Endocytic and Secretory Traffic in <i>Arabidopsis</i> Merge in the Trans-Golgi Network/Early Endosome, an Independent and Highly Dynamic Organelle

Viotti, Corrado; Bubeck, Julia; Stierhof, York‐Dieter; Krebs, Melanie; Langhans, Markus; Berg, W. van den; Dongen, Walter Van; Richter, Sandra; Geldner, Niko; Takano, Junpei; Jürgens, Gerd; Vries, S.C. de; Robinson, David G.; Schumacher, Karin

doi:10.1105/tpc.109.072637

Cited by 424 publications

(486 citation statements)

References 66 publications

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“…The SYP61 compartment appears to function as an EE for specific PM proteins [17]. The exact role of SYP61 is unclear, but it has been implicated in stress responses induced by abscisic acid [18], and it may be involved in trafficking of components to and from the prevacuolar compartment (PVC) [6,7,15,16,19]. In order to clarify the role of SYP61, and characterize the compartment in which it resides in endomembrane trafficking, we purified SYP61 vesicles using a novel, universally adoptable immunoisolation procedure for plants and conducted a detailed proteomic analysis of the vesicle components.…”

Section: Introductionmentioning

confidence: 99%

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Isolation and proteomic analysis of the SYP61 compartment reveal its role in exocytic trafficking in Arabidopsis

et al. 2011

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The endomembrane system is a complex and dynamic intracellular trafficking network. It is very challenging to track individual vesicles and their cargos in real time; however, affinity purification allows vesicles to be isolated in their natural state so that their constituent proteins can be identified. Pioneering this approach in plants, we isolated the SYP61 trans-Golgi network compartment and carried out a comprehensive proteomic analysis of its contents with only minimal interference from other organelles. The proteome of SYP61 revealed the association of proteins of unknown function that have previously not been ascribed to this compartment. We identified a complete SYP61 SNARE complex, including regulatory proteins and validated the proteome data by showing that several of these proteins associated with SYP61 in planta. We further identified the SYP121-complex and cellulose synthases, suggesting that SYP61 plays a role in the exocytic trafficking and the transport of cell wall components to the plasma membrane. The presence of proteins of unknown function in the SYP61 proteome including ECHIDNA offers the opportunity to identify novel trafficking components and cargos. The affinity purification of plant vesicles in their natural state provides a basis for further analysis and dissection of complex endomembrane networks. The approach is widely applicable and can afford the study of several vesicle populations in plants, which can be compared with the SYP61 vesicle proteome.

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Section: Introductionmentioning

confidence: 99%

“…The TGN is considered an early endosome (EE) compartment because it is rapidly labeled with the endocytic marker FM4-64 [5]. It is implicated in endocytic, secretory trafficking and retromermediated recycling of vacuolar sorting receptors (VSRs) [6,7].…”

Section: Introductionmentioning

confidence: 99%

Isolation and proteomic analysis of the SYP61 compartment reveal its role in exocytic trafficking in Arabidopsis

et al. 2011

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“…Golgiderived structures like those in nev mutant flowers have also been seen in pollen mutants affecting the a1 subunit (VHA-a1) of the Arabidopsis vacuolar H + -ATPase proton transporter or when cells are treated with a specific V-ATPase inhibitor, concanamycin A (Dettmer et al, 2005;Liljegren et al, 2009). Recent studies have shown that the concanamycin A-induced structures are labeled with VHA-a1 and SYP61, markers of the TGN/early endosome (Viotti et al, 2010). These results suggest the possibility that the circularized structures in nev flowers are also chimeric fusions of the Golgi cisternae and the TGN and that traffic through the TGN/early endosome is affected by mutations in NEV. Disruption of CST, EVR, or SERK1 activity appears to restore the identity and independence of the TGN from the Golgi in nev flowers Lewis et al, 2010).…”

Section: Discussionmentioning

confidence: 99%

“…These results suggest the possibility that the circularized structures in nev flowers are also chimeric fusions of the Golgi cisternae and the TGN and that traffic through the TGN/early endosome is affected by mutations in NEV. Disruption of CST, EVR, or SERK1 activity appears to restore the identity and independence of the TGN from the Golgi in nev flowers Lewis et al, 2010). Defects in membrane trafficking are thought to underlie the inappropriate fusion of the TGN and the Golgi, as V-ATPase-mediated endomembrane acidification is required to recruit ARF G-proteins, ARF-GEFs, and coat components involved in vesicle budding (Zeuzem et al, 1992;Aniento et al, 1996;Maranda et al, 2001;Hurtado-Lorenzo et al, 2006;Viotti et al, 2010). As an ARF-GAP, NEV may regulate the activity and recruitment of the same TGN-localized ARF G-protein(s) and adaptor molecules as the V-ATPase complex.…”

