Functional specialization within the vacuolar sorting receptor family: VSR1, VSR3 and VSR4 sort vacuolar storage cargo in seeds and vegetative tissues

Zouhar, Jan; Muñoz, Alfonso; Rojo, Enrique

doi:10.1111/j.1365-313x.2010.04349.x

Cited by 73 publications

(101 citation statements)

References 44 publications

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“…The SYP61 proteome included two Qa-SNARE proteins (SYP41 and SYP43), one Qb protein (VTI12), the bait Qc protein SYP61 and the regulatory protein VPS45. Immunocytochemical experiments with protoplasts isolated from SYP61-CFP transgenic plants confirmed the localization of VPS45 (Supplementary information, Figure S3A-S3C) and corroborate with previous reports describing a SYP41/SYP61/VTI12 SNARE complex [16,19,29]. Other SYP4 members such as SYP43 were also found in the SYP61 vesicle proteome, establishing new protein association with SYP61.…”

Section: The Syp61 Proteome Includes a Complete Snare Complex And Itssupporting

confidence: 75%

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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: The Syp61 Proteome Includes a Complete Snare Complex And Itssupporting

confidence: 75%

“…Arabidopsis has seven VSR homologs (AtVSR1-AtVSR7), and thus far the functions of VSR1, VSR3 and VSR4 have been mainly investigated using genetic approaches [29,41,42]. However, little is known about the trafficking of VSRs through the SYP61 compartment.…”

Section: Vsrs In the Syp61 Compartmentmentioning

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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“…We observed high abundance of Vacuolar Sorting Receptor3 (VSR3; rank 9) and VSR4 (rank 12) as well as ECHIDNA, RAN1 (copper-transporting ATPase), Vacuolar Proton ATPase-a1, Yip1 integral membrane domain-containing protein, and Syntaxin43. VSR3 and VSR4 are two of the main isoforms that participate in vacuolar sorting in Arabidopsis (Zouhar et al, 2010).…”

Section: Abundance Of the Trans-golgi Network Proteinsmentioning

confidence: 99%

Label-Free Protein Quantification for Plant Golgi Protein Localization and Abundance

et al. 2014

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The proteomic composition of the Arabidopsis (Arabidopsis thaliana) Golgi apparatus is currently reasonably well documented; however, little is known about the relative abundances between different proteins within this compartment. Accurate quantitative information of Golgi resident proteins is of great importance: it facilitates a better understanding of the biochemical processes that take place within this organelle, especially those of different polysaccharide synthesis pathways. Golgi resident proteins are challenging to quantify because the abundance of this organelle is relatively low within the cell. In this study, an organelle fractionation approach targeting the Golgi apparatus was combined with a label-free quantitative mass spectrometry (dataindependent acquisition method using ion mobility separation known as LC-IMS-MS E [or HDMS E ]) to simultaneously localize proteins to the Golgi apparatus and assess their relative quantity. In total, 102 Golgi-localized proteins were quantified. These data show that organelle fractionation in conjunction with label-free quantitative mass spectrometry is a powerful and relatively simple tool to access protein organelle localization and their relative abundances. The findings presented open a unique view on the organization of the plant Golgi apparatus, leading toward unique hypotheses centered on the biochemical processes of this organelle.

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“…In plant cells, proteins known as vacuolar sorting receptors (VSRs) are involved in this process. In Arabidopsis thaliana, seven VSR isoforms have been identified (Ahmed et al, 1997;Shimada et al, 2003;Zouhar et al, 2010). They are type I membrane proteins and are highly conserved in different plant species (Kirsch et al, 1994(Kirsch et al, , 1996Ahmed et al, 1997;Paris and Neuhaus, 2002).…”

Section: Introductionmentioning

confidence: 99%

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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Functional specialization within the vacuolar sorting receptor family: VSR1, VSR3 and VSR4 sort vacuolar storage cargo in seeds and vegetative tissues

Cited by 73 publications

References 44 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

Label-Free Protein Quantification for Plant Golgi Protein Localization and Abundance

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

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