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Molecular and Cellular Biology
Sorek, N., School of Plant Sciences and Food Security, Tel Aviv University, Ramat Aviv, Tel Aviv, Israel, Beilinson Hospital, Rain Medical Center, Petah Tikva, Israel
Poraty, L., School of Plant Sciences and Food Security, Tel Aviv University, Ramat Aviv, Tel Aviv, Israel
Sternberg, H., School of Plant Sciences and Food Security, Tel Aviv University, Ramat Aviv, Tel Aviv, Israel
Buriakovsky, E., School of Plant Sciences and Food Security, Tel Aviv University, Ramat Aviv, Tel Aviv, Israel
Bar, E., Department of Field and Vegetable Crops, Agricultural Research Organization, Newe Ya'ar Reseach Center, Ramat Yishay, Israel
Lewinsohn, E., Department of Field and Vegetable Crops, Agricultural Research Organization, Newe Ya'ar Reseach Center, Ramat Yishay, Israel
Yalovsky, S., School of Plant Sciences and Food Security, Tel Aviv University, Ramat Aviv, Tel Aviv, Israel
ROPs or RACs are plant Rho-related GTPases implicated in the regulation of a multitude of signaling pathways that function at the plasma membrane via posttranslational lipid modifications. The relationships between ROP activation status and membrane localization has not been established. Here, we show that endogenous ROPs, as well as a transgenic His6-green fluorescent protein (GFP)-Arabidopsis thaliana ROP6 (AtROP6) fusion protein, were partitioned between Triton X-100- soluble and -insoluble membranes. In contrast, the His6-GFP-Atrop6CA activated mutant accumulated exclusively in detergent-resistant membranes. GDP induced accumulation of ROPs in Triton-soluble membranes, whereas GTPγS induced accumulation of ROPs in detergent-resistant membranes. Recombinant wild-type and constitutively active AtROP6 proteins were purified from Arabidopsis plants, and in turn, their lipids were cleaved and analyzed by gas chromatography-coupled mass spectrometry. In Tritonsoluble membranes, the wild-type AtROP6 was only prenylated, primarily by geranylgeranyl. The activated AtROP6 that accumulated in detergent-resistant membranes was modified by prenyl and acyl lipids, identified as palmitic and stearic acids. Consistently, activated His6-GFP-Atrop6CAmS156, in which C156 was mutated into serine, accumulated in Triton-soluble membranes. These findings show that upon GTP binding and activation, AtROP6, and possibly other ROPs, are transiently S-acylated, inducing their partitioning into detergent-resistant membranes. © 2017 American Society for Microbiology.
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Corrected and Republished from: Activation status-coupled transient S-acylation determines membrane partitioning of a plant Rho-related GTPase
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Sorek, N., School of Plant Sciences and Food Security, Tel Aviv University, Ramat Aviv, Tel Aviv, Israel, Beilinson Hospital, Rain Medical Center, Petah Tikva, Israel
Poraty, L., School of Plant Sciences and Food Security, Tel Aviv University, Ramat Aviv, Tel Aviv, Israel
Sternberg, H., School of Plant Sciences and Food Security, Tel Aviv University, Ramat Aviv, Tel Aviv, Israel
Buriakovsky, E., School of Plant Sciences and Food Security, Tel Aviv University, Ramat Aviv, Tel Aviv, Israel
Bar, E., Department of Field and Vegetable Crops, Agricultural Research Organization, Newe Ya'ar Reseach Center, Ramat Yishay, Israel
Lewinsohn, E., Department of Field and Vegetable Crops, Agricultural Research Organization, Newe Ya'ar Reseach Center, Ramat Yishay, Israel
Yalovsky, S., School of Plant Sciences and Food Security, Tel Aviv University, Ramat Aviv, Tel Aviv, Israel
Corrected and Republished from: Activation status-coupled transient S-acylation determines membrane partitioning of a plant Rho-related GTPase
ROPs or RACs are plant Rho-related GTPases implicated in the regulation of a multitude of signaling pathways that function at the plasma membrane via posttranslational lipid modifications. The relationships between ROP activation status and membrane localization has not been established. Here, we show that endogenous ROPs, as well as a transgenic His6-green fluorescent protein (GFP)-Arabidopsis thaliana ROP6 (AtROP6) fusion protein, were partitioned between Triton X-100- soluble and -insoluble membranes. In contrast, the His6-GFP-Atrop6CA activated mutant accumulated exclusively in detergent-resistant membranes. GDP induced accumulation of ROPs in Triton-soluble membranes, whereas GTPγS induced accumulation of ROPs in detergent-resistant membranes. Recombinant wild-type and constitutively active AtROP6 proteins were purified from Arabidopsis plants, and in turn, their lipids were cleaved and analyzed by gas chromatography-coupled mass spectrometry. In Tritonsoluble membranes, the wild-type AtROP6 was only prenylated, primarily by geranylgeranyl. The activated AtROP6 that accumulated in detergent-resistant membranes was modified by prenyl and acyl lipids, identified as palmitic and stearic acids. Consistently, activated His6-GFP-Atrop6CAmS156, in which C156 was mutated into serine, accumulated in Triton-soluble membranes. These findings show that upon GTP binding and activation, AtROP6, and possibly other ROPs, are transiently S-acylated, inducing their partitioning into detergent-resistant membranes. © 2017 American Society for Microbiology.
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