Section: Discussionmentioning

confidence: 99%

CAST AWAY, a Membrane-Associated Receptor-Like Kinase, Inhibits Organ Abscission in Arabidopsis

et al. 2011

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Receptor-like kinase-mediated cell signaling pathways play fundamental roles in many aspects of plant growth and development. A pair of Arabidopsis (Arabidopsis thaliana) leucine-rich repeat receptor-like kinases (LRR-RLKs), HAESA (HAE) and HAESA-LIKE2 (HSL2), have been shown to activate the cell separation process that leads to organ abscission. Another pair of LRR-RLKs, EVERSHED (EVR) and SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE1, act as inhibitors of abscission, potentially by modulating HAE/HSL2 activity. Cycling of these RLKs to and from the cell surface may be regulated by NEVERSHED (NEV), a membrane trafficking regulator that is essential for organ abscission. We report here the characterization of CAST AWAY (CST), a receptor-like cytoplasmic kinase that acts as a spatial inhibitor of cell separation. Disruption of CST suppresses the abscission defects of nev mutant flowers and restores the discrete identity of the trans-Golgi network in nev abscission zones. After organ shedding, enlarged abscission zones with obscured boundaries are found in nev cst flowers. We show that CST is a dual-specificity kinase in vitro and that myristoylation at its amino terminus promotes association with the plasma membrane. Using the bimolecular fluorescence complementation assay, we have detected interactions of CST with HAE and EVR at the plasma membrane of Arabidopsis protoplasts and hypothesize that CST negatively regulates cell separation signaling directly and indirectly. A model integrating the potential roles of receptor-like kinase signaling and membrane trafficking during organ separation is presented.

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“…In Arabidopsis, the trafficking inhibitor BFA targets the Arf-GEF GNOM and induces the formation of BFA compartments (Geldner et al, 2001), most likely by homotypic fusion of the TGN (which is also an early endosome) and heterotypic fusion between the TGN and other endosomes (Dettmer et al, 2006;Lam et al, 2009;Viotti et al, 2010). Therefore, SNAREs at the TGN mayfunction in these fusion events upon BFA treatment.…”

Section: Involvement Of Tno1 In Vesicle Fusionmentioning

confidence: 99%

TNO1 Is Involved in Salt Tolerance and Vacuolar Trafficking in Arabidopsis

Kim

Bassham

2011

Plant Physiology

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The Arabidopsis (Arabidopsis thaliana) soluble N-ethylmaleimide-sensitive factor attachment protein receptor SYP41 is involved in vesicle fusion at the trans-Golgi network (TGN) and interacts with AtVPS45, SYP61, and VTI12. These proteins are involved in diverse cellular processes, including vacuole biogenesis and stress tolerance. A previously uncharacterized protein, named TNO1 (for TGN-localized SYP41-interacting protein), was identified by coimmunoprecipitation as a SYP41-interacting protein.TNO1 was found to localize to the TGN by immunofluorescence microscopy. A tno1 mutant showed increased sensitivity to high concentrations of NaCl, KCl, and LiCl and also to mannitol-induced osmotic stress. Localization of SYP61, which is involved in the salt stress response, was disrupted in the tno1 mutant. Vacuolar proteins were partially secreted to the apoplast in the tno1 mutant, suggesting that TNO1 is required for efficient protein trafficking to the vacuole. The tno1 mutant had delayed formation of the brefeldin A (BFA) compartment in cotyledons upon application of BFA, suggesting less efficient membrane fusion processes in the mutant. Unlike most TGN proteins, TNO1 does not relocate to the BFA compartment upon BFA treatment. These data demonstrate that TNO1 is involved in vacuolar trafficking and salt tolerance, potentially via roles in vesicle fusion and in maintaining TGN structure or identity.

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Endocytic and Secretory Traffic in Arabidopsis Merge in the Trans-Golgi Network/Early Endosome, an Independent and Highly Dynamic Organelle

Cited by 424 publications

References 66 publications

Isolation and proteomic analysis of the SYP61 compartment reveal its role in exocytic trafficking in Arabidopsis

Isolation and proteomic analysis of the SYP61 compartment reveal its role in exocytic trafficking in Arabidopsis

CAST AWAY, a Membrane-Associated Receptor-Like Kinase, Inhibits Organ Abscission in Arabidopsis

TNO1 Is Involved in Salt Tolerance and Vacuolar Trafficking in Arabidopsis

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