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Sci. Signal., 8 September 2009
Vol. 2, Issue 87, p. ra52
A key regulator of cell motility is the negatively charged lipid phosphatidic acid (PA), which can be generated from the membrane lipid phosphatidylcholine by phospholipase D (PLD). The mechanisms by which PA and PLD regulate cell migration are not well understood. Focusing on the cytosolic tyrosine kinase Fer, which promotes actin polymerization, Itoh et al. identified a PA-binding domain in Fer that they termed the FX domain. PA binding to Fer enhanced its kinase activity and required positively charged residues in the FX domain. Forced expression of Fer increased lamellipodia formation and migration compared to cells expressing a Fer mutant lacking the positively charged residues in the FX domain; these effects were dependent on PLD activity. Thus, Fer may link changes in membrane composition to actin remodeling events that drive cell migration.
Citation: T. Itoh, J. Hasegawa, K. Tsujita, Y. Kanaho, T. Takenawa, The Tyrosine Kinase Fer Is a Downstream Target of the PLD-PA Pathway that Regulates Cell Migration. Sci. Signal.2, ra52 (2009).
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[DOI: 10.1126/stke.4002007eg8] |Abstract »|Full Text »|PDF »
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