ArticleThe Plant cell1999
Saturation of the endoplasmic reticulum retention machinery reveals anterograde bulk flow
Article in The Plant cell, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
56 citing papers in PubMed, 115 citations in OpenAlex.
- StaufenC facilitates utilization of the ERAD pathway to transport dsRNA through the endoplasmic reticulum to the cytosol.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- VAMP724 and VAMP726 are involved in autophagosome formation inAutophagy · 2023Article
- Performance of plant-produced RBDs as SARS-CoV-2 diagnostic reagents: a tale of two plant platforms.Frontiers in plant science · 2023Article
- A Model for ERD2 Function in Higher Plants.Frontiers in plant science · 2020Review
- Plant Cell Wall Proteomics: A Focus on Monocot Species,International journal of molecular sciences · 2019Review
- Integrins and ERp57 Coordinate to Regulate Cell Surface Calreticulin in Immunogenic Cell Death.Frontiers in oncology · 2019Article
- Predominant Golgi Residency of the Plant K/HDEL Receptor Is Essential for Its Function in Mediating ER Retention.The Plant cell · 2018Article
- Salicylic acid-independent role of NPR1 is required for protection from proteotoxic stress in the plant endoplasmic reticulum.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- ATG9 regulates autophagosome progression from the endoplasmic reticulum in Arabidopsis.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Arabidopsis COG Complex Subunits COG3 and COG8 Modulate Golgi Morphology, Vesicle Trafficking Homeostasis and Are Essential for Pollen Tube Growth.PLoS genetics · 2016Article
- Vesicles versus Tubes: Is Endoplasmic Reticulum-Golgi Transport in Plants Fundamentally Different from Other Eukaryotes?Plant physiology · 2015Review
- The effect of the unfolded protein response on the production of recombinant proteins in plants.Plant cell reports · 2015Review
- Golgi-dependent transport of vacuolar sorting receptors is regulated by COPII, AP1, and AP4 protein complexes in tobacco.The Plant cell · 2014Article
- Endoplasmic reticulum chaperones and oxidoreductases: critical regulators of tumor cell survival and immunorecognition.Frontiers in oncology · 2014Review
- Silencing of Nicotiana benthamiana Neuroblastoma-Amplified Gene causes ER stress and cell death.BMC plant biology · 2013Article
- Is the 6 kDa tobacco etch viral protein a bona fide ERES marker?Journal of experimental botany · 2011Article
- Modulatory role of calreticulin as chaperokine for dendritic cell-based immunotherapy.Clinical and experimental immunology · 2011Article
- A missense mutation in the Arabidopsis COPII coat protein Sec24A induces the formation of clusters of the endoplasmic reticulum and Golgi apparatus.The Plant cell · 2009Article
- Viral and murine interleukin-10 are correctly processed and retain their biological activity when produced in tobacco.BMC biotechnology · 2009Article
- What is moving in the secretory pathway of plants?Plant physiology · 2008Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have studied the possible mechanisms of endoplasmic reticulum (ER) export and retention by using natural residents of the plant ER. Under normal physiological conditions, calreticulin and the lumenal binding protein (BiP) are efficiently retained in the ER. When the ER retention signal is removed, truncated calreticulin is much more rapidly secreted than truncated BiP. Calreticulin carries two glycans of the typical ER high-mannose form. Both glycans are competent for Golgi-based modifications, as determined from treatment with brefeldin A or based on the deletion of the ER retention motif. In contrast to BiP, calreticulin accumulation is strongly dependent on its retention signal, thereby allowing us to test whether saturation of the retention mechanism is possible. Overexpression of calreticulin led to 100-fold higher levels in dilated globular ER cisternae as well as dilated nuclear envelopes and partial secretion of both BiP and calreticulin. This result shows that both molecules are competent for ER export and supports the concept that proteins are secreted by default. This result also supports previous data suggesting that truncated BiP devoid of its retention motif can be retained in the ER by association with calreticulin. Moreover, even under these saturating conditions, cellular calreticulin did not carry significant amounts of complex glycans, in contrast to secreted calreticulin. This result shows that calreticulin is rapidly secreted once complex glycans have been synthesized in the medial/trans Golgi apparatus and that the modified protein does not appear to recycle back to the ER.
Identifiers
What OpenQuestion holds
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.