An S-Acylation Switch of Conserved G Domain Cysteines Is Required for Polarity Signaling by ROP GTPases

Abstract

(Current Biology 20, 914–920; May 25, 2010) The authors recently noticed an error that occurred during the preparation of Figure S2E of this paper. Because of this unintentional error, some of the bands shown on the Ponceau S loading controls have been duplicated. To resolve possible concerns, we are providing a revised Figure S2 in which panel E has been changed. The revised panel E displays the full gels of protein immunoblots decorated with anti-ROP6 (α-ROP6) polyclonal antibodies and their Ponceau S-stained loading controls. The immunoblots are of protein extracts prepared from transgenic Arabidopsis lines expressing one of the following recombinant proteins: His6-GFP-ROP6 (6WT), His6GFP-rop6CA (6CA), His6-GFP-rop6CA21mS (21), His6-GFP-rop6CA156mS (156), or His6-GFP-rop6CA21+156mSS (21+156). For each of the recombinant proteins, the protein extracts have been prepared from three independent transgenic lines. This has now been corrected in the Supplemental Information available online. The authors regret this error. An S-Acylation Switch of Conserved G Domain Cysteines Is Required for Polarity Signaling by ROP GTPasesSorek et al.Current BiologyMay 6, 2010In BriefRho GTPases are master regulators of cell polarity [1]. For their function, Rhos must associate with discrete plasma membrane domains [2]. Rho of Plants (ROPs) or RACs comprise a single family [3–5]. Prenylation and S-acylation of hypervariable domain cysteines of Ras and Rho GTPases are required for their function [6–11]; however, lipid modifications in the G domain have never been reported. Reversible S-acylation involves the attachment of palmitate (C16:0) or other saturated lipids to cysteines through a thioester linkage and was implicated in the regulation of signaling [12]. Full-Text PDF Open Archive