Publication: DYRK3 enables secretory trafficking by maintaining the liquid-like state of ER exit sites
DYRK3 enables secretory trafficking by maintaining the liquid-like state of ER exit sites
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Gallo, R., Rai, A. K., McIntyre, A. B. R., Meyer, K., & Pelkmans, L. (2023). DYRK3 enables secretory trafficking by maintaining the liquid-like state of ER exit sites. Developmental Cell, 58, 1880-1897.e11. https://doi.org/10.1016/j.devcel.2023.08.005
Abstract
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Abstract
The dual-specificity kinase DYRK3 controls the formation and dissolution of multiple biomolecular condensates, regulating processes including stress recovery and mitotic progression. Here, we report that DYRK3 functionally interacts with proteins associated with endoplasmic reticulum (ER) exit sites (ERESs) and that inhibition of DYRK3 perturbs the organization of the ERES-Golgi interface and secretory trafficking. DYRK3-mediated regulation of ERES depends on the N-terminal intrinsically disordered region (IDR) of the peripheral membr
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- Gallo, Raffaella
- Rai, Arpan Kumar
- McIntyre, Alexa B R
- Meyer, Katrina
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Gallo, R., Rai, A. K., McIntyre, A. B. R., Meyer, K., & Pelkmans, L. (2023). DYRK3 enables secretory trafficking by maintaining the liquid-like state of ER exit sites. Developmental Cell, 58, 1880-1897.e11. https://doi.org/10.1016/j.devcel.2023.08.005