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The **Sec7 domain-containing guanine-nucleotide exchange factors** are a family of enzymes characterized by the presence of a Sec7 domain, which catalyzes the exchange of GDP for GTP on ADP-ribosylation factor (ARF) GTPases, primarily involved in regulating vesicular protein trafficking and membrane remodeling[1][2][4]. These proteins function as critical regulators in the secretory and endosomal pathways, especially at the Golgi apparatus and trans-Golgi network, where they facilitate the recruitment of coat proteins and clathrin adaptors for vesicle formation and transport[5][6]. The Sec7 domain is highly conserved and defines the catalytic core of these exchange factors, while other domains (such as pleckstrin homology domains) assist in membrane association and regulation[4]. Because their activity is essential for proper cellular trafficking, Sec7 domain-containing GEFs are considered therapeutic targets, particularly in diseases marked by altered vesicular transport, but their fundamental roles in cell physiology also present therapeutic and safety challenges[6].
Inhibition of guanine nucleotide exchange activity on ARF GTPases (typical action of BFA on sensitive Sec7-GEFs)
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