Arabidopsis dynamin-related protein 1A polymers bind, but do not tubulate, liposomes |
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Authors: | Steven K Backues |
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Institution: | Department of Biochemistry, University of Wisconsin - Madison, 433 Babcock Dr., Madison, WI 53706, USA |
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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. |
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Keywords: | AtDRP1A Arabidopsis dynamin-related protein 1A CME clathrin-mediated-endocytosis DOPC dioleoyl-phosphatidyl choline DOPE dioleoyl-phosphatidyl ethanolamine DOPG dioleoyl-phosphatidyl glycerol DOPS dioleoyl-phosphatidyl serine EM negative staining electron microscopy MBP maltose binding protein PM plasma membrane PMM plasma membrane mimetic PH pleckstrin homology PIP phosphatidyl inositol phosphate PRD proline rich domain Soy PC soybean phosphatidyl choline TEV Tobacco-Etch-virus protease |
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