Guanine nucleotide-exchange factors for arf GTPases: their diverse functions in membrane traffic.
Small GTPases of the Arf family, by cycling between GDP-bound inactive and GTP-bound active states, play a crucial role not only in the regulation of membrane traffic and dynamics but also in rearrangement of actin cytoskeleton. The exchange of GDP for GTP on Arf is catalyzed by a family of guanine nucleotide-exchange factors (GEFs) containing a Sec7 domain. The Sec7 domain is a target of brefeldin A, which inhibits various trafficking processes and induces organelle disintegration. During the past few years, significant progress has been made in elucidating the structure and catalytic mechanism of the Sec7 domains and physiological functions of the Sec7 domain-containing Arf-GEFs. Here we review the structures and functions of Arf-GEFs by focusing on the regulation of membrane traffic.
Shin
Hye-Won
HW
Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan. kazunaka@pharm.kyoto-u.ac.jp
Nakayama
Kazuhisa
K
D020727:ADP-Ribosylation Factors / Q000502:physiology*; D000818:Animals; D001692:Biological Transport; D002462:Cell Membrane / Q000502:physiology*; D020558:GTP Phosphohydrolases / Q000502:physiology*; D020662:Guanine Nucleotide Exchange Factors / Q000502:physiology*; D006801:Humans
D020662:Guanine Nucleotide Exchange Factors; D020558:GTP Phosphohydrolases; D020727:ADP-Ribosylation Factors