ArticleMolecular biology of the cell2006
The Golgi apparatus maintains its organization independent of the endoplasmic reticulum.
Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Gβγ signaling regulates microtubule-dependent control of Golgi integrity.Cellular signalling · 2023Article
- Structural Organization and Function of the Golgi Ribbon During Cell Division.Frontiers in cell and developmental biology · 2022Article
- The function of GORASPs in Golgi apparatus organization in vivo.The Journal of cell biology · 2020Article
- A New Look at the Functional Organization of the Golgi Ribbon.Frontiers in cell and developmental biology · 2019Article
- Golgi enzymes do not cycle through the endoplasmic reticulum during protein secretion or mitosis.Molecular biology of the cell · 2017Article
- ER trapping reveals Golgi enzymes continually revisit the ER through a recycling pathway that controls Golgi organization.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- SLY1 and Syntaxin 18 specify a distinct pathway for procollagen VII export from the endoplasmic reticulum.eLife · 2014Article
- Golgi's way: a long path toward the new paradigm of the intra-Golgi transport.Histochemistry and cell biology · 2013Review
- Irradiation-induced protein inactivation reveals Golgi enzyme cycling to cell periphery.Journal of cell science · 2012Article
- Journeys through the Golgi--taking stock in a new era.The Journal of cell biology · 2009Review
- Membrane traffic within the Golgi apparatus.Annual review of cell and developmental biology · 2009Review
- Coat-tether interaction in Golgi organization.Molecular biology of the cell · 2008Article
- Analysis of de novo Golgi complex formation after enzyme-based inactivation.Molecular biology of the cell · 2007Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Under artificial conditions Golgi enzymes have the capacity to rapidly accumulate in the endoplasmic reticulum (ER). These observations prompted the idea that Golgi enzymes constitutively recycle through the ER. We have tested this hypothesis under physiological conditions through use of a procedure that captures Golgi enzymes in the ER. In the presence of rapamycin, which induces a tight association between FKBP (FK506-binding protein) and FRAP (FKBP-rapamycin-associated protein), an FKBP-tagged Golgi enzyme can be trapped when it visits the ER by an ER-retained protein fused to FRAP. We find that although FKBP-ERGIC-53 of the ER-Golgi intermediate compartment (ERGIC) rapidly cycles through the ER (30 min), FKBP-Golgi enzyme chimeras remain stably associated with Golgi membranes. We also demonstrate that Golgi dispersion upon nocodazole treatment mainly occurs through a mechanism that does not involve the recycling of Golgi membranes through the ER. Our findings suggest that the Golgi apparatus, as defined by its collection of resident enzymes, exists independent of the ER.
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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.