High impact information on Rab18

• In addition, association with the LD surface was increased following stimulation of lipolysis and inhibited by a caveolin mutant suggesting that recruitment of Rab18 is regulated by the metabolic state of individual LDs [1].
• To gain insights into this specific localization, Rab18 was co-expressed with Cav3DGV, a truncation mutant of caveolin-3 shown to inhibit the catabolism and motility of lipid droplets [1].
• In both adipocytes and non-adipocyte cell lines Rab18 localized to a subset of LDs [1].
• Moreover, in 3T3-L1 adipocytes, stimulation of lipolysis increased the localization of Rab18 to LDs, an effect reversed by beta-adrenergic antagonists [1].
• Consistent with this observation, overexpression of Rab18 induced a decrease in the amounts of ADRP in LDs in HepG2 and BALB/c 3T3 cells [2].

Biological context of Rab18

• Here we report the genetic mapping of Rab17 and Rab18 on mouse chromosomes 1 and 18, respectively [3].
• Rab18 may be involved in membrane traffic events during biogenesis and/or recycling steps of secretory vesicle components [4].

Analytical, diagnostic and therapeutic context of Rab18

• In contrast, GFP-Rab18 localized to LDs and immunoelectron microscopy showed direct association with the monolayer surface [1].
• In the present study, we identified Rab18 as an LD component of HepG2 cells by proteomic analysis, and confirmed its localization by immunohistochemistry and western blotting [2].

References