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Open AccessArticle

ER-to-Golgi Transport in HeLa Cells Displays High Resilience to Ca2+ and Energy Stresses

1
Molecular Biology and Biochemistry, Gottfried Schatz Research Center, Medical University of Graz, Neue Stiftingtalstraße 6/6, 8010 Graz, Austria
2
Interfaculty Institute of Cell Biology, University of Tuebingen, Auf der Morgenstelle 15, 72076 Tuebingen, Germany
3
Department of Pharmacology, Toxicology and Clinical Pharmacy, Institute of Pharmacy, University of Tuebingen, Auf der Morgenstelle 8, 72076 Tuebingen, Germany
4
Division of Biological Sciences and Center for Structural and Functional Neuroscience, The University of Montana, 32 Campus Drive, HS 302A, Missoula, MT 59812-4824, USA
5
BioTechMed Graz, Mozartgasse 12/II, 8010 Graz, Austria
*
Author to whom correspondence should be addressed.
Cells 2020, 9(10), 2311; https://doi.org/10.3390/cells9102311
Received: 11 September 2020 / Revised: 9 October 2020 / Accepted: 16 October 2020 / Published: 17 October 2020
One third of all human proteins are either transmembrane or soluble secretory proteins that first target the endoplasmic reticulum (ER). These proteins subsequently leave the ER and enter the Golgi apparatus via ER-Golgi intermediate vesicular structures. Live-cell imaging of cargos fused to fluorescent proteins (FPs) enables the high-resolution visualization and characterization of secretory transport processes. Here, we performed fluorescence time-lapse imaging to assess the Ca2+ and energy dependency of ER-to-Golgi transport in living HeLa cells, a cancer cell model which has been well investigated. Our data revealed that ER-to-Golgi transport remained highly efficient in the absence of ATP-generating substrates, despite clear reductions in cytosolic and mitochondrial ATP levels under these energy stress conditions. However, cell treatment with 2-deoxy-D-glucose (2-DG), which severely diminished subcellular ATP levels, abolished ER-to-Golgi transport. Interestingly, while 2-DG elevated cytosolic Ca2+ levels and reduced long-distance movements of glycosylphosphatidylinositol (GPI)-positive vesicles, robust short-term ER Ca2+ mobilizations, which strongly affected the motility of these vesicles, did not considerably impair ER-to-Golgi transport. In summary, we highlight that ER-to-Golgi transport in HeLa cells remains functional despite high energy and Ca2+ stress levels. View Full-Text
Keywords: ER-to-Golgi transport; coat protein complex II (COPII) vesicles; vesicle trafficking; cancer cell metabolism; cellular calcium homeostasis; fluorescent protein technology; live-cell imaging; protein transport and sorting; secretory pathway; subcellular ATP imaging ER-to-Golgi transport; coat protein complex II (COPII) vesicles; vesicle trafficking; cancer cell metabolism; cellular calcium homeostasis; fluorescent protein technology; live-cell imaging; protein transport and sorting; secretory pathway; subcellular ATP imaging
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MDPI and ACS Style

Rauter, T.; Burgstaller, S.; Gottschalk, B.; Ramadani-Muja, J.; Bischof, H.; Hay, J.C.; Graier, W.F.; Malli, R. ER-to-Golgi Transport in HeLa Cells Displays High Resilience to Ca2+ and Energy Stresses. Cells 2020, 9, 2311.

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