p24-Tango1 interactions ensure ER-Golgi interface stability and efficient transport.
| Autor: | Yang K; School of Life Sciences, Tsinghua University , Beijing, China., Feng Z; School of Life Sciences, Tsinghua University , Beijing, China., Pastor-Pareja JC; School of Life Sciences, Tsinghua University , Beijing, China.; Tsinghua-Peking Center for Life Sciences , Beijing, China.; Institute of Neurosciences, Consejo Superior de Investigaciones Científicas-Universidad Miguel Hernández , San Juan de Alicante, Spain. |
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| Jazyk: | angličtina |
| Zdroj: | The Journal of cell biology [J Cell Biol] 2024 May 06; Vol. 223 (5). Date of Electronic Publication: 2024 Mar 12. |
| DOI: | 10.1083/jcb.202309045 |
| Abstrakt: | The eukaryotic p24 family, consisting of α-, β-, γ- and δ-p24 subfamilies, has long been known to be involved in regulating secretion. Despite increasing interest in these proteins, fundamental questions remain about their role. Here, we systematically investigated Drosophila p24 proteins. We discovered that members of all four p24 subfamilies are required for general secretion and that their localizations between ER exit site (ERES) and Golgi are interdependent in an α→βδ→γ sequence. We also found that localization of p24 proteins and ERES determinant Tango1 requires interaction through their respective GOLD and SH3 lumenal domains, with Tango1 loss sending p24 proteins to the plasma membrane and vice versa. Finally, we show that p24 loss expands the COPII zone at ERES and increases the number of ER-Golgi vesicles, supporting a restrictive role of p24 proteins on vesicle budding for efficient transport. Our results reveal Tango1-p24 interplay as central to the generation of a stable ER-Golgi interface. (© 2024 Yang et al.) |
| Databáze: | MEDLINE |
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