A WD40 Repeat Protein, Arabidopsis Sec13 Homolog 1, May Play a Role in Vacuolar Trafficking by Controlling the Membrane Association of AtDRP2A
2006
Lee, M.H. (Pohang University of Science and Technology, Pohang, Republic of Korea) | Lee, S.H. (Pohang University of Science and Technology, Pohang, Republic of Korea) | Kim, H.R. (Pohang University of Science and Technology, Pohang, Republic of Korea) | Jin, J.B. (Pohang University of Science and Technology, Pohang, Republic of Korea) | Kim, D.H. (Pohang University of Science and Technology, Pohang, Republic of Korea) | Hwang, I.H. (Pohang University of Science and Technology, Pohang, Republic of Korea), E-mail: ihhwang@postech.ac.kr
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.
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