KATAMARI1/MURUS3 Is a Novel Golgi Membrane Protein That Is Required for Endomembrane Organization in Arabidopsis

Tamura, Kentaro; Shimada, Tomoo; Kondo, Maki; Nishimura, Mikio; Hara‐Nishimura, Ikuko

doi:10.1105/tpc.105.031930

Cited by 125 publications

(154 citation statements)

References 63 publications

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“…The multiorganelle aggregates in mvp1-1 were similar to structures observed in two katamari mutants, kam1/mur3 (Tamura et al, 2005) and kam2/grv2 (Tamura et al, 2007;Silady et al, 2008). The kam mutants accumulate aggregates of a vacuolar protein fusion, GFP:2SC, in a manner similar to mvp1.…”

Section: Trafficking and Physiological Defects In Mvp1supporting

confidence: 60%

“…Less severe mutations have proven successful for functional genetics studies of endomembrane trafficking proteins. For example, point mutations in the KATAMARI1/MURUS3 (KAM1/MUR3; Tamura et al, 2005) and KATAMARI2/GRAVITROPISM DEFECTIVE2 (KAM2/GRV2; Tamura et al, 2007;Silady et al, 2008) genes lead to disruption of endomembranes, resulting in the formation of perinuclear aggregates containing organelles. Nonlethal trafficking disruptions have also been generated using chemical genomics, where small molecules were used to perturb trafficking of a soluble cargo protein and localization of endomembrane markers (Surpin et al, 2005;Robert et al, 2008).…”

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confidence: 99%

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MODIFIED VACUOLE PHENOTYPE1 Is an Arabidopsis Myrosinase-Associated Protein Involved in Endomembrane Protein Trafficking

et al. 2009

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We identified an Arabidopsis (Arabidopsis thaliana) ethyl methanesulfonate mutant, modified vacuole phenotype1-1 (mvp1-1), in a fluorescent confocal microscopy screen for plants with mislocalization of a green fluorescent protein-d tonoplast intrinsic protein fusion. The mvp1-1 mutant displayed static perinuclear aggregates of the reporter protein. mvp1 mutants also exhibited a number of vacuole-related phenotypes, as demonstrated by defects in growth, utilization of stored carbon, gravitropic response, salt sensitivity, and specific susceptibility to the fungal necrotroph Alternaria brassicicola. Similarly, crosses with other endomembrane marker fusions identified mislocalization to aggregate structures, indicating a general defect in protein trafficking. Map-based cloning showed that the mvp1-1 mutation altered a gene encoding a putative myrosinase-associated protein, and glutathione S-transferase pull-down assays demonstrated that MVP1 interacted specifically with the Arabidopsis myrosinase protein, THIOGLUCOSIDE GLUCOHYDROLASE2 (TGG2), but not TGG1. Moreover, the mvp1-1 mutant showed increased nitrile production during glucosinolate hydrolysis, suggesting that MVP1 may play a role in modulation of myrosinase activity. We propose that MVP1 is a myrosinase-associated protein that functions, in part, to correctly localize the myrosinase TGG2 and prevent inappropriate glucosinolate hydrolysis that could generate cytotoxic molecules.

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Section: Trafficking and Physiological Defects In Mvp1supporting

confidence: 60%

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confidence: 99%

MODIFIED VACUOLE PHENOTYPE1 Is an Arabidopsis Myrosinase-Associated Protein Involved in Endomembrane Protein Trafficking

et al. 2009

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“…Protoplasts from wild-type or mag1-1 plants were transformed with sporamin:green fluorescent protein (Spo: GFP), a chimeric LV-targeted protein fusion of sporamin from sweet potato (Ipomoea batatas) and GFP (Jin et al, 2001;Kim et al, 2001). The majority of wild-type protoplasts expressing Spo:GFP showed a vacuolar localization pattern, with a small proportion exhibiting the network and spot pattern reported previously (Sohn et al, 2003;Tamura et al, 2005). However, mag1-1 protoplasts showed a clearly different localization pattern; the majority of mag1-1 protoplasts produced a punctate staining pattern with a minor portion showing the vacuolar pattern ( Figure 1A).…”

