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Updated: Mar 17, 2026

Manipulation and Analysis of Cell Cycle-Dependent Processes in Budding Yeast
Published on: September 26, 2025
Parallel Actin-Independent Recycling Pathways Polarize Cdc42 in Budding Yeast
Benjamin Woods1, Helen Lai1, Chi-Fang Wu1
1Department of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, NC 27710, USA.
The Rho-family GTPase Cdc42 is crucial for cell polarity. New findings reveal that guanine nucleotide dissociation inhibitor (GDI) and GTPase-activating protein (GAP) pathways cooperate to maintain Cdc42 concentration at the cell front.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Cdc42, a Rho-family GTPase, is vital for establishing cell polarity by concentrating at cortical sites.
- This concentration requires balancing Cdc42 loss via diffusion with recycling to the cell front.
- In yeast, guanine nucleotide dissociation inhibitor (GDI) Rdi1 recycles Cdc42, but other pathways likely exist.
Purpose of the Study:
- To investigate alternative Cdc42 recycling pathways beyond Rdi1.
- To explore the role of actin in Cdc42 concentration.
- To uncover novel regulators of Cdc42 polarization.
Main Methods:
- Genetic analysis of Saccharomyces cerevisiae mutants (e.g., rdi1Δ, bem2Δ).
- Observation of Cdc42 localization and dynamics.
- Computational modeling of Cdc42 exchange between membrane and cytoplasm.
Main Results:
- F-actin does not play a role in Cdc42 concentration, even when Rdi1 is absent.
- Cdc42 exchanges between the membrane and cytoplasm, with GDP-Cdc42 exchange being faster.
- GTPase-activating protein (GAP) Bem2 has a novel role in Cdc42 polarization, acting in parallel with Rdi1.
Conclusions:
- Cell polarity is maintained by membrane-cytoplasm exchange of Cdc42, sufficient for polarization.
- GDI and GAP activities cooperate to counteract Cdc42 diffusion away from the polarity site.
- A previously unappreciated pathway allows GTP-Cdc42 to escape the polarity site, which is counteracted by GAP activity.
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