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Biochem Biophys Res Commun. 2010 Mar 19;393(4):734-9. doi: 10.1016/j.bbrc.2010.02.070. Epub 2010 Feb 18.

Arabidopsis dynamin-related protein 1A polymers bind, but do not tubulate, liposomes.

Author information

1
Department of Biochemistry, University of Wisconsin - Madison, 433 Babcock Dr., Madison, WI 53706, USA.

Abstract

The Arabidopsis dynamin-related protein 1A (AtDRP1A) is involved in endocytosis and cell plate maturation in Arabidopsis. Unlike dynamin, AtDRP1A does not have any recognized membrane binding or protein-protein interaction domains. We report that GTPase active AtDRP1A purified from Escherichia coli as a fusion to maltose binding protein forms homopolymers visible by negative staining electron microscopy. These polymers interact with protein-free liposomes whose lipid composition mimics that of the inner leaflet of the Arabidopsis plasma membrane, suggesting that lipid-binding may play a role in AtDRP1A function. However, AtDRP1A polymers do not appear to assemble and disassemble in a dynamic fashion and do not have the ability to tubulate liposomes in vitro, suggesting that additional factors or modifications are necessary for AtDRP1A's in vivo function.

PMID:
20171176
PMCID:
PMC2874938
DOI:
10.1016/j.bbrc.2010.02.070
[Indexed for MEDLINE]
Free PMC Article

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