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  • 1
    Language: English
    In: eLife, 2014-04-08, Vol.3, p.e02131-e02131
    Description: Membrane trafficking is essential to fundamental processes in eukaryotic life, including cell growth and division. In plant cytokinesis, post-Golgi trafficking mediates a massive flow of vesicles that form the partitioning membrane but its regulation remains poorly understood. Here, we identify functionally redundant Arabidopsis ARF guanine-nucleotide exchange factors (ARF-GEFs) BIG1-BIG4 as regulators of post-Golgi trafficking, mediating late secretion from the trans-Golgi network but not recycling of endocytosed proteins to the plasma membrane, although the TGN also functions as an early endosome in plants. In contrast, BIG1-4 are absolutely required for trafficking of both endocytosed and newly synthesized proteins to the cell-division plane during cytokinesis, counteracting recycling to the plasma membrane. This change from recycling to secretory trafficking pathway mediated by ARF-GEFs confers specificity of cargo delivery to the division plane and might thus ensure that the partitioning membrane is completed on time in the absence of a cytokinesis-interphase checkpoint. DOI: http://dx.doi.org/10.7554/eLife.02131.001.
    Subject(s): Arabidopsis Proteins - metabolism ; Endocytosis ; Cell Division ; Golgi Apparatus - metabolism ; Arabidopsis Proteins - secretion ; Arabidopsis - metabolism ; Protein Transport ; Seeds ; Cytokinesis ; Guanine ; Golgi apparatus ; Proteins ; Microscopy ; Phylogenetics ; Membrane trafficking ; Physiology ; Software ; Flowers & plants ; Recycling ; Molecular biology ; Guanine nucleotide exchange factor ; Localization ; Plant Biology ; ARF-GEF ; secretion ; Arabidopsis ; cell division ; post-Golgi trafficking ; recycling ; gegulation of vesicle traffic ; Cell Biology
    ISSN: 2050-084X
    E-ISSN: 2050-084X
    Source: PubMed Central
    Source: DOAJ Directory of Open Access Journals - Not for CDI Discovery
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  • 2
    Language: English
    In: eLife, 2017-05-19, Vol.6
    Description: Intracellular membrane fusion mediates diverse processes including cell growth, division and communication. Fusion involves complex formation between SNARE proteins anchored to adjacent membranes. How and in what form interacting SNARE proteins reach their sites of action is virtually unknown. We have addressed this problem in the context of plant cell division in which a large number of TGN-derived membrane vesicles fuse with one another to form the partitioning membrane. Blocking vesicle formation at the TGN revealed -SNARE complexes. These inactive cytokinetic SNARE complexes were already assembled at the endoplasmic reticulum and, after passage through Golgi/TGN to the cell division plane, transformed into fusogenic SNARE complexes. This mode of trafficking might ensure delivery of large stoichiometric quantities of SNARE proteins required for forming the partitioning membrane in the narrow time frame of plant cytokinesis. Such long-distance trafficking of inactive SNARE complexes would also facilitate directional growth processes during cell differentiation.
