Author: José L. Martínez; Francesca Arnoldi; Elisabeth M. Schraner; Catherine Eichwald; Daniela Silva-Ayala; Eunjoo Lee; Elizabeth Sztul; Óscar R. Burrone; Susana López; Carlos F. Arias
Title: The guanine nucleotide exchange factor GBF1 participates in rotavirus replication Document date: 2019_4_29
ID: jkjkkjrf_2
Snippet: Arf1GAP complex stimulates the binding and concentration of different cargoes located in 105 the membrane, association that induces the bending of the membrane into a vesicle. Once 106 completed, the vesicle buds from the membrane covered by the COPI complex proteins. 107 Finally, the coat proteins are disassembled when the GTPase activity of Arf1 is enhanced by 108 Arf1GAP, leading to the hydrolysis of the GTP bound to Arf1. This hydrolysis lead.....
Document: Arf1GAP complex stimulates the binding and concentration of different cargoes located in 105 the membrane, association that induces the bending of the membrane into a vesicle. Once 106 completed, the vesicle buds from the membrane covered by the COPI complex proteins. 107 Finally, the coat proteins are disassembled when the GTPase activity of Arf1 is enhanced by 108 Arf1GAP, leading to the hydrolysis of the GTP bound to Arf1. This hydrolysis leads to the 109 release from the membrane of Arf1, COPI, and Arf1GAP (34, 35). 110 GBF1 belongs to a subfamily of large guanine nucleotide exchange factors (GEFs) that also 111 includes the mammalian BIG1, and BIG2 located at the trans-Golgi network (TGN) (36).
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