PLD (phospholipase D) activity catalyses the generation of the lipid messenger phosphatidic acid, which has been implicated in a number of cellular processes, particularly the regulation of membrane traffic. In the present study, we report that disruption of PLD signalling causes unexpectedly profound effects on the actin-based motility of Dictyostelium. Cells in which PLD activity is inhibited by butan-1-ol show a complete loss of actin-based structures, accompanied by relocalization of F-actin into small clusters, and eventually the nucleus, without a visible fall in levels of F-actin. Addition of exogenous phosphatidic acid reverses the effects of butan-1-ol, confirming that these effects are caused by inhibition of PLD. Loss of motility correlates with complete inhibition of endocytosis and a reduction in phagocytosis. Inhibition of PLD caused a major decrease in the synthesis of PtdIns(4,5)P2, which could again be reversed by exogenously applied phosphatidic acid. Thus the essential role of PLD signalling in both motility and endocytosis appears to be mediated directly via regulation of PtdIns(4)P kinase activity. This implies that localized PLD-regulated synthesis of PtdIns(4,5)P2 is essential for Dictyostelium actin function.
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Research Article|
June 21 2005
Phospholipase D activity is essential for actin localization and actin-based motility in Dictyostelium
Soha ZOUWAIL;
Soha ZOUWAIL
*School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K.
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Trevor R. PETTITT;
Trevor R. PETTITT
†Cancer Research UK Institute for Cancer Studies, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K.
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Stephen K. DOVE;
Stephen K. DOVE
*School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K.
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Margarita V. CHIBALINA;
Margarita V. CHIBALINA
1
*School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K.
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Dale J. POWNER;
Dale J. POWNER
†Cancer Research UK Institute for Cancer Studies, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K.
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Lee HAYNES;
Lee HAYNES
2
†Cancer Research UK Institute for Cancer Studies, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K.
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Michael J. O. WAKELAM;
Michael J. O. WAKELAM
†Cancer Research UK Institute for Cancer Studies, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K.
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Robert H. INSALL
Robert H. INSALL
3
*School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K.
3To whom correspondence should be addressed (email R.H.Insall@bham.ac.uk).
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Publisher: Portland Press Ltd
Received:
January 12 2005
Revision Received:
March 14 2005
Accepted:
March 15 2005
Accepted Manuscript online:
March 15 2005
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London
2005
Biochem J (2005) 389 (1): 207–214.
Article history
Received:
January 12 2005
Revision Received:
March 14 2005
Accepted:
March 15 2005
Accepted Manuscript online:
March 15 2005
Citation
Soha ZOUWAIL, Trevor R. PETTITT, Stephen K. DOVE, Margarita V. CHIBALINA, Dale J. POWNER, Lee HAYNES, Michael J. O. WAKELAM, Robert H. INSALL; Phospholipase D activity is essential for actin localization and actin-based motility in Dictyostelium. Biochem J 1 July 2005; 389 (1): 207–214. doi: https://doi.org/10.1042/BJ20050085
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