Analysis of cell-cycle specific localization of the Rdi1p RhoGDI and the structural determinants required for Cdc42p membrane localization and clustering at sites of polarized growth

Richman, Tamara J.; Toenjes, Kurt A.; Morales, Sergio E.; Cole, Karen C.; Wasserman, Burton S.; Taylor, Chad M.; Koster, Jacob A.; Whelihan, Matthew F.; Johnson, Douglas I.

doi:10.1007/s00294-004-0505-9

Cited by 37 publications

(11 citation statements)

References 47 publications

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“…Most interestingly, An18g04590, an ortholog of the S. cerevisiae Rho GDP dissociation inhibitor Rdi1p displayed increased expression. Rdi1p regulates the Rho GTPases Cdc42p, Rho1p and Rho4p, localizes to polarized growth sites at specific times of the cell cycle and extracts all three proteins from the plasma membrane to keep them in an inactive cytosolic state [52]–[54]. Overexpression of Rdi1p causes slightly rounder cell morphology in S. cerevisiae [55].…”

Section: Resultsmentioning

confidence: 99%

The Transcriptomic Signature of RacA Activation and Inactivation Provides New Insights into the Morphogenetic Network of Aspergillus niger

et al. 2013

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RacA is the main Rho GTPase in Aspergillus niger regulating polarity maintenance via controlling actin dynamics. Both deletion and dominant activation of RacA (RacG18V) provoke an actin localization defect and thereby loss of polarized tip extension, resulting in frequent dichotomous branching in the ΔracA strain and an apolar growing phenotype for RacG18V. In the current study the transcriptomics and physiological consequences of these morphological changes were investigated and compared with the data of the morphogenetic network model for the dichotomous branching mutant ramosa-1. This integrated approach revealed that polar tip growth is most likely orchestrated by the concerted activities of phospholipid signaling, sphingolipid signaling, TORC2 signaling, calcium signaling and CWI signaling pathways. The transcriptomic signatures and the reconstructed network model for all three morphology mutants (ΔracA, RacG18V, ramosa-1) imply that these pathways become integrated to bring about different physiological adaptations including changes in sterol, zinc and amino acid metabolism and changes in ion transport and protein trafficking. Finally, the fate of exocytotic (SncA) and endocytotic (AbpA, SlaB) markers in the dichotomous branching mutant ΔracA was followed, demonstrating that hyperbranching does not per se result in increased protein secretion.

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Section: Resultsmentioning

confidence: 99%

The Transcriptomic Signature of RacA Activation and Inactivation Provides New Insights into the Morphogenetic Network of Aspergillus niger

et al. 2013

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“…1A). Cdc42p also regulates the filamentous-growth pathway at the level of Ste20p (23)(24)(25)(26) and functions at the PM (123)(124)(125). Bem4p and Cdc42p were previously shown to interact and exhibit genetic interactions (39,41).…”

Section: Bem4pmentioning

confidence: 99%

Cdc42p-Interacting Protein Bem4p Regulates the Filamentous-Growth Mitogen-Activated Protein Kinase Pathway

Pitoniak

Chavel

Chow

et al. 2015

Molecular and Cellular Biology

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The ubiquitous Rho (Ras homology) GTPase Cdc42p can function in different settings to regulate cell polarity and cellular signaling. How Cdc42p and other proteins are directed to function in a particular context remains unclear. We show that the Cdc42p-interacting protein Bem4p regulates the mitogen-activated protein kinase (MAPK) pathway that controls filamentous growth in Saccharomyces cerevisiae. Bem4p controlled the filamentous-growth pathway but not other MAPK pathways (mating or high-osmolarity glycerol response [HOG]) that also require Cdc42p and other shared components. Bem4p associated with the plasma membrane (PM) protein, Sho1p, to regulate MAPK activity and cell polarization under nutrient-limiting conditions that favor filamentous growth. Bem4p also interacted with the major activator of Cdc42p, the guanine nucleotide exchange factor (GEF) Cdc24p, which we show also regulates the filamentous-growth pathway. Bem4p interacted with the pleckstrin homology (PH) domain of Cdc24p, which functions in an autoinhibitory capacity, and was required, along with other pathway regulators, to maintain Cdc24p at polarized sites during filamentous growth. Bem4p also interacted with the MAPK kinase kinase (MAPKKK) Ste11p. Thus, Bem4p is a new regulator of the filamentous-growth MAPK pathway and binds to general proteins, like Cdc42p and Ste11p, to promote a pathway-specific response.

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“…In order to gain insights into the molecular mechanisms regulating the location and rate of Rdi1-mediated Cdc42 recycling, we performed a suppressor screen taking advantage of the fact that over-expression of Rdi1 under the Gal1 promoter represses yeast growth, likely due to over-extraction of Cdc42 and other essential Rho family GTPases from membrane compartments 13 (also see Fig. 1).…”

mentioning

confidence: 99%

Flippase-mediated phospholipid asymmetry promotes fast Cdc42 recycling in dynamic maintenance of cell polarity

et al. 2012

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Lipid asymmetry at the plasma membrane is essential for such processes as cell polarity, cytokinesis and phagocytosis1-3. Here we identify the lipid flippase complex, composed of Lem3, Dnf1 or Dnf24, to play a role in the dynamic recycling of the Cdc42 GTPase, a key regulator of cell polarity5, in yeast. By using quantitative microscopy methods, we show that the flippase complex is required for fast dissociation of Cdc42 from the polar cortex by the guanine nucleotide dissociation inhibitor (GDI). A loss of flippase activity, or pharmacological blockage of the inward flipping of phosphatidylethanolamine (PE), a phospholipid with a neutral head group, disrupts Cdc42 polarity maintained by GDI-mediated recycling. PE flipping may reduce the charge interaction between a Cdc42 C-terminal cationic region with the plasma membrane inner leaflet, enriched for the negatively charged lipid phosphatidylserine (PS). Using a reconstituted system with supported lipid bilayers, we show that the relative composition of PE versus PS directly modulates Cdc42 extraction from the membrane by GDI.

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Analysis of cell-cycle specific localization of the Rdi1p RhoGDI and the structural determinants required for Cdc42p membrane localization and clustering at sites of polarized growth

Cited by 37 publications

References 47 publications

The Transcriptomic Signature of RacA Activation and Inactivation Provides New Insights into the Morphogenetic Network of Aspergillus niger

The Transcriptomic Signature of RacA Activation and Inactivation Provides New Insights into the Morphogenetic Network of Aspergillus niger

Cdc42p-Interacting Protein Bem4p Regulates the Filamentous-Growth Mitogen-Activated Protein Kinase Pathway

Flippase-mediated phospholipid asymmetry promotes fast Cdc42 recycling in dynamic maintenance of cell polarity

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