ArticleThe Plant cell2001
A vacuolar sorting domain may also influence the way in which proteins leave the endoplasmic reticulum.
Article in The Plant cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 85 citations in OpenAlex.
- Heterologous Production of Cyprosin B in Nicotiana benthamiana: Unveiling the Role of the Plant-Specific Insert Domain in Protein Function and Subcellular Localisation.Plant biotechnology journal · 2026Article
- Shifting Routes: Plant-Specific Insert Trafficking and Function in Arabidopsis Seedlings Under Abiotic Stress.Plant direct · 2025Article
- Aspartic proteases from Silybum marianum: different plant-specific inserts, different destinations.Planta · 2025Article
- Interaction Dynamics of Plant-Specific Insert Domains fromMolecules (Basel, Switzerland) · 2024Article
- Insights into the mechanism of membrane fusion induced by the plant defense element, plant-specific insert.The Journal of biological chemistry · 2020Article
- Plant Aspartic Proteases for Industrial Applications: Thistle Get Better.Plants (Basel, Switzerland) · 2020Review
- N-Linked Glycosylation Modulates Golgi-Independent Vacuolar Sorting Mediated by the Plant Specific Insert.Plants (Basel, Switzerland) · 2019Article
- An Arabidopsis protoplast isolation method reduces cytosolic acidification and activation of the chloroplast stress sensor SENSITIVE TO FREEZING 2.Plant signaling & behavior · 2019Article
- Protein Structure Insights into the Bilayer Interactions of the Saposin-Like Domain of Solanum tuberosum Aspartic Protease.Scientific reports · 2017Article
- Rice stripe tenuivirus NSvc2 glycoproteins targeted to the golgi body by the N-terminal transmembrane domain and adjacent cytosolic 24 amino acids via the COP I- and COP II-dependent secretion pathway.Journal of virology · 2014Article
- Article
- Degradation of the endoplasmic reticulum by autophagy during endoplasmic reticulum stress in Arabidopsis.The Plant cell · 2012Article
- Reliable transient transformation of intact maize leaf cells for functional genomics and experimental study.Plant physiology · 2012Article
- Chlapsin, a chloroplastidial aspartic proteinase from the green algae Chlamydomonas reinhardtii.Planta · 2012Article
- A genome-wide RNAi screen identifies regulators of cholesterol-modified hedgehog secretion in Drosophila.PloS one · 2012Article
- Surface α-1,3-glucan facilitates fungal stealth infection by interfering with innate immunity in plants.PLoS pathogens · 2012Article
- Nodulin 41, a novel late nodulin of common bean with peptidase activity.BMC plant biology · 2011Article
- TNO1 is involved in salt tolerance and vacuolar trafficking in Arabidopsis.Plant physiology · 2011Article
- The rice alpha-amylase glycoprotein is targeted from the Golgi apparatus through the secretory pathway to the plastids.The Plant cell · 2009Article
- Ricin B chain targeted to the endoplasmic reticulum of tobacco protoplasts is degraded by a CDC48- and vacuole-independent mechanism.The Journal of biological chemistry · 2008Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein sorting to plant vacuoles is known to be dependent on a considerable variety of protein motifs recognized by a family of sorting receptors. This can involve either traffic from the endoplasmic reticulum (ER) through the Golgi apparatus or direct ER-to-vacuole transport. Barley aspartic protease (Phytepsin) was shown previously to reach the vacuole via trafficking through the Golgi apparatus. Here we show that Phytepsin normally exits the ER in a COPII-mediated manner, because the Phytepsin precursor accumulates in the ER upon specific inhibition of the formation of COPII vesicles in vivo. Phytepsin differs from its yeast and mammalian counterparts by the presence of a saposin-like plant-specific insert (PSI). Deletion of this domain comprising 104 amino acids causes efficient secretion of the truncated molecule (Phytepsin Delta PSI) without affecting the enzymatic activity of the enzyme. Interestingly, deletion of the PSI also changes the way in which Phytepsin exits the ER. Inhibition of COPII vesicle formation causes accumulation of the Phytepsin precursor in the ER but has no effect on the secretion of Phytepsin Delta PSI. This suggests either that vacuolar sorting commences at the ER export step and involves recruitment into COPII vesicles or that the PSI domain carries two signals, one for COPII-dependent export from the ER and one for vacuolar delivery from the Golgi. The relevance of these observations with respect to the bulk flow model of secretory protein synthesis is discussed.
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