Maintaining endoplasmic reticulum （ER） homeostasis is essential for the production of biomolecules. ER retrieval, i.e., the retrograde transport of compounds from the Golgi to the ER, is one of the pathways that ens...Maintaining endoplasmic reticulum （ER） homeostasis is essential for the production of biomolecules. ER retrieval, i.e., the retrograde transport of compounds from the Golgi to the ER, is one of the pathways that ensures ER homeostasis. However, the mechanisms underlying the regulation of ER retrieval in plants remain largely unknown. Plant ERD2-1ike proteins （ERD2s） were recently suggested to function as ER luminal protein receptors that mediate ER retrieval. Here, we demon- strate that heterotrimeric G protein signaling is involved in ERD2-mediated ER retrieval. We show that ERD2s interact with the heterotrimeric G protein Gα and Gγsubunits at the Golgi. Silencing of Gα, Gβ, or Gγ increased the retention of ER luminal proteins. Furthermore, overexpression of Gα, Gβ, or Gγ caused ER luminal proteins to escape from the ER, as did the co-silencing of ERD2a and ERD2b. These results suggest that G proteins interact with ER luminal protein receptors to regulate ER retrieval.展开更多
基金supported by the National Basic Research Program of China (2017YFA0503401)the National Natural Science Foundation of China (31530059, 3142100007, 31470254)the National Transgenic Program of China (2016ZX08009-003, 2016ZX08005-001 and 2016ZX08009001-004)
文摘Maintaining endoplasmic reticulum （ER） homeostasis is essential for the production of biomolecules. ER retrieval, i.e., the retrograde transport of compounds from the Golgi to the ER, is one of the pathways that ensures ER homeostasis. However, the mechanisms underlying the regulation of ER retrieval in plants remain largely unknown. Plant ERD2-1ike proteins （ERD2s） were recently suggested to function as ER luminal protein receptors that mediate ER retrieval. Here, we demon- strate that heterotrimeric G protein signaling is involved in ERD2-mediated ER retrieval. We show that ERD2s interact with the heterotrimeric G protein Gα and Gγsubunits at the Golgi. Silencing of Gα, Gβ, or Gγ increased the retention of ER luminal proteins. Furthermore, overexpression of Gα, Gβ, or Gγ caused ER luminal proteins to escape from the ER, as did the co-silencing of ERD2a and ERD2b. These results suggest that G proteins interact with ER luminal protein receptors to regulate ER retrieval.
