Association of the Rho family small GTP-binding proteins with Rho GDP dissociation inhibitor (Rho GDI) in Saccharomyces cerevisiae

Koch, Gertrude; Tanaka, Kazuma; Masuda, Tomomi; Yamochi, Wataru; Nonaka, Hidemi; Takai, Yoshimi

doi:10.1038/sj.onc.1201194

Cited by 62 publications

(60 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…RhoGDIa has been described as a ubiquitously expressed protein, which is found primarily in the cytoplasm of cells (Koch et al 1997). Thus, we were surprised when we identified endogenously expressed RhoGDIa from HeLa nuclear extracts as a component of a large multiprotein complex associated with the DNA-bound ERa (Schultz-Norton et al 2007).…”

Section: Resultsmentioning

confidence: 98%

“…RhoGTPases act as molecular switches cycling between an active, GTP-bound form, which is anchored to the cell membrane, and an inactive, GDP-bound form, which is present in the cytoplasm (Koch et al 1997). When bound to GTP, RhoGTPases interact with downstream effector proteins and foster signal propagation.…”

Section: Introductionmentioning

confidence: 99%

“…Using agarose gel mobility shift assays and mass spectrometry analysis, we identified novel HeLa nuclear proteins associated with the DNA-bound estrogen receptor a (ERa; Schultz-Norton et al 2007). One of these ERa-associated proteins was the 28 kDa protein Rho GDP dissociation inhibitor a (RhoGDIa), which was originally characterized as a negative regulator of the RhoGTPase family members RhoA, Rac1, and Cdc42 (Fukumoto et al 1990, Leonard et al 1992, Masuda et al 1994, Koch et al 1997, Olofsson 1999. Although the ability of RhoGDIa to enhance transcription of an estrogen response element (ERE)-containing reporter plasmid has been reported previously, it was thought that this enhanced activity was due to the cytoplasmic actions of RhoGDIa (Su et al 2001(Su et al , 2002).…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Rho GDP dissociation inhibitor α interacts with estrogen receptor α and influences estrogen responsiveness

Marzouk

Schultz-Norton

Likhite

et al. 2007

Journal of Molecular Endocrinology

View full text Add to dashboard Cite

Estrogen receptor a (ERa) is a ligand-activated transcription factor that regulates expression of estrogen-responsive genes. Upon binding of the ligand-occupied ERa to estrogen response elements (EREs) in DNA, the receptor interacts with a variety of coregulatory proteins to modulate transcription of target genes. We have isolated and identified a number of proteins associated with the DNA-bound ERa. One of these proteins, Rho guanosine diphosphate (GDP) dissociation inhibitor a (RhoGDIa), is a negative regulator of the Rho family of GTP-binding proteins. In this study, we demonstrate that endogenously expressed RhoGDIa is present in the nucleus as well as the cytoplasm of MCF-7 breast cancer cells, and that RhoGDIa binds directly to ERa, alters the ERa-ERE interaction, and influences the ability of ERa to regulate transcription of a heterologous estrogen-responsive reporter plasmid in transient transfection assays as well as endogenous, estrogen-responsive genes in MCF-7 cells. Our studies suggest that, in addition to the activity of RhoGDIa in the cytoplasm, it also influences ERa signaling in the nucleus.

show abstract

Section: Resultsmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Rho GDP dissociation inhibitor α interacts with estrogen receptor α and influences estrogen responsiveness

Marzouk

Schultz-Norton

Likhite

et al. 2007

Journal of Molecular Endocrinology

View full text Add to dashboard Cite

show abstract

“…It has been shown that Rdi1 is able to extract Cdc42 and Rho1 from membranes (Koch et al, 1997;Eitzen et al, 2001;Richman et al, 2004;Tcheperegine et al, 2005), but it has not been tested whether Rdi1 interacts with other Rho GTPases as well. Therefore, we performed immunoprecipitation experiments with strains in which Rho GTPases were N-terminally tagged with the HA and Rdi1 C-terminally with the myc epitope.…”

