Mutual regulation of plant phospholipase D and the actin cytoskeleton

0350391 - ÚEB 2011 RIV GB eng J - Journal Article
Pleskot, Roman - Potocký, Martin - Pejchar, Přemysl - Linek, J. - Bezvoda, R. - Martinec, Jan - Valentová, O. - Novotná, Z. - Žárský, Viktor
Mutual regulation of plant phospholipase D and the actin cytoskeleton.
Plant Journal. Roč. 62, č. 3 (2010), s. 494-507. ISSN 0960-7412. E-ISSN 1365-313X
R&D Projects: GA AV ČR IAA601110916; GA MŠMT(CZ) LC06034; GA ČR GA522/05/0340
Institutional research plan: CEZ:AV0Z50380511
Keywords : phospholipase D * actin * signaling
Subject RIV: ED - Physiology
Impact factor: 6.948, year: 2010

Membrane lipids and cytoskeleton dynamics are intimately inter-connected in the eukaryotic cell and phospholipase D (PLD) and its product phosphatidic acid (PA) were discovered to be important regulators in the membrane–cytoskeleton interface in eukaryotes. Here we report the mechanistic details of plant PLD–actin interactions. Inhibition of PLD by compromises, and PA rescues, pollen tube actin. We identified NtPLDb1 as a regulatory partner of actin, by both activity and in vitro interaction assays. The activity of tobacco PIP2-dependent PLD (PLDb) is specifically enhanced by F-actin and inhibited by G-actin. Using sequence- and structure-based analysis, together with site-directed mutagenesis, we identified Asn323 and Thr382 of NtPLDb1 as the crucial amino acids in the actin-interacting fold. The effect of antisense-mediated suppression of NtPLDb1 or NtPLDd on pollen tube F-actin dynamics shows that NtPLDb1 is the active partner in PLD–actin interplay.
Permanent Link: http://hdl.handle.net/11104/0190406