    Subject(s): Endoplasmic Reticulum - metabolism ; Arabidopsis - physiology ; Cell Membrane - metabolism ; Cytokinesis ; SNARE Proteins - metabolism ; Protein Transport ; Physiological aspects ; Cell membranes ; Observations ; Arabidopsis ; Endoplasmic reticulum ; Proteins ; Membrane fusion ; Cell division ; Intracellular signalling ; Membrane vesicles ; SNAP receptors ; Mutation ; Molecular biology ; Cell interactions ; Golgi cells ; Plant Biology ; cytokinesis ; A. thaliana ; Short Report ; SNARE complex ; membrane traffic ; Cell Biology ; membrane fusion
    ISSN: 2050-084X
    E-ISSN: 2050-084X
    Source: PubMed Central
    Source: DOAJ Directory of Open Access Journals - Not for CDI Discovery
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  • 3
    Language: English
    In: Plant physiology (Bethesda), 2004-02-01, Vol.134 (2), p.625-639
    Description: Protein storage vacuoles (PSVs) are specialized vacuoles devoted to the accumulation of large amounts of protein in the storage tissues of plants. In this study, we investigated the presence of the storage vacuole and protein trafficking to the compartment in cells of tobacco (Nicotiana tabacum), common bean (Phaseolus vulgaris), and Arabidopsis leaf tissue. When we expressed phaseolin, the major storage protein of common bean, or an epitope-tagged version of α-tonoplast intrinsic protein (α-TIP, a tonoplast aquaporin of PSV), in protoplasts derived from leaf tissues, these proteins were targeted to a compartment ranging in size from 2 to 5 μm in all three plant species. Most Arabidopsis leaf cells have one of these organelles. In contrast, from one to five these organelles occurred in bean and tobacco leaf cells. Also, endogenous α-TIP is localized in a similar compartment in untransformed leaf cells of common bean and is colocalized with transiently expressed epitope-tagged α-TIP. In Arabidopsis, phaseolin contained N-glycans modified by Golgi enzymes and its traffic was sensitive to brefeldin A. However, trafficking of α-TIP was insensitive to brefeldin A treatment and was not affected by the dominant-negative mutant of AtRab1. In addition, a modified α-TIP with an insertion of an N-glycosylation site has the endoplasmic reticulum-type glycans. Finally, the early step of phaseolin traffic, from the endoplasmic reticulum to the Golgi complex, required the activity of the small GTPase Sar1p, a key component of coat protein complex II-coated vesicles, independent of the presence of the vacuolar sorting signal in phaseolin. Based on these results, we propose that the proteins we analyzed are targeted to the PSV or equivalent organelle in leaf cells and that proteins can be transported to the PSV by two different pathways, the Golgi-dependent and Golgi-independent pathways, depending on the individual cargo proteins.
    Subject(s): Proteins ; Protoplasts ; Traffic ; Antibodies ; Cell Biology and Signal Transduction ; Plants ; Organelles ; Vacuoles ; Storage proteins ; Plant cells ; Golgi apparatus ; Fundamental and applied biological sciences. Psychology ; Storage and secretion, pigments, phytochrome ; Economic plant physiology ; Reserves and secretions. Pigments. Phytochromes ; Plant physiology and development ; Biological and medical sciences ; Nutrition. Photosynthesis. Respiration. Metabolism ; Agronomy. Soil science and plant productions ; Metabolism ; Immunohistochemistry ; Brefeldin A - pharmacology ; rab GTP-Binding Proteins - genetics ; Protein Transport - drug effects ; Arabidopsis Proteins - metabolism ; Phaseolus - genetics ; Plants - genetics ; Gene Expression Regulation, Plant ; Membrane Proteins - metabolism ; Plant Proteins - metabolism ; rab GTP-Binding Proteins - metabolism ; Arabidopsis Proteins - genetics ; Membrane Proteins - genetics ; Tobacco - metabolism ; Plant Leaves - cytology ; Arabidopsis - metabolism ; Arabidopsis - genetics ; Phaseolus - metabolism ; Plant Proteins - genetics ; Plants - metabolism ; Plant Leaves - genetics ; Plant Leaves - metabolism ; Tobacco - genetics ; Vacuoles - metabolism ; Golgi Apparatus - metabolism ; Mutation ; Protein research ; Glycosylation ; Research ; Analysis
    ISSN: 0032-0889
    E-ISSN: 1532-2548
    Source: American Society of Plant Biologists
    Source: JSTOR Life Sciences
    Source: Hellenic Academic Libraries Link
    Source: JSTOR Ecology & Botany II
    Source: PubMed Central
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  • 4
    Language: English
    In: The Journal of cell biology, 2005-08-29, Vol.170 (5), p.757-767
    Description: Organellar proteins are sorted by cargo receptors on the way to their final destination. However, receptors for proteins that are destined for the protein storage vacuole (PSV) are largely unknown. In this study, we investigated the biological role that Arabidopsis thaliana receptor homology region transmembrane domain ring H2 motif protein (AtRMR) 1 plays in protein trafficking to the PSV. AtRMR1 mainly colocalized to the prevacuolar compartment of the PSV, but a minor portion also localized to the Golgi complex. The coexpression of AtRMR1 mutants that were localized to the Golgi complex strongly inhibited the trafficking of phaseolin to the PSV and caused accumulation of phaseolin in the Golgi complex or its secretion. Coimmunoprecipitation and in vitro binding assays revealed that the lumenal domain of AtRMR1 interacts with the COOH-terminal sorting signal of phaseolin at acidic pH. Furthermore, phaseolin colocalized with AtRMR1 on its way to the PSV. Based on these results, we propose that AtRMR1 functions as the sorting receptor of phaseolin for its trafficking to the PSV.
