ArticlePlant physiology2013
Traffic of human α-mannosidase in plant cells suggests the presence of a new endoplasmic reticulum-to-vacuole pathway without involving the Golgi complex.
Article in Plant physiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 23 citations in OpenAlex.
- Unconventional Pathways of Protein Secretion: MammalsFrontiers in cell and developmental biology · 2022Review
- Article
- Vacuolar targeting of recombinant antibodies in Nicotiana benthamiana.Plant biotechnology journal · 2016Article
- Lysosomal and vacuolar sorting: not so different after all!Biochemical Society transactions · 2016Review
- Unconventional protein secretion in plants: a critical assessment.Protoplasma · 2016Review
- Molecular Composition of Plant Vacuoles: Important but Less Understood Regulations and Roles of Tonoplast Lipids.Plants (Basel, Switzerland) · 2015Review
- Production of the Main Celiac Disease Autoantigen by Transient Expression in Nicotiana benthamiana.Frontiers in plant science · 2015Article
- Delivering of proteins to the plant vacuole--an update.International journal of molecular sciences · 2014Review
- Plant vacuole morphology and vacuolar trafficking.Frontiers in plant science · 2014Review
- ER and vacuoles: never been closer.Frontiers in plant science · 2014Review
- Unconventional pathways of secretory plant proteins from the endoplasmic reticulum to the vacuole bypassing the Golgi complex.Plant signaling & behavior · 2013Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The transport of secretory proteins from the endoplasmic reticulum to the vacuole requires sorting signals as well as specific transport mechanisms. This work is focused on the transport in transgenic tobacco (Nicotiana tabacum) plants of a human α-mannosidase, MAN2B1, which is a lysosomal enzyme involved in the turnover of N-linked glycoproteins and can be used in enzyme replacement therapy. Although ubiquitously expressed, α-mannosidases are targeted to lysosomes or vacuoles through different mechanisms according to the organisms in which these proteins are produced. In tobacco cells, MAN2B1 reaches the vacuole even in the absence of mannose-6-phosphate receptors, which are responsible for its transport in animal cells. We report that MAN2B1 is targeted to the vacuole without passing through the Golgi complex. In addition, a vacuolar targeting signal that is recognized in plant cells is located in the MAN2B1 amino-terminal region. Indeed, when this amino-terminal domain is removed, the protein is retained in the endoplasmic reticulum. Moreover, when this domain is added to a plant-secreted protein, the resulting fusion protein is partially redirected to the vacuole. These results strongly suggest the existence in plants of a new type of vacuolar traffic that can be used by leaf cells to transport vacuolar proteins.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.