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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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ADRP is dissociated from lipid droplets by ARF1-dependent mechanism.

Adipocyte differentiation-related protein ( ADRP) is a member of PAT proteins existing in lipid droplets (LDs). By yeast two-hybrid screening, we identified ADP-ribosylation factor 1 ( ARF1) as a binding partner of ADRP. The interaction of ADRP and ARF1 was verified by GST pull-down and co-immunoprecipitation experiments. Interestingly, ADRP precipitated the GDP- bound ARF1 preferentially to the GTP-bound ARF1. Consistent with this, either brefeldin A (BFA), a fungal metabolite to inhibit ARF- GEF, or a dominant-negative mutant of ARF1 caused dissociation of ADRP from LD. On the other hand, overexpression of wild-type ARF1 did not promote the ADRP dissociation or new LD formation. By using deletion mutants, a central domain of ADRP, which is dispensable for LD binding, was shown to bind to ARF1. The present study showed that the GDP-bound ARF1 induces dissociation of ADRP from the LD surface, and that LD is a target of BFA action.[1]

References

  1. ADRP is dissociated from lipid droplets by ARF1-dependent mechanism. Nakamura, N., Akashi, T., Taneda, T., Kogo, H., Kikuchi, A., Fujimoto, T. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
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