    Subject(s): Proteins ; Receptors ; Protoplasts ; Antibodies ; Organelles ; Vacuoles ; Freight ; Storage proteins ; Plant cells ; Golgi apparatus ; Protein Structure, Tertiary ; Arabidopsis Proteins - genetics ; Membrane Proteins - genetics ; Protein Transport - physiology ; Recombinant Fusion Proteins - metabolism ; Plant Leaves - cytology ; Protein Sorting Signals ; Arabidopsis - metabolism ; Arabidopsis Proteins - metabolism ; Protoplasts - metabolism ; Plant Leaves - metabolism ; Protoplasts - ultrastructure ; Recombinant Fusion Proteins - genetics ; Vacuoles - metabolism ; Golgi Apparatus - metabolism ; Membrane Proteins - metabolism ; Mutation ; Arabidopsis thaliana ; Research
    ISSN: 0021-9525
    E-ISSN: 1540-8140
    Source: HighWire Press (Free Journals)
    Source: Rockefeller University Press
    Source: Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals
    Source: PubMed Central
    Source: Alma/SFX Local Collection
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  • 5
    Language: English
    In: The Plant cell, 2005-03-01, Vol.17 (3), p.888-902
    Description: Actin filaments are thought to play an important role in intracellular trafficking in various eukaryotic cells. However, their involvement in intracellular trafficking in plant cells has not been clearly demonstrated. Here, we investigated the roles actin filaments play in intracellular trafficking in plant cells using latrunculin B (Lat B), an inhibitor of actin filament assembly, or actin mutants that disrupt actin filaments when overexpressed. Lat B and actin2 mutant overexpression inhibited the trafficking of two vacuolar reporter proteins, sporamin:green fluorescent protein (GFP) and Arabidopsis thaliana aleurainlike protein:GFP, to the central vacuole; instead, a punctate staining pattern was observed. Colocalization experiments with various marker proteins indicated that these punctate stains corresponded to the Golgi complex. The A. thaliana vacuolar sorting receptor VSR-At, which mainly localizes to the prevacuolar compartment, also accumulated at the Golgi complex in the presence of Lat B. However, Lat B had no effect on the endoplasmic reticulum (ER) to Golgi trafficking of sialytransferase or retrograde Golgi to ER trafficking. Lat B also failed to influence the Golgi to plasma membrane trafficking of or the secretion of invertase:GFP. Based on these observations, we propose that actin filaments play a critical role in the trafficking of proteins from the Golgi complex to the central vacuole.
