Vacuolar protein sorting mechanisms in plants

Li, Xiang; Etxeberria, Ed; Ende, Wim Van den

doi:10.1111/febs.12092

Cited by 100 publications

(110 citation statements)

References 206 publications

(277 reference statements)

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“…In general, the protein secretory pathway in plants begins in the ER, passes through the Golgi complex, and finally reaches its final destination, which may be the vacuole, other compartments, or the extracellular space. The movement between the components in the pathway is mainly by vesicle trafficking (Xiang et al, 2013). In the mature litchi pericarp cells, most of the organelles were disintegrated, and ER, Golgi complex, and cytoplasm were hardly observed.…”

Section: The Litchi Ade/lac Is Located In the Vacuole Of The Pericarpmentioning

confidence: 99%

An Intracellular Laccase is Responsible for the Epicatechin Mediated Anthocyanin Degradation in Litchi Fruit Pericarp

Fang¹,

et al. 2015

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Section: The Litchi Ade/lac Is Located In the Vacuole Of The Pericarpmentioning

confidence: 99%

An Intracellular Laccase is Responsible for the Epicatechin Mediated Anthocyanin Degradation in Litchi Fruit Pericarp

Fang¹,

et al. 2015

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“…In general, vacuolar proteins are synthesized on the rough endoplasmic reticulum and then transported to vacuoles via the Golgi apparatus (Xiang et al, 2013;Robinson and Pimpl, 2014). The vacuolar trafficking in plants has been studied by monitoring the transport of reporter proteins to lytic vacuoles in vegetative cells and tissues (Jin et al, 2001;Pimpl et al, 2003;Miao et al, 2008;Niemes et al, 2010).…”

mentioning

confidence: 99%

The Adaptor Complex AP-4 Regulates Vacuolar Protein Sorting at the trans-Golgi Network by Interacting with VACUOLAR SORTING RECEPTOR1

et al. 2015

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Adaptor protein (AP) complexes play critical roles in protein sorting among different post-Golgi pathways by recognizing specific cargo protein motifs. Among the five AP complexes (AP-1-AP-5) in plants, AP-4 is one of the most poorly understood; the AP-4 components, AP-4 cargo motifs, and AP-4 functional mechanism are not known. Here, we identify the AP-4 components and show that the AP-4 complex regulates receptor-mediated vacuolar protein sorting by recognizing VACUOLAR SORTING RECEPTOR1 (VSR1), which was originally identified as a sorting receptor for seed storage proteins to target protein storage vacuoles in Arabidopsis (Arabidopsis thaliana). From the vacuolar sorting mutant library GREEN FLUORESCENT SEED (GFS), we isolated three gfs mutants that accumulate abnormally high levels of VSR1 in seeds and designated them as gfs4, gfs5, and gfs6. Their responsible genes encode three (AP4B, AP4M, and AP4S) of the four subunits of the AP-4 complex, respectively, and an Arabidopsis mutant (ap4e) lacking the fourth subunit, AP4E, also had the same phenotype. Mass spectrometry demonstrated that these four proteins form a complex in vivo. The four mutants showed defects in the vacuolar sorting of the major storage protein 12S globulins, indicating a role for the AP-4 complex in vacuolar protein transport. AP4M bound to the tyrosine-based motif of VSR1. AP4M localized at the trans-Golgi network (TGN) subdomain that is distinct from the AP-1-localized TGN subdomain. This study provides a novel function for the AP-4 complex in VSR1-mediated vacuolar protein sorting at the specialized domain of the TGN.

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“…As many nonstructured C‐terminal peptide sequences have been reported to direct vacuole targeting in plants (Xiang et al ., 2013), it may explain the observed vacuole‐targeting property of the C‐terminal F2A extension. To this end, another notable observation from this study is that some of the RFP Strep released from the ND‐4 polyprotein accumulated inside the vacuole (Figure 7d, ND‐4) although we did also detect extracellular RFP (Figure 7b).…”

Section: Resultsmentioning

confidence: 92%

Coordinated protein co‐expression in plants by harnessing the synergy between an intein and a viral 2A peptide

Zhang

Rapolu

Kumar³

et al. 2017

Plant Biotechnology Journal

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SummaryA novel approach is developed for coordinated expression of multiple proteins from a single transgene in plants. An Ssp DnaE mini‐intein variant engineered for hyper‐N‐terminal autocleavage is covalently linked to the foot‐and‐mouth disease virus 2A (F2A) peptide with unique ribosome skipping property, via a peptide linker, to create an ‘IntF2A’ self‐excising fusion protein domain. This IntF2A domain acts, in cis, to direct highly effective release of its flanking proteins of interest (POIs) from a ‘polyprotein’ precursor in plants. This is successfully demonstrated in stably transformed cultured tobacco cells as well as in different organs of transgenic tobacco plants. Highly efficient polyprotein processing mediated by the IntF2A domain was also demonstrated in lettuce and Nicotiana benthamiana based on transient expression. Protein constituents released from the polyprotein precursor displayed proper function and accumulated at similar levels inside the cells. Importantly, no C‐terminal F2A extension remains on the released POIs. We demonstrated co‐expression of as many as three proteins in plants without compromising expression levels when compared with those using single‐protein vectors. Accurate differential cellular targeting of released POIs is also achieved. In addition, we succeeded in expressing a fully assembled and functional chimeric anti‐His Tag antibody in N. benthamiana leaves. The IntF2A‐based polyprotein transgene system overcomes key impediments of existing strategies for multiprotein co‐expression in plants, which is particularly important for gene/trait stacking.

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Vacuolar protein sorting mechanisms in plants

Cited by 100 publications

References 206 publications

An Intracellular Laccase is Responsible for the Epicatechin Mediated Anthocyanin Degradation in Litchi Fruit Pericarp

An Intracellular Laccase is Responsible for the Epicatechin Mediated Anthocyanin Degradation in Litchi Fruit Pericarp

The Adaptor Complex AP-4 Regulates Vacuolar Protein Sorting at the trans-Golgi Network by Interacting with VACUOLAR SORTING RECEPTOR1

Coordinated protein co‐expression in plants by harnessing the synergy between an intein and a viral 2A peptide

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