Yeast Gdt1 is a Golgi-localized calcium transporter required for stress-induced calcium signaling and protein glycosylation
| Autor: | Didier Demaegd, Louise Thines, Antoine Deschamps, François Foulquier, Palanivelu Sengottaiyan, Anne-Sophie Colinet, Pascal Hols, Pierre Morsomme, Marie-Clémence Duchêne, Marie-Lise Colsoul |
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| Přispěvatelé: | UCL - SST/ISV - Institut des sciences de la vie |
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Glycosylation Saccharomyces cerevisiae Proteins Calcium pump Antiporter chemistry.chemical_element Gene Expression Saccharomyces cerevisiae Biology Calcium Article 03 medical and health sciences chemistry.chemical_compound Osmotic Pressure Calcium flux Calcium Signaling Calcium signaling Multidisciplinary 030102 biochemistry & molecular biology Voltage-dependent calcium channel Recombinant Proteins Cell biology Lactococcus lactis 030104 developmental biology Biochemistry chemistry Plasma membrane Ca2+ ATPase Calcium Channels |
| Zdroj: | Scientific Reports, Vol. 6, no.24282, p. 1-11 (2016) Scientific Reports |
| Popis: | Calcium signaling depends on a tightly regulated set of pumps, exchangers and channels that are responsible for controlling calcium fluxes between the different subcellular compartments of the eukaryotic cell. We have recently reported that two members of the highly-conserved UPF0016 family, human TMEM165 and budding yeast Gdt1p, are functionally related and might form a new group of Golgi-localized cation/Ca2+ exchangers. Defects in the human protein TMEM165 are known to cause a subtype of Congenital Disorders of Glycosylation. Using an assay based on the heterologous expression of GDT1 in the bacterium Lactococcus lactis, we demonstrated the calcium transport activity of Gdt1p. We observed a Ca2+ uptake activity in cells expressing GDT1, which was dependent on the external pH, indicating that Gdt1p may act as a Ca2+/H+ antiporter. In yeast, we found that Gdt1p controls cellular calcium stores and plays a major role in the calcium response induced by osmotic shock when the Golgi calcium pump, Pmr1p, is absent. Importantly, we also discovered that, in the presence of a high concentration of external calcium, Gdt1p is required for glycosylation of carboxypeptidase Y and the glucanosyltransferase Gas1p. Finally we showed that glycosylation process is restored by providing more Mn2+ to the cells. |
| Databáze: | OpenAIRE |
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