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KMID : 0578320060220020210
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Molecules and Cells
2006 Volume.22 No. 2 p.210 ~ p.219
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A WD40 Repeat Protein, Arabidopsis Sec13 Homolog 1, May Play a Role in Vacuolar Trafficking by Controlling the Membrane Association of AtDRP2A
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Lee Myoung-Hui
Lee Sung-Hoon
Kim Hey-Ran
Jin Jing-Bo
Kim Dae-Hyeon
Hwang Inhwan
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Abstract
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Dynamin-related protein 2A (AtDRP2A, formally ADL6), a member of the dynamin family, is critical for protein trafficking from the TGN to the central vacuole. However, the mechanism controlling its activity is not well understood in plant cells. We isolated Arabidopsis sec13 homolog1 (AtSeh1) that interacts with AtDRP2A by a yeast two-hybrid screening. AtSeh1 has four WD40 motifs and amino acid sequence homology to Sec13, a component of COPII vesicles. Coimmunoprecipitation and protein pull-down experiments demonstrated specific interaction between AtSeh1 and AtDRP2A. AtSeh1 bound to the pleckstrin homology domain of AtDRP2A in competition with the C-terminal domain of the latter, and this resulted in inhibition of the interaction between AtDRP2A and PtdIns3P in vitro. AtSeh1 localized to multiple locations: the nucleus, the prevacuolar compartment and the Golgi complex. Based on these results we propose that AtSeh1 plays a role in regulating cycling of AtDRP2A between membrane-bound and soluble forms.
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KEYWORD
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Arabidopsis Sec13 Homolog, Dynamin-related Protein 2A, Phospholipid Binding, Protein-Protein Interaction
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