Section: Trafficking Of Soluble Proteins To the Vacuole Is Inhibited mentioning

confidence: 97%

Trafficking of Vacuolar Proteins: The Crucial Role of Arabidopsis Vacuolar Protein Sorting 29 in Recycling Vacuolar Sorting Receptor

et al. 2012

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The retromer is involved in recycling lysosomal sorting receptors in mammals. A component of the retromer complex in Arabidopsis thaliana, vacuolar protein sorting 29 (VPS29), plays a crucial role in trafficking storage proteins to protein storage vacuoles. However, it is not known whether or how vacuolar sorting receptors (VSRs) are recycled from the prevacuolar compartment (PVC) to the trans-Golgi network (TGN) during trafficking to the lytic vacuole (LV). Here, we report that VPS29 plays an essential role in the trafficking of soluble proteins to the LV from the TGN to the PVC. maigo1-1 (mag1-1) mutants, which harbor a knockdown mutation in VPS29, were defective in trafficking of two soluble proteins, Arabidopsis aleurain-like protein (AALP):green fluorescent protein (GFP) and sporamin:GFP, to the LV but not in trafficking membrane proteins to the LV or plasma membrane or via the secretory pathway. AALP:GFP and sporamin:GFP in mag1-1 protoplasts accumulated in the TGN but were also secreted into the medium. In mag1-1 mutants, VSR1 failed to recycle from the PVC to the TGN; rather, a significant proportion was transported to the LV; VSR1 overexpression rescued this defect. Moreover, endogenous VSRs were expressed at higher levels in mag1-1 plants. Based on these results, we propose that VPS29 plays a crucial role in recycling VSRs from the PVC to the TGN during the trafficking of soluble proteins to the LV.

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“…Fine mapping identified the gene as a glycosyl-transferase family 20 member, trehalose-6-P synthase/phosphatase. With a similar strategy, a screen based on transgenic Arabidopsis EMS mutant lines expressing a soluble vacuolar marker, GFP-2sc, has been used to identify KAM1, a type II Golgi-localized protein (Tamura et al, 2005). kam1 mutants had a disrupted actin cytoskeleton and showed defects in endomembrane organization.…”

Section: Optical Imaging As a Mutant Screening Toolmentioning

confidence: 99%

“…kam1 mutants had a disrupted actin cytoskeleton and showed defects in endomembrane organization. These findings suggest the exciting possibility that KAM1 may be a key component in the Golgi-mediated organization of actin in plant cells (Tamura et al, 2005). Similarly, to identify genes involved in secretory trafficking, Teh and Moore (2007) mutagenized Arabidopsis stably expressing secreted GFP (sec-GFP), a secreted form of soluble GFP.…”

Section: Optical Imaging As a Mutant Screening Toolmentioning

confidence: 99%

Advances in Fluorescent Protein-Based Imaging for the Analysis of Plant Endomembranes

2008

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An exciting new era for live cell imaging of plant endomembranes was ushered in just over 10 years ago when Jim Haseloff and colleagues reported on the removal of a cryptic intron in the sequence of wildtype GFP for successful expression in plant cells (Haseloff et al., 1997). Haseloff's success was quickly welcomed by labs around the globe; by targeting GFP to secretory organelles, scientists could now bring to light the secret life of plant endomembranes. The plant endomembranes comprise several organelles functionally interlinked for the production and transport of secretory compounds, such as proteins, lipids, and sugars. Most of the secretory compounds are synthesized in the endoplasmic reticulum (ER) and then transported to the Golgi apparatus to be sorted for transport to distal compartments such as the plasma membrane and vacuoles. A forward transport of secretory molecules from the ER is counterbalanced by a retrograde flow from distal compartments that allows membrane homeostasis and communication with the cell's surroundings. Fluorescent protein technology applied to live cell imaging of plant endomembranes has aided immensely in providing subcellular markers for the study of the complex spatial and temporal relationships among secretory organelles. Live cell imaging is now moving forward to novel challenges. With the integration of genomic, transcriptomic, and proteomic techniques, we begin to collect data on the putative functions of plant genes; we need to understand the intricate relationships among thousands of proteins. To complete the puzzle, we must understand how the pieces fit together; we must define the functions of gene products. Important questions include: When are our proteins synthesized? Where are they targeted? With what elements do they interact? Advances in the development of optical imaging at the cellular level now offer the exciting opportunity to answer these questions.In this Update, we discuss several state-of-the-art applications of GFP imaging and how these techniques have been used to answer critical biological questions, with a focus on plant endomembrane trafficking.

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KATAMARI1/MURUS3 Is a Novel Golgi Membrane Protein That Is Required for Endomembrane Organization in Arabidopsis

Cited by 125 publications

References 63 publications

MODIFIED VACUOLE PHENOTYPE1 Is an Arabidopsis Myrosinase-Associated Protein Involved in Endomembrane Protein Trafficking

MODIFIED VACUOLE PHENOTYPE1 Is an Arabidopsis Myrosinase-Associated Protein Involved in Endomembrane Protein Trafficking

Trafficking of Vacuolar Proteins: The Crucial Role of Arabidopsis Vacuolar Protein Sorting 29 in Recycling Vacuolar Sorting Receptor

Advances in Fluorescent Protein-Based Imaging for the Analysis of Plant Endomembranes

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