    Subject(s): Gels ; Microfilaments ; Secretion ; Protoplasts ; Actins ; Antibodies ; Cell membranes ; Vacuoles ; Plant cells ; Golgi apparatus ; Arabidopsis Proteins - genetics ; Genes, Plant ; Arabidopsis - cytology ; Biological Transport, Active - drug effects ; Actins - metabolism ; Endoplasmic Reticulum - metabolism ; Recombinant Fusion Proteins - metabolism ; Actins - genetics ; Arabidopsis - metabolism ; Arabidopsis - genetics ; Arabidopsis Proteins - metabolism ; Bridged Bicyclo Compounds, Heterocyclic - pharmacology ; Thiazolidines ; Base Sequence ; Plants, Genetically Modified ; Recombinant Fusion Proteins - genetics ; Vacuoles - metabolism ; Golgi Apparatus - metabolism ; Cell Membrane - metabolism ; Thiazoles - pharmacology ; Mutation ; DNA, Plant - genetics ; Plant cells and tissues ; Research ; Actin ; s
    ISSN: 1040-4651
    E-ISSN: 1532-298X
    Source: American Society of Plant Biologists
    Source: JSTOR Life Sciences
    Source: JSTOR Ecology & Botany II
    Source: Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals
    Source: PubMed Central
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  • 6
    Language: English
    In: Proceedings of the National Academy of Sciences - PNAS, 2013-06-18, Vol.110 (25), p.10318-10323
    Description: Adaptor protein (AP) complexes are the predominant coat proteins of membrane vesicles in post-Golgi trafficking of mammalian cells. Each AP complex contains a specific medium subunit, µ-adaptin, that selects cargo proteins bearing sequence-specific sorting motifs. Much less is known about the AP complexes and their µ subunits in plants. Because of uncertain homology, the µ-adaptins of Arabidopsis have been designated muA through muD [Happel et al. (2004) Plant J 37(5):678-693]. Furthermore, only muD has been assigned to a specific AP complex, AP-3, involved in Golgi-vacuolar trafficking [Niihama et al. (2009) Plant Cell Physiol 50(12):2057-2068, Zwiewka et al. (2011) Cell Res 21(12):1711-1722, and Wolfenstetter et al. (2012) Plant Cell 24(1):215-232]. In contrast the µ subunit of neither the post-Golgi trafficking AP-1 complex nor the endocytic AP-2 complex has been identified. Here, we report the functional analysis of redundant AP-1 µ-adaptins AP1M1 (also known as muB1) and AP1M2 (also known as muB2). Coimmunoprecipitation revealed that both AP1M2 and its less strongly expressed isoform AP1M1 are complexed with the large subunit γ-adaptin of AP-1. In addition, AP1M2 was localized at or near the trans-Golgi network. Knockout mutations of AP1M2 impaired pollen function and arrested plant growth whereas the ap1m1 ap1m2 double mutant was nearly pollen-lethal. At the cellular level, the absence of AP1M2 entailed inhibition of multiple trafficking pathways from the frans-Golgi network to the vacuole and to the plasma membrane in interphase and to the plane of cell division in cytokinesis. Thus, AP-1 is crucial in post-Golgi trafficking in plant cells and required for cell division and plant growth.
    Subject(s): Phenotypes ; Epithelial cells ; Biological transport ; Protoplasts ; Cell membranes ; Plants ; Vacuoles ; Freight ; Plant cells ; Seedlings ; Vacuoles - ultrastructure ; Adaptor Protein Complex gamma Subunits - metabolism ; Adaptor Protein Complex mu Subunits - metabolism ; Interphase - physiology ; Arabidopsis - growth & development ; Secretory Vesicles - metabolism ; Protein Transport - physiology ; Adaptor Protein Complex alpha Subunits - metabolism ; Cell Membrane - physiology ; Adaptor Protein Complex 1 - metabolism ; Arabidopsis Proteins - metabolism ; Adaptor Protein Complex 1 - genetics ; trans-Golgi Network - metabolism ; Cytokinesis - physiology ; Golgi Apparatus - ultrastructure ; Microscopy, Electron, Transmission ; Arabidopsis Proteins - genetics ; Adaptor Protein Complex mu Subunits - genetics ; Secretory Vesicles - ultrastructure ; Cell Membrane - ultrastructure ; Arabidopsis - metabolism ; Arabidopsis - genetics ; trans-Golgi Network - ultrastructure ; Vacuoles - metabolism ; Golgi Apparatus - metabolism ; Mutagenesis, Insertional ; Biological Sciences ; adaptor complex 1 ; secretory pathway ; development ; membrane traffic
    ISSN: 0027-8424
    E-ISSN: 1091-6490
    Source: JSTOR Life Sciences
    Source: HighWire Press (Free Journals)
    Source: Hellenic Academic Libraries Link
    Source: PubMed Central
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  • 7
    Language: English
    In: Proceedings of the National Academy of Sciences - PNAS, 2018-06-12, Vol.115 (24), p.6309-6314
    Description: Sec1/Munc18 (SM) proteins contribute to membrane fusion by interacting with Qa-SNAREs or nascent -SNARE complexes. Gymnosperms and the basal angiosperm have only a single gene related to the gene in . However, the genomes of most angiosperms including encode three SEC1-related SM proteins of which only KEULE has been functionally characterized as interacting with the cytokinesis-specific Qa-SNARE KNOLLE during cell-plate formation. Here we analyze the closest paralog of KEULE named SEC1B. In contrast to the cytokinesis defects of mutants, mutants are homozygous viable. However, the double mutant was nearly gametophytically lethal, displaying collapsed pollen grains, which suggests substantial overlap between SEC1B and KEULE functions in secretion-dependent growth. SEC1B had a strong preference for interaction with the evolutionarily ancient Qa-SNARE SYP132 involved in secretion and cytokinesis, whereas KEULE interacted with both KNOLLE and SYP132. This differential interaction with Qa-SNAREs is likely conferred by domains 1 and 2a of the two SM proteins. Comparative analysis of all four possible combinations of the relevant SEC1 Qa-SNARE double mutants revealed that in cytokinesis, the interaction of SEC1B with KNOLLE plays no role, whereas the interaction of KEULE with KNOLLE is prevalent and functionally as important as the interactions of both SEC1B and KEU with SYP132 together. Our results suggest that functional diversification of the two SEC1-related SM proteins during angiosperm evolution resulted in enhanced interaction of SEC1B with Qa-SNARE SYP132, and thus a predominant role of SEC1B in secretion.
