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pubmed-article:20171176pubmed:abstractTextThe 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.lld:pubmed
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pubmed-article:20171176pubmed:copyrightInfoCopyright 2010 Elsevier Inc. All rights reserved.lld:pubmed
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pubmed-article:20171176pubmed:articleTitleArabidopsis dynamin-related protein 1A polymers bind, but do not tubulate, liposomes.lld:pubmed
pubmed-article:20171176pubmed:affiliationDepartment of Biochemistry, University of Wisconsin - Madison, 433 Babcock Dr., Madison, WI 53706, USA.lld:pubmed
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pubmed-article:20171176pubmed:publicationTypeResearch Support, U.S. Gov't, Non-P.H.S.lld:pubmed
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