ArticleMolecular and cellular biology2013
Identification of a novel prenyl and palmitoyl modification at the CaaX motif of Cdc42 that regulates RhoGDI binding.
Article in Molecular and cellular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed, 90 citations in OpenAlex.
- Non-canonical and constitutive activation of small GTPases: more than an exception to the rule?The Biochemical journal · 2026Review
- Rac1 palmitoylation is required for cardiac stress adaptation and regulation of protein kinase A signaling.JCI insight · 2025Article
- Protein lipidation in the tumor microenvironment: enzymology, signaling pathways, and therapeutics.Molecular cancer · 2025Review
- Oleate Promotes Triple-Negative Breast Cancer Cell Migration by Enhancing Filopodia Formation through a PLD/Cdc42-Dependent Pathway.International journal of molecular sciences · 2024Article
- Protein Tyrosine Phosphatase PRL-3: A Key Player in Cancer Signaling.Biomolecules · 2024Review
- The distinct localization of CDC42 isoforms is responsible for their specific functions during migration.The Journal of cell biology · 2024Article
- Salmonella engages CDC42 effector protein 1 for intracellular invasion.Journal of cellular physiology · 2024Article
- Molecular dynamics simulations reveal the inhibition mechanism of Cdc42 by RhoGDI1.Journal of computer-aided molecular design · 2023Article
- An isoform-specific function of Cdc42 in regulating mammalian Exo70 during axon formation.Life science alliance · 2023Article
- Palmitoylation of the small GTPase Cdc42 by DHHC5 modulates spine formation and gene transcription.The Journal of biological chemistry · 2022Article
- Underappreciated roles for Rho GDP dissociation inhibitors (RhoGDIs) in cell function: Lessons learned from the pancreatic islet β-cell.Biochemical pharmacology · 2022Review
- The complex, dynamic SpliceOme of the small GTPase transcripts altered by technique, sex, genetics, tissue specificity, and RNA base editing.Frontiers in cell and developmental biology · 2022Article
- Lipidation of small GTPase Cdc42 as regulator of its physiological and pathophysiological functions.Frontiers in physiology · 2022Review
- Molecular subversion of Cdc42 signalling in cancer.Biochemical Society transactions · 2021Review
- A Not-So-Ancient Grease History: Click Chemistry and Protein Lipid Modifications.Chemical reviews · 2021Review
- Selective axonal translation of the mRNA isoform encoding prenylated Cdc42 supports axon growth.Journal of cell science · 2021Article
- Roles of palmitoylation in structural long-term synaptic plasticity.Molecular brain · 2021Review
- Targeting SMYD3 to Sensitize Homologous Recombination-Proficient Tumors to PARP-Mediated Synthetic Lethality.iScience · 2020Article
- Elevating EGFR-MAPK program by a nonconventional Cdc42 enhances intestinal epithelial survival and regeneration.JCI insight · 2020Article
- Prenylation of Axonally Translated Rac1 Controls NGF-Dependent Axon Growth.Developmental cell · 2020Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Membrane localization of Rho GTPases is essential for their biological functions and is dictated in part by a series of posttranslational modifications at a carboxyl-terminal CaaX motif: prenylation at cysteine, proteolysis of the aaX tripeptide, and carboxymethylation. The fidelity and variability of these CaaX processing steps are uncertain. The brain-specific splice variant of Cdc42 (bCdc42) terminates in a CCIF sequence. Here we show that brain Cdc42 undergoes two different types of posttranslational modification: classical CaaX processing or novel tandem prenylation and palmitoylation at the CCaX cysteines. In the dual lipidation pathway, bCdc42 was prenylated, but it bypassed proteolysis and carboxymethylation to undergo modification with palmitate at the second cysteine. The alternative postprenylation processing fates were conserved in the GTPases RalA and RalB and the phosphatase PRL-3, proteins terminating in a CCaX motif. The differentially modified forms of bCdc42 displayed functional differences. Prenylated and palmitoylated brain Cdc42 did not interact with RhoGDIα and was enriched in the plasma membrane relative to the classically processed form. The alternative processing of prenylated CCaX motif proteins by palmitoylation or by endoproteolysis and methylation expands the diversity of signaling GTPases and enables another level of regulation through reversible modification with palmitate.
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