    Subject(s): Arabidopsis Proteins - metabolism ; Carrier Proteins - metabolism ; Cytokinesis - physiology ; Qa-SNARE Proteins - metabolism ; Munc18 Proteins - metabolism ; Protein Transport - physiology ; Cell Membrane - metabolism ; Cell Membrane - physiology ; Membrane Fusion - physiology ; Arabidopsis - metabolism ; Arabidopsis thaliana ; Plant proteins ; Physiological aspects ; Biological Sciences ; cell-plate formation ; secretion ; SEC1 ; Qa-SNAREs ; membrane traffic ; Munc18
    ISSN: 0027-8424
    E-ISSN: 1091-6490
    Source: JSTOR Life Sciences
    Source: HighWire Press (Free Journals)
    Source: Hellenic Academic Libraries Link
    Source: PubMed Central
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  • 8
    Article
    Article
    2011
    ISSN: 1664-462X 
    Language: English
    In: Frontiers in plant science, 2011, Vol.2, p.111-111
    Description: Complete sequencing of the Arabidopsis genome a decade ago has facilitated the functional analysis of various biological processes including membrane traffic by which many proteins are delivered to their sites of action and turnover. In particular, membrane traffic between post-Golgi compartments plays an important role in cell signaling, taking care of receptor-ligand interaction and inactivation, which requires secretion, endocytosis, and recycling or targeting to the vacuole for degradation. Here, we discuss recent studies that address the identity of post-Golgi compartments, the machinery involved in traffic and fusion or functionally characterized cargo proteins that are delivered to or pass through post-Golgi compartments. We also provide an outlook on future challenges in this area of research.
    Subject(s): Plant Science ; endosome ; secretion ; plant ; endocytosis ; recycling ; exocytosis ; trans-Golgi network ; Endocytosis ; Recycling ; Exocytosis ; trans-Golgi Network
    ISSN: 1664-462X
    E-ISSN: 1664-462X
    Source: PubMed Central
    Source: DOAJ Directory of Open Access Journals - Not for CDI Discovery
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  • 9
    Language: English
    In: Plant physiology (Bethesda), 2004-02-01, Vol.134 (2), p.625-639
    Description: Protein storage vacuoles (PSVs) are specialized vacuoles devoted to the accumulation of large amounts of protein in the storage tissues of plants. In this study, we investigated the presence of the storage vacuole and protein trafficking to the compartment in cells of tobacco (Nicotiana tabacum), common bean (Phaseolus vulgaris), and Arabidopsis leaf tissue. When we expressed phaseolin, the major storage protein of common bean, or an epitope-tagged version of alpha-tonoplast intrinsic protein (alpha-TIP, a tonoplast aquaporin of PSV), in protoplasts derived from leaf tissues, these proteins were targeted to a compartment ranging in size from 2 to 5 microm in all three plant species. Most Arabidopsis leaf cells have one of these organelles. In contrast, from one to five these organelles occurred in bean and tobacco leaf cells. Also, endogenous alpha-TIP is localized in a similar compartment in untransformed leaf cells of common bean and is colocalized with transiently expressed epitope-tagged alpha-TIP. In Arabidopsis, phaseolin contained N-glycans modified by Golgi enzymes and its traffic was sensitive to brefeldin A. However, trafficking of alpha-TIP was insensitive to brefeldin A treatment and was not affected by the dominant-negative mutant of AtRab1. In addition, a modified alpha-TIP with an insertion of an N-glycosylation site has the endoplasmic reticulum-type glycans. Finally, the early step of phaseolin traffic, from the endoplasmic reticulum to the Golgi complex, required the activity of the small GTPase Sar1p, a key component of coat protein complex II-coated vesicles, independent of the presence of the vacuolar sorting signal in phaseolin. Based on these results, we propose that the proteins we analyzed are targeted to the PSV or equivalent organelle in leaf cells and that proteins can be transported to the PSV by two different pathways, the Golgi-dependent and Golgi-independent pathways, depending on the individual cargo proteins.
