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Eur J Cell Biol. 2006 Sep;85(9-10):991-1000. Epub 2006 Jun 5.

Vacuolin, a flotillin/reggie-related protein from Dictyostelium oligomerizes for endosome association.

Author information

1
Laboratory for Molecular Cell Biology, University College London, London, UK.

Abstract

We have analysed the domain structure of vacuolin, a Dictyostelium protein binding to the cytoplasmic surface of late endosomes. Localisation studies using GFP fusions together with a yeast two-hybrid analysis and co-immunoprecipitation experiments reveal that a region close to the C-terminus mediates oligomer formation of the protein through a coiled-coil mechanism which in turn is a prerequisite for the efficient binding to endosomal membranes via a prohibitin (PHB) domain in the middle of the molecule. Overexpression of the coiled-coil domain strongly competes with endogenous vacuolin in the oligomers and reduces the efficiency of membrane targeting. The domain arrangement of vacuolin is most similar to flotillin/reggie, a protein found on late endosomes of mammalian cells.

PMID:
16750281
DOI:
10.1016/j.ejcb.2006.04.010
[Indexed for MEDLINE]

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