ArticlePlant physiology2007
De novo formation of plant endoplasmic reticulum export sites is membrane cargo induced and signal mediated.
Article in Plant physiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
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Who cites it
34 citing papers in PubMed, 84 citations in OpenAlex.
- ER-associated VAP27-1 and VAP27-3 proteins functionally link the lipid-binding ORP2A at the ER-chloroplast contact sites.Nature communications · 2024Article
- A rich and bountiful harvest: Key discoveries in plant cell biology.The Plant cell · 2022Review
- The plant endoplasmic reticulum: an organized chaos of tubules and sheets with multiple functions.Journal of microscopy · 2020Review
- Dynamic Capture and Release of Endoplasmic Reticulum Exit Sites by Golgi Stacks in Arabidopsis.iScience · 2020Article
- 3D electron tomographic and biochemical analysis of ER, Golgi andJournal of biological research (Thessalonike, Greece) · 2018Article
- Effect of the unfolded protein response on ER protein export: a potential new mechanism to relieve ER stress.Cell stress & chaperones · 2018Article
- Transport from the endoplasmic reticulum to the Golgi in plants: Where are we now?Seminars in cell & developmental biology · 2018Review
- The Arabidopsis COPII components, AtSEC23A and AtSEC23D, are essential for pollen wall development and exine patterning.Journal of experimental botany · 2018Article
- The plant membrane surrounding powdery mildew haustoria shares properties with the endoplasmic reticulum membrane.Journal of experimental botany · 2017Article
- Organelle biogenesis in the endoplasmic reticulum.Nature cell biology · 2017Review
- GOLGI TRANSPORT 1B Regulates Protein Export from the Endoplasmic Reticulum in Rice Endosperm Cells.The Plant cell · 2016Article
- Secretory COPII Protein SEC31B Is Required for Pollen Wall Development.Plant physiology · 2016Article
- Vesicles versus Tubes: Is Endoplasmic Reticulum-Golgi Transport in Plants Fundamentally Different from Other Eukaryotes?Plant physiology · 2015Review
- ER network homeostasis is critical for plant endosome streaming and endocytosis.Cell discovery · 2015Article
- 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
- MAIGO5 functions in protein export from Golgi-associated endoplasmic reticulum exit sites in Arabidopsis.The Plant cell · 2013Article
- ARF1 and SAR1 GTPases in endomembrane trafficking in plants.International journal of molecular sciences · 2013Review
- The cytosolic nucleoprotein of the plant-infecting bunyavirus tomato spotted wilt recruits endoplasmic reticulum-resident proteins to endoplasmic reticulum export sites.The Plant cell · 2013Article
- Article
- Organization of the ER-Golgi interface for membrane traffic control.Nature reviews. Molecular cell biology · 2013Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The plant endoplasmic reticulum (ER) contains functionally distinct subdomains at which cargo molecules are packed into transport carriers. To study these ER export sites (ERES), we used tobacco (Nicotiana tabacum) leaf epidermis as a model system and tested whether increased cargo dosage leads to their de novo formation. We have followed the subcellular distribution of the known ERES marker based on a yellow fluorescent protein (YFP) fusion of the Sec24 COPII coat component (YFP-Sec24), which, differently from the previously described ERES marker, tobacco Sar1-YFP, is visibly recruited at ERES in both the presence and absence of overexpressed membrane cargo. This allowed us to quantify variation in the ERES number and in the recruitment of Sec24 to ERES upon expression of cargo. We show that increased synthesis of membrane cargo leads to an increase in the number of ERES and induces the recruitment of Sec24 to these ER subdomains. Soluble proteins that are passively secreted were found to leave the ER with no apparent up-regulation of either the ERES number or the COPII marker, showing that bulk flow transport has spare capacity in vivo. However, de novo ERES formation, as well as increased recruitment of Sec24 to ERES, was found to be dependent on the presence of the diacidic ER export motif in the cytosolic domain of the membrane cargo. Our data suggest that the plant ER can adapt to a sudden increase in membrane cargo-stimulated secretory activity by signal-mediated recruitment of COPII machinery onto existing ERES, accompanied by de novo generation of new ERES.
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Registered trials
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.