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Septin ring assembly involves cycles of GTP loading and hydrolysis by Cdc42p
Amy S Gladfelter1, Indrani Bose, Trevin R Zyla
1Department of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, NC 27710, USA.
The Journal of Cell Biology
|January 25, 2002
Summary
GTP hydrolysis by the GTPase Cdc42p is crucial for proper septin ring assembly during the yeast cell cycle. Defects in GTP hydrolysis lead to septin misorganization, highlighting Cdc42p
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- The GTPase Cdc42p regulates cell cycle events in budding yeast.
- Septin ring assembly is essential for cytokinesis and bud emergence.
Purpose of the Study:
- To investigate the role of Cdc42p GTP hydrolysis in septin ring organization.
- To identify specific Cdc42p functions in septin assembly.
Main Methods:
- Analysis of cdc42 mutants with defects in GTP hydrolysis.
- Genetic analysis involving GTPase-activating proteins (GAPs) and their deletions.
- Investigating the effects of altered GTP hydrolysis on septin organization.
Main Results:
- Mutants with impaired GTP hydrolysis by Cdc42p exhibited septin misorganization.
- Overexpression of Cdc42p GAPs suppressed septin defects.
- Deletion of Cdc42p GAPs also led to septin misorganization.
Conclusions:
- GTP hydrolysis by Cdc42p is critical for the dynamic assembly of the septin ring.
- Cdc42p may function as an assembly factor, utilizing its GTPase cycle for macromolecular structure formation.
- This contrasts with its known role as a GTP-dependent effector switch.