Journal
CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 65, Issue 21, Pages 3433-3445Publisher
SPRINGER BASEL AG
DOI: 10.1007/s00018-008-8227-7
Keywords
Membrane traffic; large ARF guanine nucleotide exchange factors (ARF-GEFs); Brefeldin A (BFA); ARF GTPases; ARF-GEF interactors
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In eukaryotic cells membrane compartments are connected through cargo-selective vesicle trafficking mediating the exchange of components between different organelles. This exchange is essential to maintain their structural integrity and specific composition. A fundamental regulatory step in vesicle formation is the activation of small ARF GTPases by exchanging their bound GDP for GTP, which is a prerequisite for ARF-mediated effector recruitment. Activation of ARFs is catalyzed by the characteristic SEC7 domain of guanine nucleotide exchange factors (ARF-GEFs), which are classified according to their additional protein domains.The only group of ARF-GEFs conserved in mammals, yeast and plants are the large ARF-GEFs. This review summarizes recent findings on the function of large ARF-GEFs, and the use of the inhibitor Brefeldin A as a potent tool in understanding membrane trafficking. Furthermore we highlight common themes and apparent differences in large ARF-GEF function between eukaryotic kingdoms.
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