Constitutive activation of S1P receptors at the trans -Golgi network is required for surface transport carrier formation.
Autor: | Okada T; Division of Biochemistry, Department of Biochemistry and Molecular Biology, Kobe University Graduate School of Medicine, Kobe 650-0017, Japan., Nishida S; Division of Biochemistry, Department of Biochemistry and Molecular Biology, Kobe University Graduate School of Medicine, Kobe 650-0017, Japan., Zhang L; Division of Biochemistry, Department of Biochemistry and Molecular Biology, Kobe University Graduate School of Medicine, Kobe 650-0017, Japan., Ibrahim Mohamed NN; Division of Biochemistry, Department of Biochemistry and Molecular Biology, Kobe University Graduate School of Medicine, Kobe 650-0017, Japan.; Department of Agricultural Biochemistry, Faculty of Agriculture, Ain Shams University, Cairo, Egypt., Wang T; Division of Biochemistry, Department of Biochemistry and Molecular Biology, Kobe University Graduate School of Medicine, Kobe 650-0017, Japan., Ijuin T; Division of Biochemistry, Department of Biochemistry and Molecular Biology, Kobe University Graduate School of Medicine, Kobe 650-0017, Japan., Kajimoto T; Division of Biochemistry, Department of Biochemistry and Molecular Biology, Kobe University Graduate School of Medicine, Kobe 650-0017, Japan., Nakamura SI; Division of Biochemistry, Department of Biochemistry and Molecular Biology, Kobe University Graduate School of Medicine, Kobe 650-0017, Japan. |
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Jazyk: | angličtina |
Zdroj: | IScience [iScience] 2021 Oct 29; Vol. 24 (11), pp. 103351. Date of Electronic Publication: 2021 Oct 29 (Print Publication: 2021). |
DOI: | 10.1016/j.isci.2021.103351 |
Abstrakt: | The importance of the G-protein βγ subunits in the regulation of cargo transport from the trans -Golgi network (TGN) to the plasma membrane (PM) is well accepted; however, the molecular mechanism underlying the G-protein activation at the TGN remains unclear. We show here that sphingosine 1-phosphate (S1P) receptors at the PM were trafficked to the TGN in response to a surface transport cargo, temperature-sensitive vesicular stomatitis virus glycoprotein tagged with green fluorescent protein accumulation in the Golgi. The receptor internalization occurred in an S1P-independent manner but required phosphorylation by G-protein receptor kinase 2 and β-arrestin association before internalization. Continuously activated S1P receptors in a manner dependent on S1P at the TGN kept transmitting G-protein signals including the βγ subunits supply necessary for transport carrier formation at the TGN destined for the PM. Competing Interests: The authors declare no competing interests. (© 2021 The Author(s).) |
Databáze: | MEDLINE |
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