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Biochem Biophys Res Commun. 2004 Sep 24;322(3):957-65.

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

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1
Department of Anatomy and Molecular Cell Biology, Nagoya University, Graduate School of Medicine, 65 Tsurumai, Showa, Nagoya 466-8550, Japan. noriko@med.nagoya-u.ac.jp

Abstract

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.

PMID:
15336557
DOI:
10.1016/j.bbrc.2004.08.010
[Indexed for MEDLINE]
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