    ISSN: 0032-0889
    E-ISSN: 1532-2548
    Source: American Society of Plant Biologists
    Source: JSTOR Life Sciences
    Source: Hellenic Academic Libraries Link
    Source: JSTOR Ecology & Botany II
    Source: PubMed Central
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  • 10
    Language: English
    In: Developmental cell, 2012-05-15, Vol.22 (5), p.989-1000
    Description: Intracellular membrane fusion requires complexes of syntaxins with other SNARE proteins and regulatory Sec1/Munc18 (SM) proteins. In membrane fusion mediating, e.g., neurotransmitter release or glucose-stimulated insulin secretion in mammals, SM proteins preferentially interact with the inactive closed, rather than the active open, conformation of syntaxin or with the assembled SNARE complex. Other membrane fusion processes such as vacuolar fusion in yeast involve like membranes carrying cis-SNARE complexes, and the role of SM protein is unknown. We investigated syntaxin-SM protein interaction in membrane fusion of Arabidopsis cytokinesis, which involves cytokinesis-specific syntaxin KNOLLE and SM protein KEULE. KEULE interacted with an open conformation of KNOLLE that complemented both knolle and keule mutants. This interaction occurred at the cell division plane and required the KNOLLE linker sequence between helix Hc and SNARE domain. Our results suggest that in cytokinesis, SM protein stabilizes the fusion-competent open form of syntaxin, thereby promoting trans-SNARE complex formation. ► Interaction of syntaxin KNOLLE with SM protein KEULE is a pivotal step in cytokinesis ► KEULE interacts with the open, rather than the closed, conformation of KNOLLE ► The KNOLLE SNARE domain-adjacent linker is a sequence-specific binding site for KEULE ► Expression of a constitutively open form of KNOLLE bypasses the requirement of KEULE Intracellular vesicular membrane fusion requires complex formation between syntaxins, SNAREs, and regulatory Sec1/Munc18 (SM) proteins. Park et al. provide evidence that in plant cytokinesis, unlike other contexts, stabilization of an open syntaxin conformation by the SM protein is key to the formation of the partition membrane through vesicular fusion.
    Subject(s): Fundamental and applied biological sciences. Psychology ; Cell differentiation, maturation, development, hematopoiesis ; Secretion. Exocytosis ; Biological and medical sciences ; Cell physiology ; Molecular and cellular biology ; Cell cycle, cell proliferation ; Arabidopsis - cytology ; Munc18 Proteins - metabolism ; Mutant Proteins - metabolism ; Arabidopsis - metabolism ; Arabidopsis Proteins - metabolism ; Microscopy, Confocal ; Two-Hybrid System Techniques ; Carrier Proteins - metabolism ; Cytokinesis - physiology ; Qa-SNARE Proteins - metabolism ; Protein Binding ; Protein Conformation ; Membrane Fusion - physiology ; Intracellular Membranes - metabolism ; Vacuoles ; Proteins ; Arabidopsis thaliana ; Arabidopsis
    ISSN: 1534-5807
    E-ISSN: 1878-1551
    Source: Cell Press Collection [ECCPC]
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