ArticleCurrent biology : CB2016
Parallel Actin-Independent Recycling Pathways Polarize Cdc42 in Budding Yeast.
Article in Current biology : CB, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
28 citing papers in PubMed, 45 citations in OpenAlex.
- Sortase A-Mediated Farnesylation of Cdc42ACS synthetic biology · 2026Article
- Polarization as a Process: The Potential of Process Ontology for Understanding Cellular Symmetry Breaking.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026Review
- Global genetic rewiring during compensatory evolution in the yeast polarity network.EMBO reports · 2026Article
- Design principles and feedback mechanisms in organelle size control.Current opinion in cell biology · 2025Review
- The biochemical mechanism of Rho GTPase membrane binding, activation and retention in activity patterning.The EMBO journal · 2025Article
- Cdc42 mobility and membrane flows regulate fission yeast cell shape and survival.Nature communications · 2024Article
- Article
- Redundancy and the role of protein copy numbers in the cell polarization machinery of budding yeast.Nature communications · 2023Article
- Chaperone-Dependent Degradation of Cdc42 Promotes Cell Polarity and Shields the Protein from Aggregation.Molecular and cellular biology · 2023Article
- Regulation of Cdc42 protein turnover modulates the filamentous growth MAPK pathway.The Journal of cell biology · 2022Article
- Pole position: How plant cells polarize along the axes.The Plant cell · 2022Review
- Chemotactic movement of a polarity site enables yeast cells to find their mates.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- A Fully Functional ROP Fluorescent Fusion Protein Reveals Roles for This GTPase in Subcellular and Tissue-Level Patterning.The Plant cell · 2020Article
- Auxin-induced signaling protein nanoclustering contributes to cell polarity formation.Nature communications · 2020Article
- Article
- Regulation of Cdc42 for polarized growth in budding yeast.Microbial cell (Graz, Austria) · 2020Review
- Mechanistic insights into actin-driven polarity site movement in yeast.Molecular biology of the cell · 2020Article
- Review
- Polarity establishment by Cdc42: Key roles for positive feedback and differential mobility.Small GTPases · 2019Review
- Cell-cycle control of cell polarity in yeast.The Journal of cell biology · 2019Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
The highly conserved Rho-family GTPase Cdc42 is an essential regulator of polarity in many different cell types. During polarity establishment, Cdc42 becomes concentrated at a cortical site, where it interacts with downstream effectors to orient the cytoskeleton along the front-back axis. To concentrate Cdc42, loss of Cdc42 by diffusion must be balanced by recycling to the front. In Saccharomyces cerevisiae, the guanine nucleotide dissociation inhibitor (GDI) Rdi1 recycles Cdc42 through the cytoplasm. Loss of Rdi1 slowed but did not eliminate Cdc42 accumulation at the front, suggesting the existence of other recycling pathways. One proposed pathway involves actin-directed trafficking of vesicles carrying Cdc42 to the front. However, we found no role for F-actin in Cdc42 concentration, even in rdi1Δ cells. Instead, Cdc42 was still able to exchange between the membrane and cytoplasm in rdi1Δ cells, albeit at a reduced rate. Membrane-cytoplasm exchange of GDP-Cdc42 was faster than that of GTP-Cdc42, and computational modeling indicated that such exchange would suffice to promote polarization. We also uncovered a novel role for the Cdc42-directed GTPase-activating protein (GAP) Bem2 in Cdc42 polarization. Bem2 was known to act in series with Rdi1 to promote recycling of Cdc42, but we found that rdi1Δ bem2Δ mutants were synthetically lethal, suggesting that they also act in parallel. We suggest that GAP activity cooperates with the GDI to counteract the dissipative effect of a previously unappreciated pathway whereby GTP-Cdc42 escapes from the polarity site through the cytoplasm.
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What OpenQuestion holds
Registered trials
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.