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THE PLANT CELL, Vol 4, Issue 8 941-951, Copyright © 1992 by American Society of Plant Biologists
Association of Phosphatidylinositol 4-Kinase with the Plant Cytoskeleton
P. Xu, C. W. Lloyd, C. J. Staiger and B. K. Drobak
Department of Cell Biology, John Innes Centre for Plant Science Research, Colney Lane, Norwich NR4 7UH, United Kingdom
In eukaryotic cells, phosphatidylinositol 4-hydroxy kinase and
phosphatidylinositol-4-phosphate 5-hydroxy kinase are responsible for the
formation of the two second messenger precursors
phosphatidylinositol-4-phosphate (Ptdlns(4)P) and
phosphatidylinositol-4,5-bisphosphate (Ptdlns(4,5)P2). In plant cells,
these kinases have been considered to be exclusively membrane associated,
with the majority of activity residing in the inner leaflet of the
plasmalemma. By sequentially extracting carrot protoplasts with the
detergent Nonidet P-40 then more rigorously with Triton X-100, we were able
to remove the activity of three separate plasma membrane marker enzymes and
to demonstrate that a significant proportion of cellular Ptdlns 4-kinase is
associated with the cytoskeleton. When only endogenous substrates were
present, Nonidet P-40-permeabilized protoplasts and Nonidet P-40-extracted
cytoskeletons displayed a pattern of lipid phosphorylation similar to that
obtained with isolated plant membranes or permeabilized cells, whereas the
Triton X-100-extracted cytoskeletons showed little or no activity. In
contrast, when exogenous substrates were added, a major proportion of
PtdlnsP formed was due to kinase activity associated with the cytoskeleton
as well as nuclei. However, by subtracting the activity of isolated nuclei,
it could be demonstrated that a significant proportion of the
detergent-resistant Ptdlns kinase activity resides with the cytoskeletal
fraction. These findings suggest that the pathways of polyphosphoinositide
biosynthesis in plant cells should be reevaluated to take account of the
cytoskeleton and that Ptdlns(4)P itself may play a unique role in
modulation of plant cytoskeletal integrity and cellular signal
transduction.
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