| Literature DB >> 33401608 |
Susana Sabido-Bozo1,2, Ana Maria Perez-Linero1,2, Javier Manzano-Lopez1,3, Sofia Rodriguez-Gallardo1,2, Auxiliadora Aguilera-Romero1,2, Alejandro Cortes-Gomez1,2, Sergio Lopez1,2, Ralf Erik Wellinger3,4, Manuel Muñiz1,2.
Abstract
Golgi trafficking depends on the small GTPase Arf1 which, upon activation, drives the assembly of different coats onto budding vesicles. Two related types of guanine nucleotide exchange factors (GEFs) activate Arf1 at different Golgi sites. In yeast, Gea1 in the cis-Golgi and Gea2 in the medial-Golgi activate Arf1 to form COPI-coated vesicles for retrograde cargo sorting, whereas Sec7 generates clathrin/adaptor-coated vesicles at the trans-Golgi network (TGN) for forward cargo transport. A central question is how the same activated Arf1 protein manages to assemble different coats depending on the donor Golgi compartment. A previous study has postulated that the interaction between Gea1 and COPI would channel Arf1 activation for COPI vesicle budding. Here, we found that the p24 complex, a major COPI vesicle cargo, promotes the binding of Gea1 with COPI by increasing the COPI association to the membrane independently of Arf1 activation. Furthermore, the p24 complex also facilitates the interaction of Arf1 with its COPI effector. Therefore, our study supports a mechanism by which the p24 complex contributes to program Arf1 activation by Gea1 for selective COPI coat assembly at the cis-Golgi compartment.Entities:
Keywords: Arf1; ArfGEFs; COPI; Golgi; p24 complex
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Year: 2021 PMID: 33401608 PMCID: PMC7794930 DOI: 10.3390/ijms22010423
Source DB: PubMed Journal: Int J Mol Sci ISSN: 1422-0067 Impact factor: 5.923