ArticleThe Plant cell2002
A cell-specific, prenylation-independent mechanism regulates targeting of type II RACs.
Article in The Plant cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.
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Who cites it
66 citing papers in PubMed, 143 citations in OpenAlex.
- Nucleotide-dependent switching and RIPb effector recognition of the barley susceptibility factor RACB.Communications biology · 2026Article
- C-terminal S-acylation governs membrane distribution, interaction dynamics and function of a plant Rho GTPase.PloS one · 2026Article
- Protein Prenylation Makeovers in Plants: Insights into Substrate Diversification.International journal of molecular sciences · 2025Review
- Global analysis of membrane protein S-acylation in the model plantbioRxiv : the preprint server for biology · 2025Article
- Protein Prenylation in Plants: Mechanisms and Functional Implications.Plants (Basel, Switzerland) · 2025Review
- Versatile CYP98A enzymes catalyse meta-hydroxylation reveals diversity of salvianolic acids biosynthesis.Plant biotechnology journal · 2024Article
- Cloning and Functional Analysis of CsROP5 and CsROP10 Genes Involved in Cucumber Resistance toBiology · 2024Article
- Analysis of Rac/Rop Small GTPase Family Expression inLife (Basel, Switzerland) · 2022Article
- Microtubule-associated ROP interactors affect microtubule dynamics and modulate cell wall patterning and root hair growth.Development (Cambridge, England) · 2022Article
- Protein S-acyltransferases and acyl protein thioesterases, regulation executors of protein S-acylation in plants.Frontiers in plant science · 2022Review
- Interaction of OsRopGEF3 Protein With OsRac3 to Regulate Root Hair Elongation and Reactive Oxygen Species Formation in Rice (Frontiers in plant science · 2021Article
- A Fully Functional ROP Fluorescent Fusion Protein Reveals Roles for This GTPase in Subcellular and Tissue-Level Patterning.The Plant cell · 2020Article
- Article
- A novel Ca2+-binding protein that can rapidly transduce auxin responses during root growth.PLoS biology · 2019Article
- Dynamic Protein S-Acylation in Plants.International journal of molecular sciences · 2019Review
- S-acylation of a geminivirus C4 protein is essential for regulating the CLAVATA pathway in symptom determination.Journal of experimental botany · 2018Article
- ROP GTPases Structure-Function and Signaling Pathways.Plant physiology · 2018Review
- Corrected and Republished from: Activation Status-Coupled Transient S-Acylation Determines Membrane Partitioning of a Plant Rho-Related GTPase.Molecular and cellular biology · 2017Article
- A Lipid-Anchored NAC Transcription Factor Is Translocated into the Nucleus and ActivatesThe Plant cell · 2017Article
- The RopGEF2-ROP7/ROP2 Pathway Activated by phyB Suppresses Red Light-Induced Stomatal Opening.Plant physiology · 2017Article
6 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The RHO proteins, which regulate numerous signaling cascades, undergo prenylation, facilitating their interaction with membranes and with proteins called RHO.GDP dissociation inhibitors. It has been suggested that prenylation is required for RHO function. Eleven RHO-related proteins were identified in Arabidopsis. Eight of them are putatively prenylated. We show that targeting of the remaining three proteins, AtRAC7, AtRAC8, and AtRAC10, is prenylation independent, requires palmitoylation, and occurs by a cell-specific mechanism. AtRAC8 and AtRAC10 could not be prenylated by either farnesyltransferase or geranylgeranyltransferase I, whereas AtRAC7 could be prenylated by both enzymes in yeast. The association of AtRAC7 with the plasma membrane in plants did not require farnesyltransferase or a functional CaaX box. Recombinant AtRAC8 was palmitoylated in vitro, and inhibition of protein palmitoylation relieved the association of all three proteins with the plasma membrane. Interestingly, AtRAC8 and a constitutively active mutant, Atrac7mV(15), were not associated with the plasma membrane in root hair cells, whose elongation requires the localization of prenylated RHOs in the plasma membrane at the cell tip. Moreover, Atrac7mV(15) did not induce root hair deformation, unlike its prenylated homologs. Thus, AtRAC7, AtRAC8, and AtRAC10 may represent a group of proteins that have evolved to fulfill unique functions.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.