The Golgi apparatus comprises an enormous array of components that generate its unique architecture and function within cells. Here, we use quantitative fluorescence imaging techniques and ultrastructural analysis to address whether the Golgi apparatus is a steady-state or a stable organelle. We found that all classes of Golgi components are dynamically associated with this organelle, contrary to the prediction of the stable organelle model. Enzymes and recycling components are continuously exiting and reentering the Golgi apparatus by membrane trafficking pathways to and from the ER, whereas Golgi matrix proteins and coatomer undergo constant, rapid exchange between membrane and cytoplasm. When ER to Golgi transport is inhibited without disrupting COPII-dependent ER export machinery (by brefeldin A treatment or expression of Arf1[T31N]), the Golgi structure disassembles, leaving no residual Golgi membranes. Rather, all Golgi components redistribute into the ER, the cytoplasm, or to ER exit sites still active for recruitment of selective membrane-bound and peripherally associated cargos. A similar phenomenon is induced by the constitutively active Sar1[H79G] mutant, which has the additional effect of causing COPII-associated membranes to cluster to a juxtanuclear region. In cells expressing Sar1[T39N], a constitutively inactive form of Sar1 that completely disrupts ER exit sites, Golgi glycosylation enzymes, matrix, and itinerant proteins all redistribute to the ER. These results argue against the hypothesis that the Golgi apparatus contains stable components that can serve as a template for its biogenesis. Instead, they suggest that the Golgi complex is a dynamic, steady-state system, whose membranes can be nucleated and are maintained by the activities of the Sar1–COPII and Arf1–coatomer systems.
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12 November 2001
Article|
November 12 2001
Maintenance of Golgi structure and function depends on the integrity of ER export
Theresa H. Ward,
Theresa H. Ward
Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892
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Roman S. Polishchuk,
Roman S. Polishchuk
Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892
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Steve Caplan,
Steve Caplan
Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892
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Koret Hirschberg,
Koret Hirschberg
Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892
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Jennifer Lippincott-Schwartz
Jennifer Lippincott-Schwartz
Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892
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Theresa H. Ward
Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892
Roman S. Polishchuk
Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892
Steve Caplan
Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892
Koret Hirschberg
Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892
Jennifer Lippincott-Schwartz
Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892
Address correspondence to Dr. Jennifer Lippincott-Schwartz, CBMB, NICHD, NIH, Building 18T, Room 101, 18 Library Dr., Bethesda, MD 20892-5430. Tel.: (301) 402-1010. Fax: (301) 402-0078. E-mail: [email protected]
The online version of this article includes supplemental material.
*
Abbreviations used in this paper: BFA, brefeldin A; CFP, cyan fluorescent protein; FRAP, fluorescence recovery after photobleaching; GFP, green fluorescent protein; MTOC, microtubule organizing center; NRK, normal rat kidney; VTC, vesicular tubular clusters; YFP, yellow fluorescent protein.
Received:
July 11 2001
Revision Received:
October 10 2001
Accepted:
October 10 2001
Online ISSN: 1540-8140
Print ISSN: 0021-9525
The Rockefeller University Press
2001
J Cell Biol (2001) 155 (4): 557–570.
Article history
Received:
July 11 2001
Revision Received:
October 10 2001
Accepted:
October 10 2001
Citation
Theresa H. Ward, Roman S. Polishchuk, Steve Caplan, Koret Hirschberg, Jennifer Lippincott-Schwartz; Maintenance of Golgi structure and function depends on the integrity of ER export . J Cell Biol 12 November 2001; 155 (4): 557–570. doi: https://doi.org/10.1083/jcb.200107045
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