<scp>MAG</scp>2 and three <scp>MAG</scp>2‐<scp>INTERACTING PROTEIN</scp>s form an <scp>ER</scp>‐localized complex to facilitate storage protein transport in <i>Arabidopsis thaliana</i>

Li, Lixin; Shimada, Tomoo; Takahashi, Hideyuki; Koumoto, Yasuko; Shirakawa, Makoto; Takagi, Junpei; Zhao, Xiaonan; Tu, Baoyu; Jin, Hongmin; Shen, Zhe; Han, Baoda; Jia, Meihui; Kondo, Maki; Nishimura, Mikio; Hara‐Nishimura, Ikuko

doi:10.1111/tpj.12347

Cited by 36 publications

(53 citation statements)

References 63 publications

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“…However, this complex has the fourth subunit, MIP3, which contains a Sec1 domain. This is the first report of a Sec1-containing protein involved in ER-Golgi trafficking including animals and yeast (Li et al, 2013).…”

Section: Tethering Factors and Snaresmentioning

confidence: 90%

Formation and Maintenance of the Golgi Apparatus in Plant Cells

Ito

Uemura

Nakano

2014

International Review of Cell and Molecular Biology

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Section: Tethering Factors and Snaresmentioning

confidence: 90%

Formation and Maintenance of the Golgi Apparatus in Plant Cells

Ito

Uemura

Nakano

2014

International Review of Cell and Molecular Biology

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“…The two genes were significantly up-regulated across combined stresses, except for S & D. In addition, we examined the expression of an unknown gene (BRADI4G33310) from module 04 that displayed a negative correlation with RWC. Its Arabidopsis ortholog (AT5G24350, AtMIP2) was recently shown to be part of a unique complex on the ER that is responsible for efficient transport of seed storage proteins (Li et al, 2013). Expression levels of BdMIP2 were significantly up-regulated across combined stresses, with the exception of S & D (Supplemental Figure S12).…”

Section: Pathway and Coexpression Analyses Detected Functional Differmentioning

confidence: 99%

Unique Physiological and Transcriptional Shifts under Combinations of Salinity, Drought, and Heat

Shaar-Moshe

Blumwald²,

Peleg³

2017

Plant Physiol.

111

101

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Climate-change-driven stresses such as extreme temperatures, water deficit, and ion imbalance are projected to exacerbate and jeopardize global food security. Under field conditions, these stresses usually occur simultaneously and cause damages that exceed single stresses. Here, we investigated the transcriptional patterns and morpho-physiological acclimations of Brachypodium dystachion to single salinity, drought, and heat stresses, as well as their double and triple stress combinations. Hierarchical clustering analysis of morpho-physiological acclimations showed that several traits exhibited a gradually aggravating effect as plants were exposed to combined stresses. On the other hand, other morphological traits were dominated by salinity, while some physiological traits were shaped by heat stress. Response patterns of differentially expressed genes, under single and combined stresses (i.e. common stress genes), were maintained only among 37% of the genes, indicating a limited expression consistency among partially overlapping stresses. A comparison between common stress genes and genes that were uniquely expressed only under combined stresses (i.e. combination unique genes) revealed a significant shift from increased intensity to antagonistic responses, respectively. The different transcriptional signatures imply an alteration in the mode of action under combined stresses and limited ability to predict plant responses as different stresses are combined. Coexpression analysis coupled with enrichment analysis revealed that each gene subset was enriched with different biological processes. Common stress genes were enriched with known stress response pathways, while combination unique-genes were enriched with unique processes and genes with unknown functions that hold the potential to improve stress tolerance and enhance cereal productivity under suboptimal field conditions.

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“…The GFP fluorescence of dry seeds was observed as described previously (Fuji et al, 2007). The immunoelectron microscopic analysis of dry seeds was performed as described previously (Li et al, 2013;Shimada et al, 2014).…”

Section: Confocal Laser Scanning Microscopy and Electron Microscopymentioning

confidence: 99%

The Adaptor Complex AP-4 Regulates Vacuolar Protein Sorting at the trans-Golgi Network by Interacting with VACUOLAR SORTING RECEPTOR1

et al. 2015

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Adaptor protein (AP) complexes play critical roles in protein sorting among different post-Golgi pathways by recognizing specific cargo protein motifs. Among the five AP complexes (AP-1-AP-5) in plants, AP-4 is one of the most poorly understood; the AP-4 components, AP-4 cargo motifs, and AP-4 functional mechanism are not known. Here, we identify the AP-4 components and show that the AP-4 complex regulates receptor-mediated vacuolar protein sorting by recognizing VACUOLAR SORTING RECEPTOR1 (VSR1), which was originally identified as a sorting receptor for seed storage proteins to target protein storage vacuoles in Arabidopsis (Arabidopsis thaliana). From the vacuolar sorting mutant library GREEN FLUORESCENT SEED (GFS), we isolated three gfs mutants that accumulate abnormally high levels of VSR1 in seeds and designated them as gfs4, gfs5, and gfs6. Their responsible genes encode three (AP4B, AP4M, and AP4S) of the four subunits of the AP-4 complex, respectively, and an Arabidopsis mutant (ap4e) lacking the fourth subunit, AP4E, also had the same phenotype. Mass spectrometry demonstrated that these four proteins form a complex in vivo. The four mutants showed defects in the vacuolar sorting of the major storage protein 12S globulins, indicating a role for the AP-4 complex in vacuolar protein transport. AP4M bound to the tyrosine-based motif of VSR1. AP4M localized at the trans-Golgi network (TGN) subdomain that is distinct from the AP-1-localized TGN subdomain. This study provides a novel function for the AP-4 complex in VSR1-mediated vacuolar protein sorting at the specialized domain of the TGN.

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MAG2 and three MAG2‐INTERACTING PROTEINs form an ER‐localized complex to facilitate storage protein transport in Arabidopsis thaliana

Cited by 36 publications

References 63 publications

Formation and Maintenance of the Golgi Apparatus in Plant Cells

Formation and Maintenance of the Golgi Apparatus in Plant Cells

Unique Physiological and Transcriptional Shifts under Combinations of Salinity, Drought, and Heat

The Adaptor Complex AP-4 Regulates Vacuolar Protein Sorting at the trans-Golgi Network by Interacting with VACUOLAR SORTING RECEPTOR1

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