ArticlePlant physiology2003
C-terminal KDEL sequence of a KDEL-tailed cysteine proteinase (sulfhydryl-endopeptidase) is involved in formation of KDEL vesicle and in efficient vacuolar transport of sulfhydryl-endopeptidase.
Article in Plant physiology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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30 citing papers in PubMed, 61 citations in OpenAlex.
- A View into Seed Autophagy: From Development to Environmental Responses.Plants (Basel, Switzerland) · 2022Article
- Specialized endoplasmic reticulum-derived vesicles in plants: Functional diversity, evolution, and biotechnological exploitation.Journal of integrative plant biology · 2022Review
- A rich and bountiful harvest: Key discoveries in plant cell biology.The Plant cell · 2022Review
- An Apoplastic Defensin of Wheat Elicits the Production of Extracellular Polysaccharides in Snow Mold.Plants (Basel, Switzerland) · 2021Article
- Exploring Mechanisms of Quantitative Resistance toPlants (Basel, Switzerland) · 2020Article
- Barley cysteine protease PAP14 plays a role in degradation of chloroplast proteins.Journal of experimental botany · 2019Article
- Physiology and molecular biology of plants : an international journal of functional plant biology · 2019Article
- Article
- The role of KDEL-tailed cysteine endopeptidases of Arabidopsis (AtCEP2 and AtCEP1) in root development.PloS one · 2018Article
- Inhibitory properties of cysteine protease pro-peptides from barley confer resistance to spider mite feeding.PloS one · 2015Article
- Silencing of the CaCP gene delays salt- and osmotic-induced leaf senescence in Capsicum annuum L.International journal of molecular sciences · 2014Article
- Ex vivo processing for maturation of Arabidopsis KDEL-tailed cysteine endopeptidase 2 (AtCEP2) pro-enzyme and its storage in endoplasmic reticulum derived organelles.Plant molecular biology · 2014Article
- Endoplasmic reticulum KDEL-tailed cysteine endopeptidase 1 of Arabidopsis (AtCEP1) is involved in pathogen defense.Frontiers in plant science · 2014Article
- Involvement of autophagy in the direct ER to vacuole protein trafficking route in plants.Frontiers in plant science · 2014Review
- The dynamic behavior of storage organelles in developing cereal seeds and its impact on the production of recombinant proteins.Frontiers in plant science · 2014Review
- Trafficking of endoplasmic reticulum-retained recombinant proteins is unpredictable in Arabidopsis thaliana.Frontiers in plant science · 2014Review
- The Arabidopsis exocyst subcomplex subunits involved in a golgi-independent transport into the vacuole possess consensus autophagy-associated atg8 interacting motifs.Plant signaling & behavior · 2013Article
- Plant species and organ influence the structure and subcellular localization of recombinant glycoproteins.Plant molecular biology · 2013Article
- Classification of protein motifs based on subcellular localization uncovers evolutionary relationships at both sequence and functional levels.BMC bioinformatics · 2013Article
- Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sulfhydryl-endopeptidase (SH-EP) is a papain-type vacuolar proteinase expressed in cotyledons of germinated Vigna mungo seeds, and the enzyme possesses a C-terminal propeptide containing KDEL tail, an endoplasmic reticulum retention signal for soluble proteins. SH-EP is transported to vacuoles via a KDEL vesicle (KV) through a Golgi complex-independent route. To see the function of the KDEL sequence of SH-EP, wild-type SH-EP and its KDEL deletion mutant (SH-EPDeltaKDEL) were heterologously expressed in Arabidopsis and in cultured tobacco Bright Yellow 2 cells, and their intracellular transport pathways and localizations were analyzed. A combination of the results from analyses for transformed Arabidopsis and tobacco (Nicotiana tabacum) cells indicated that wild-type SH-EP is packed into KV-like vesicles through the KDEL sequence and is transported to vacuoles in the cells of transformants. In contrast, KV was not formed/induced in the cells expressing SH-EPDeltaKDEL, and the mutant protein was mainly secreted. Therefore, the C-terminal KDEL sequence of the KDEL-tailed cysteine proteinase is thought to be involved in the formation of KV, and in the efficient vacuolar transport of the proteins through KV.
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