normal transport of proglutelin from the Golgi to PSVs, resulting in the initial extracellular secretion of these proteins followed, in turn, by the formation of PMBs. Overall, our results indicate that GLUP6/GEF is the activator of Rab5 GTPase and that the cycling of GTP- and GDP-bound forms of this regulatory protein is essential for the intracellular transport of proglutelin and a-globulin from the Golgi to PSVs and in the maintenance of the general structural organization of the endomembrane system in rice seeds.",
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T1 - A guanine nucleotide exchange factor for Rab5 proteins is essential for intracellular transport of the proglutelin from the golgi apparatus to the protein storage vacuole in rice endosperm

AU - Fukuda, Masako

AU - Wen, Liuying

AU - Satoh-Cruz, Mio

AU - Kawagoe, Yasushi

AU - Nagamura, Yoshiaki

AU - Okita, Thomas W.

AU - Washida, Haruhiko

AU - Sugino, Aya

AU - Ishino, Sonoko

AU - Ishino, Yoshizumi

AU - Ogawa, Masahiro

AU - Sunada, Mariko

AU - Ueda, Takashi

AU - Kumamaru, Toshihiro

PY - 2013/6/1

Y1 - 2013/6/1

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