Vacuolar sorting receptor for seed storage proteins in
            <i>Arabidopsis thaliana</i>

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

doi:10.1073/pnas.2530568100

Cited by 233 publications

(338 citation statements)

References 41 publications

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“…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%

“…However, little is known about the trafficking of VSRs through the SYP61 compartment. VSR1 is thought to direct ntVSS cargo to the PVC in a clathrin-dependent pathway [43], although recent studies have expanded this view by showing that ctVSS cargo follows the same route [41,44,45]. Our proteomic analysis revealed the presence of several VSRs in SYP61 vesicles, including VSR4 (At2g14720), VSR3 (At2g14740) and VSR7 (At4g20110; Supplementary information, Tables S1 and S2), with localization studies showing clearly that VSR4-YFP was colocalized with SYP61-CFP in stably transformed plants ( Figure 2D-2F).…”

Section: Vsrs In the Syp61 Compartmentmentioning

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: Vsrs In the Syp61 Compartmentmentioning

confidence: 99%

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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“…Disruption of vacuolar transport typically leads to the secretion of vacuolar proteins by a default pathway (Shimada et al, 1997(Shimada et al, , 2003a. Previously, disruption of either of the SYP41-interacting proteins, AtVPS45 or VTI12, was shown to cause the secretion of aleurain and of a vacuolar marker consisting of CLAVATA3 fused to the vacuolar sorting signal from barley (Hordeum vulgare) lectin (Sanmartín et al, 2007;Zouhar et al, 2009).…”

Section: Lack Of Tno1 Causes the Secretion Of Vacuolar Proteinsmentioning

confidence: 99%

“…In the TGN, vacuolar proteins with sequencespecific vacuolar sorting determinants are thought to be recognized by vacuolar sorting receptors (VSRs; Kirsch et al, 1994;Ahmed et al, 2000;daSilva et al, 2005), although a recent report has suggested that recognition of cargo by VSRs may occur as early as the ER (Niemes et al, 2010). Storage proteins with C-terminal sorting sequences are also bound by VSRs or by a second putative sorting receptor, RMR1 (Jiang et al, 2000;Shimada et al, 2003a;Park et al, 2005Park et al, , 2007Hinz et al, 2007). After the receptors recognize their cargo, vacuolar proteins are transported to the prevacuolar compartment (PVC; Sanderfoot et al, 1998;Happel et al, 2004;Song et al, 2006) before transport on to the vacuole.…”

mentioning

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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“…The pro-globulin trimer is formed within the endoplasmic reticulum, with the hexamer appearing during the latter stages of localization [38,39]. Requisite for hexamer assembly is proteolytic cleavage (at the β-cleavage site) to generate α-and β-subunits, each of which contains a single cupin domain, and the subsequent linkage of these subunits by an interchain disulfide bond [40,41].…”

Section: Implications Of Cruciferin Phosphorylation For Processing Amentioning

confidence: 99%

Phosphorylation of the 12 S globulin cruciferin in wild-type and abi1-1 mutant Arabidopsis thaliana (thale cress) seeds

Wan

Ross

Yang

et al. 2007

Biochemical Journal

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Cruciferin (a 12 S globulin) is the most abundant storage protein in the seeds of Arabidopsis thaliana (thale cress) and other crucifers, sharing structural similarity with the cupin superfamily of proteins. Cruciferin is synthesized as a precursor in the rough endoplasmic reticulum. Subunit assembly is accompanied by structural rearrangements involving proteolysis and disulfidebond formation prior to deposition in protein storage vacuoles. The A. thaliana cv. Columbia genome contains four cruciferin loci, two of which, on the basis of cDNA analysis, give rise to three alternatively spliced variants. Using MS, we confirmed the presence of four variants encoded by genes At4g28520.1, At5g44120.3, At1g03880.1 and At1g3890.1 in A. thaliana seeds. Two-dimensional gel electrophoresis, along with immunological detection using anti-cruciferin antiserum and antibodies against phosphorylated amino acid residues, revealed that cruciferin was the major phosphorylated protein in Arabidopsis seeds and that polymorphism far exceeded that predicted on the basis of known isoforms. The latter may be attributed, at least in part, to phosphorylation site heterogeneity. A total of 20 phosphorylation sites, comprising nine serine, eight threonine and three tyrosine residues, were identified by MS. Most of these are located on the IE (interchain disulfide-containing) face of the globulin trimer, which is involved in hexamer formation. The implications of these findings for cruciferin processing, assembly and mobilization are discussed. In addition, the protein phosphatase 2C-impaired mutant, abi1-1, was found to exhibit increased levels of cruciferin phosphorylation, suggesting either that cruciferin may be an in vivo target for this enzyme or that abi1-1 regulates the protein kinase/phosphatase system required for cruciferin phosphorylation.

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Vacuolar sorting receptor for seed storage proteins in Arabidopsis thaliana

Cited by 233 publications

References 41 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

TNO1 Is Involved in Salt Tolerance and Vacuolar Trafficking in Arabidopsis

Phosphorylation of the 12 S globulin cruciferin in wild-type and abi1-1 mutant Arabidopsis thaliana (thale cress) seeds

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