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• W2320532413 abstract "Prenylation, the post-translational attachment of prenyl groups to substrate proteins, can affect their distribution and interactomes. Arabidopsis PLURIPETALA (PLP) encodes the shared α subunit of two heterodimeric protein isoprenyltransferases, whose functional loss provides a unique opportunity to study developmental and cellular processes mediated by its prenylated substrates, such as ROP GTPases. As molecular switches, the distribution and activation of ROPs are mediated by various factors, including guanine nucleotide exchange factors, GTPase activating proteins, guanine nucleotide dissociation inhibitors (RhoGDIs), prenylation, and S-acylation. However, how these factors together ensure that dynamic ROP signalling is still obscure. We report here that a loss-of-function allele of PLP resulted in cytoplasmic accumulation of ROP2 in root hairs and reduced its stability. Consequently, two downstream events of ROP signalling, i.e. actin microfilament (MF) organization and the production of reactive oxygen species (ROS), were compromised. Genetic, cytological and biochemical evidence supports an additive interaction between prenylation and RhoGDI1/SCN1 in ROP2 distribution and stability whereas PLP acts synergistically with the protein S-acyl transferase TIP GROWTH DEFECTIVE1 during root hair growth. By using root hair growth as a model system, we uncovered complex interactions among prenylation, RhoGDIs, and S-acylation in dynamic ROP signalling." @default.
• W2320532413 created "2016-06-24" @default.
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• W2320532413 date "2016-06-01" @default.
• W2320532413 modified "2023-10-18" @default.
• W2320532413 title "<i>PLURIPETALA</i>mediates ROP2 localization and stability in parallel to<i>SCN1</i>but synergistically with<i>TIP1</i>in root hairs" @default.
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• W2320532413 doi "https://doi.org/10.1111/tpj.13179" @default.
• W2320532413 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27037800" @default.
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