ArticleThe Journal of biological chemistry2012
C-terminal di-arginine motif of Cdc42 protein is essential for binding to phosphatidylinositol 4,5-bisphosphate-containing membranes and inducing cellular transformation.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 55 citations in OpenAlex.
- Protein Language Model Embeddings Recover Evolutionary and Functional Organization Across the Ras Superfamily.Journal of molecular evolution · 2026Article
- Sortase A-Mediated Farnesylation of Cdc42ACS synthetic biology · 2026Article
- Oligomerization-dependent and synergistic regulation of Cdc42 GTPase cycling by a GEF and a GAP.EMBO reports · 2026Article
- Distinct impact of PI(4)P flux on PI(4,5)PProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Nanoscale clustering and dynamics of phosphatidylinositol 4,5-bisphosphate in an immune cell model.Biophysical journal · 2025Article
- Atypical Protein Kinase C Promotes its own Asymmetric Localisation by Phosphorylating Cdc42 in thebioRxiv : the preprint server for biology · 2024Article
- mTORC2-NDRG1-CDC42 axis couples fasting to mitochondrial fission.Nature cell biology · 2023Article
- Why Does Synergistic Activation of WASP, but Not N-WASP, by Cdc42 and PIPJournal of molecular biology · 2023Article
- Repair of traumatic lesions to the plasmalemma of neurons and other cells: Commonalities, conflicts, and controversies.Frontiers in physiology · 2023Review
- The role of cell division control protein 42 in tumor and non-tumor diseases: A systematic review.Journal of Cancer · 2022Review
- Lipidation of small GTPase Cdc42 as regulator of its physiological and pathophysiological functions.Frontiers in physiology · 2022Review
- PIPCell calcium · 2021Article
- RHO GTPases: from new partners to complex immune syndromes.Nature reviews. Immunology · 2021Review
- Molecular subversion of Cdc42 signalling in cancer.Biochemical Society transactions · 2021Review
- Active and Inactive Cdc42 Differ in Their Insert Region Conformational Dynamics.Biophysical journal · 2021Article
- Elevating EGFR-MAPK program by a nonconventional Cdc42 enhances intestinal epithelial survival and regeneration.JCI insight · 2020Article
- Monoterpenes Differently Regulate Acid-Sensitive and Mechano-Gated KFrontiers in pharmacology · 2020Article
- Actin Remodeling Defects Leading to Autoinflammation and Immune Dysregulation.Frontiers in immunology · 2020Review
- Human Autoinflammatory Diseases Mediated by NLRP3-, Pyrin-, NLRP1-, and NLRC4-Inflammasome Dysregulation Updates on Diagnosis, Treatment, and the Respective Roles of IL-1 and IL-18.Frontiers in immunology · 2020Review
- Severe autoinflammation in 4 patients with C-terminal variants in cell division control protein 42 homolog (CDC42) successfully treated with IL-1β inhibition.The Journal of allergy and clinical immunology · 2019Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Rho GTPases regulate a diverse range of processes that are dependent on their proper cellular localization. The membrane localization of these GTPases is due in large part to their carboxyl-terminal geranylgeranyl moiety. In addition, most of the Rho family members contain a cluster of positively charged residues (i.e. a "polybasic domain"), directly preceding their geranylgeranyl moiety, and it has been suggested that this domain serves to fine-tune their localization among different cellular membrane sites. Here, we have taken a closer look at the role of the polybasic domain of Cdc42 in its ability to bind to membranes and induce the transformation of fibroblasts. A FRET assay for the binding of Cdc42 to liposomes of defined composition showed that Cdc42 associates more strongly with liposomes containing phosphatidylinositol 4,5-bisphosphate (PIP(2)) when compared either with uncharged control membranes or with liposomes containing a charge-equivalent amount of phosphatidylserine. The carboxyl-terminal di-arginine motif (Arg-186 and Arg-187) was shown to play an essential role in the binding of Cdc42 to PIP(2)-containing membranes. We further showed that substitutions for the di-arginine motif, when introduced within a constitutively active ("fast cycling") Cdc42(F28L) background, had little effect on the ability of the activated Cdc42 mutant to induce microspikes/filopodia in NIH 3T3 cells, whereas they eliminated its ability to transform fibroblasts. Taken together, these findings suggest that the di-arginine motif within the carboxyl terminus of Cdc42 is necessary for this GTPase to bind at membrane sites containing PIP(2), where it can initiate signaling activities that are essential for the oncogenic transformation of cells.
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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.