Molecular Cloning and Further Characterization of a Probable Plant Vacuolar Sorting Receptor

Paris, Nadine; Rogers, Sally W.; Jiang, Liwen; Kirsch, Thomas; Beevers, Leonard; Phillips, Thomas E.; Rogers, John C.

doi:10.1104/pp.115.1.29

Cited by 204 publications

(286 citation statements)

References 37 publications

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“…In mammalian cells, cargo receptors are recycled from their destination to the site of cargo binding (Seaman, 2005). VSR1 was found to localize to the TGN and the PVC (Paris et al, 1997;Sanderfoot et al, 1998); thus, VSR1 was also suggested to cycle between these organelles.…”

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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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TNO1 Is Involved in Salt Tolerance and Vacuolar Trafficking in Arabidopsis

Kim

Bassham

2011

Plant Physiology

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“…Research has indicated that some vacuolar cargo is packaged into clathrincoated vesicles through the action of the putative vacuolar cargo receptor AtELP/BP-80 (Ahmed et al, 1997;Paris et al, 1997;Sanderfoot et al, 1998). AtELP co-localizes with the v-SNARE AtVTI1a at the trans-Golgi network (Zheng et al, 1999b), and both proteins are probably packaged into clathrin-coated vesicles that travel to the PVC.…”

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The t-SNARE AtVAM3p Resides on the Prevacuolar Compartment in Arabidopsis Root Cells

et al. 1999

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Protein cargo is trafficked between the organelles of the endomembrane system inside transport vesicles, a process mediated by integral membrane proteins called SNAREs (soluble N-ethylmaleimide sensitive factor attachment protein receptors) that reside on the surface of the vesicle (v-SNAREs) and target membrane (t-SNAREs). In examining transport of cargo between the trans-Golgi network and the vacuole in Arabidopsis, we have previously characterized AtPEP12p as a t-SNARE residing on the prevacuolar compartment and AtVTI1a as a v-SNARE that interacts with AtPEP12p. Recently, we have begun to characterize AtVAM3p, another Arabidopsis t-SNARE that shows high sequence homology to AtPEP12p. We have found that AtVTI1a also interacts with AtVAM3p, suggesting a role for this t-SNARE in post-Golgi trafficking. AtVAM3p has been suggested to localize to the vacuolar membrane in Arabidopsis cells; however, using specific antisera and expression of epitope-tagged versions of each t-SNARE, we have discovered that AtVAM3p is found on the same prevacuolar structure as AtPEP12p in Arabidopsis root cells.

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“…Putative plant PVCs were identified using antibodies specific for the Arabidopsis (Arabidopsis thaliana) syntaxin Pep12p and the pea (Pisum sativum) vacuolar sorting receptor (VSR) BP-80 (Bassham et al, 1995;Conceicao et al, 1997;Paris et al, 1997). Studies on the relative distribution of VSR proteins between Golgi stacks and PVCs in various plant cells demonstrated that VSR proteins largely separated from Golgi markers and thus must be concentrated on PVCs under steady-state conditions (Li et al, 2002).…”

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Dynamic Response of Prevacuolar Compartments to Brefeldin A in Plant Cells

Tse

Hillmer

et al. 2006

Plant Physiology

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Little is known about the dynamics and molecular components of plant prevacuolar compartments (PVCs) in the secretory pathway. Using transgenic tobacco (Nicotiana tabacum) Bright-Yellow-2 (BY-2) cells expressing membrane-anchored yellow fluorescent protein (YFP) reporters marking Golgi or PVCs, we have recently demonstrated that PVCs are mobile multivesicular bodies defined by vacuolar sorting receptor proteins. Here, we demonstrate that Golgi and PVCs have different sensitivity in response to brefeldin A (BFA) treatment in living tobacco BY-2 cells. BFA at low concentrations (5-10 mg mL 21 ) induced YFPmarked Golgi stacks to form both endoplasmic reticulum-Golgi hybrid structures and BFA-induced aggregates, but had little effect on YFP-marked PVCs in transgenic BY-2 cells at both confocal and immunogold electron microscopy levels. However, BFA at high concentrations (50-100 mg mL 21 ) caused both YFP-marked Golgi stacks and PVCs to form aggregates in a dose-and timedependent manner. Normal Golgi or PVC signals can be recovered upon removal of BFA from the culture media. Confocal immunofluorescence and immunogold electron microscopy studies with specific organelle markers further demonstrate that the PVC aggregates are distinct, but physically associated, with Golgi aggregates in BFA-treated cells and that PVCs might lose their internal vesicle structures at high BFA concentration. In addition, vacuolar sorting receptor-marked PVCs in root-tip cells of tobacco, pea (Pisum sativum), mung bean (Vigna radiata), and Arabidopsis (Arabidopsis thaliana) upon BFA treatment are also induced to form similar aggregates. Thus, we have demonstrated that the effects of BFA are not limited to endoplasmic reticulum and Golgi, but extend to PVC in the endomembrane system, which might provide a quick tool for distinguishing Golgi from PVC for its identification and characterization, as well as a possible new tool in studying PVC-mediated protein traffic in plant cells.

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Molecular Cloning and Further Characterization of a Probable Plant Vacuolar Sorting Receptor

Cited by 204 publications

References 37 publications

TNO1 Is Involved in Salt Tolerance and Vacuolar Trafficking in Arabidopsis

TNO1 Is Involved in Salt Tolerance and Vacuolar Trafficking in Arabidopsis

The t-SNARE AtVAM3p Resides on the Prevacuolar Compartment in Arabidopsis Root Cells

Dynamic Response of Prevacuolar Compartments to Brefeldin A in Plant Cells

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