NDLI: The Intermolecular Interaction between the PH Domain and the C-terminal Domain of Arabidopsis Dynamin-like 6 Determines Lipid Binding Specificity

Content Provider	Journal of Biological Chemistry (JBC)
Author	Lee, Sung Hoon Jin, Jing Bo Song, Jinhee Min, Myung Ki Park, Dae Sup Kim, Yong-Woo Hwang, Inhwan
Abstract	Dynamin and its related proteins are a group of mechanochemical proteins involved in the modulation of lipid membranes in various biological processes. Here we investigate the nature of membrane binding of the Arabidopsis dynamin-like 6 (ADL6) involved in vesicle trafficking from the trans-Golgi network to the central vacuole. Fractionation experiments by continuous sucrose gradients and gel filtration revealed that the majority of ADL6 is associated with membranes in vivo. Amino acid sequence analysis revealed that ADL6 has a putative pleckstrin homology (PH) domain. In vitro lipid binding assays demonstrated that ADL6 showed high affinity binding to phosphatidylinositol 3-phosphate (PtdIns-3-P) and that the PH domain was responsible for this interaction. However, the PH domain alone binds equally well to both PtdIns-3-P and phosphatidylinositol 4-phosphate (PtdIns-4-P). Interestingly, the high affinity binding of the PH domain to PtdIns-3-P was restored by a protein-protein interaction between the PH domain and the C-terminal region. In addition, deletion of the inserted regions within the PH domain results in high affinity binding of the PH domain to PtdIns-3-P. These results suggest that ADL6 binds specifically to PtdIns-3-P and that the lipid binding specificity is determined by the interaction between the PH domain and the C-terminal domain of ADL6.
Related Links	http://www.jbc.org/content/277/35/31842.abstract
Ending Page	31849
Starting Page	31842
Page Count	8
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
Issue Number	35
Volume Number	277
DOI	10.1074/jbc.M204770200
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2002-08-30
Access Restriction	Open
Subject Keyword	Trans-Golgi network (TGN) Arabidopsisdynamin-like (ADL) Pleckstrin homology (PH) C-terminal domain (CTD) Maltose-binding protein (MBP) Phosphatidylcholine (PC) Phosphatidylethanolamine (PE) Phosphatidylinositol (PtdInd) Phospholipase C (PLC) GTPase effector domain (GED) MEMBRANE TRANSPORT STRUCTURE FUNCTION AND BIOGENESIS
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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