Arabidopsis Rab-E GTPases exhibit a novel interaction with a plasma-membrane phosphatidylinositol-4-phosphate 5-kinase

Luísa Camacho; Andrei P Smertenko; José Pérez-Gómez; Patrick J Hussey; Ian Moore

doi:10.1242/jcs.053488

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Arabidopsis Rab-E GTPases exhibit a novel interaction with a plasma-membrane phosphatidylinositol-4-phosphate 5-kinase

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Arabidopsis Rab-E GTPases exhibit a novel interaction with a plasma-membrane phosphatidylinositol-4-phosphate 5-kinase

Luísa Camacho, Andrei P Smertenko, José Pérez-Gómez, Patrick J Hussey and Ian Moore

Journal of cell science, Vol.122(Pt 23), pp.4383-4392

12/01/2009

DOI: https://doi.org/10.1242/jcs.053488

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https://hdl.handle.net/2376/109529

PMID: 19903693

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Abstract

rab GTP-Binding Proteins - metabolism

Arabidopsis Proteins - genetics

Protein Binding - genetics

Plants, Genetically Modified - genetics

Tobacco - metabolism

Phosphotransferases (Alcohol Group Acceptor) - genetics

rab GTP-Binding Proteins - genetics

Phosphotransferases (Alcohol Group Acceptor) - metabolism

Arabidopsis Proteins - metabolism

Cell Membrane - enzymology

Point Mutation

Two-Hybrid System Techniques

Plants, Genetically Modified - metabolism

Plant Leaves - genetics

Plant Leaves - metabolism

Tobacco - genetics

Cell Membrane - metabolism

Protein Binding - physiology

Rab GTPases of the Arabidopsis Rab-E subclass are related to mammalian Rab8 and are implicated in membrane trafficking from the Golgi to the plasma membrane. Using a yeast two-hybrid assay, Arabidopsis phosphatidylinositol-4-phosphate 5-kinase 2 (PtdIns(4)P 5-kinase 2; also known as PIP5K2), was shown to interact with all five members of the Rab-E subclass but not with other Rab subclasses residing at the Golgi or trans-Golgi network. Interactions in yeast and in vitro were strongest with RAB-E1d[Q74L] and weakest with the RAB-E1d[S29N] suggesting that PIP5K2 interacts with the GTP-bound form. PIP5K2 exhibited kinase activity towards phosphatidylinositol phosphates with a free 5-hydroxyl group, consistent with PtdIns(4)P 5-kinase activity and this activity was stimulated by Rab binding. Rab-E proteins interacted with PIP5K2 via its membrane occupancy and recognition nexus (MORN) domain which is missing from animal and fungal PtdIns(4)P 5-kinases. In plant cells, GFP:PIP5K2 accumulated at the plasma membrane and caused YFP:RAB-E1d to relocate there from its usual position at the Golgi. GFP:PIP5K2 was rapidly turned over by proteasomal activity in planta, and overexpression of YFP:PIP5K2 caused pleiotropic growth abnormalities in transgenic Arabidopsis. We propose that plant cells exhibit a novel interaction in which PIP5K2 binds GTP-bound Rab-E proteins, which may stimulate temporally or spatially localized PtdIns(4,5)P(2) production at the plasma membrane.

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Title: Arabidopsis Rab-E GTPases exhibit a novel interaction with a plasma-membrane phosphatidylinositol-4-phosphate 5-kinase
Creators: Luísa Camacho - Department of Plant Sciences, University of Oxford, Oxford OX1 3RB, UK
Andrei P Smertenko
José Pérez-Gómez
Patrick J Hussey
Ian Moore
Publication Details: Journal of cell science, Vol.122(Pt 23), pp.4383-4392
Academic Unit: Biological Chemistry, Institute of
Publisher: England
Grant note: BBS/B/09562 / Biotechnology and Biological Sciences Research Council REI20537 / Biotechnology and Biological Sciences Research Council
Identifiers: 99900547486801842
Language: English
Resource Type: Journal article