Section: Rdi1 Specifically Interacts With Cdc42 Rho1 and Rho4mentioning

confidence: 99%

“…In contrast, others claim that RDI1 overexpression causes only a slightly rounder cell morphology (Tcheperegine et al, 2005). Deletion of RDI1 does not produce any detectable phenotypes in budding yeast (Masuda et al, 1994), but in the human fungal pathogen Candida albicans, cells lacking RDI1 exhibit reduced polarized growth (Court and Sudbery, 2007).Rdi1 is found in the cytoplasm, but it also localizes to the tips of small buds and the bud neck region, where it interacts with Cdc42 (Koch et al, 1997;Richman et al, 2004;Cole et al, 2007). Rdi1 has the ability to extract Cdc42 and Rho1 from vacuolar membranes (Eitzen et al, 2001), and it can also extract Cdc42 from the plasma membrane (Richman et al, 2004;Tcheperegine et al, 2005).…”

mentioning

confidence: 99%

The Rho GDI Rdi1 Regulates Rho GTPases by Distinct Mechanisms

Tiedje

Sakwa

Just

et al. 2008

MBoC

View full text Add to dashboard Cite

The small guanosine triphosphate (GTP)-binding proteins of the Rho family are implicated in various cell functions, including establishment and maintenance of cell polarity. Activity of Rho guanosine triphosphatases (GTPases) is not only regulated by guanine nucleotide exchange factors and GTPase-activating proteins but also by guanine nucleotide dissociation inhibitors (GDIs). These proteins have the ability to extract Rho proteins from membranes and keep them in an inactive cytosolic complex. Here, we show that Rdi1, the sole Rho GDI of the yeast Saccharomyces cerevisiae, contributes to pseudohyphal growth and mitotic exit. Rdi1 interacts only with Cdc42, Rho1, and Rho4, and it regulates these Rho GTPases by distinct mechanisms. Binding between Rdi1 and Cdc42 as well as Rho1 is modulated by the Cdc42 effector and p21-activated kinase Cla4. After membrane extraction mediated by Rdi1, Rho4 is degraded by a novel mechanism, which includes the glycogen synthase kinase 3␤ homologue Ygk3, vacuolar proteases, and the proteasome. Together, these results indicate that Rdi1 uses distinct modes of regulation for different Rho GTPases. INTRODUCTIONSmall guanosine triphosphatases (GTPases) of the Rho family control fundamental processes of cell biology common to all eukaryotes, such as morphogenesis, polarity, movement, and cell division (Jaffe and Hall, 2005). In the budding yeast Saccharomyces cerevisiae, which encodes six Rho GTPases (Cdc42 and Rho1 to Rho5), these proteins play a pivotal role in the establishment of cell polarity (Park and Bi, 2007). Budding yeast cells undergo polarized growth during various phases of their life cycle, including budding during vegetative growth, mating between haploid cells of opposite mating types, and filamentous growth upon nutrient limitation. Although Cdc42 and Rho1 are well characterized, little is known about the other Rho proteins. Membrane association of Rho-type GTPases is essential for their function, and it depends on a C-terminal prenyl moiety and an adjacent polybasic region. Cdc42 localizes to internal membranes and the entire plasma membrane, where it clusters at sites of polarized growth, including the tips of mating projections, incipient bud sites, the tips and sides of growing buds, and the bud neck region of large-budded cells (Ziman et al., 1993;Richman et al., 2002). In addition to membranebound Cdc42, a cytoplasmic pool has been found (Ziman et al., 1993). Similar to Cdc42, Rho1 has been shown to localize at sites of polarized growth .Like other regulatory GTPases, they act as molecular switches, cycling between an active guanosine triphosphate (GTP)-bound state and an inactive guanosine diphosphate (GDP)-bound state. This activity is highly regulated by guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs). The exchange of GDP to GTP, and thus the activation of Cdc42, is catalyzed by GEFs. In the active GTP-bound state, Rho GTPases perform their regulatory function through a conformation-specific interaction with effector proteins. G...

show abstract

Analysis of proteome and transcriptome of tumor necrosis factor α stimulated vascular smooth muscle cells with or without alpha lipoic acid

et al. 2004

View full text Add to dashboard Cite

Vascular smooth muscle cells (VSMCs) play an important role in the development and progression of atherosclerosis. Tumor necrosis factor alpha (TNFalpha), a cytokine secreted by VSMCs and macrophages in atherosclerotic lesions, regulates a variety of cellular functions of inflammatory cells and VSMCs by promoting cell growth and motility, which are critical for the initiation and progression of vascularlesions. Alpha lipoic acid (ALA), a well known antioxidant, acts as a pyruvate dehydrogenase cofactor in mitochondrial metabolism. Recently, we reported that ALA has many beneficial effects on vascular cells in atherosclerosis. The aim of the current study was to examine VSMCs, treated for 24 hours with TNFalpha (10 ng/mL) in the presence or absence of ALA (2 mM), for differential protein and genes expression using two-dimensional gel electrophoresis (2-DE) and DNA microarray analysis, respectively. Using 2-DE, we identified proteins whose expression changed by at least 2.5-fold after TNFalpha stimulation. Proteins up-regulated by TNFalpha that were subsequently down-regulated in the presence of ALA were identified by matrix-assisted laser desorption/ionization-time of flight mass spectrometry as plasminogen activator inhibitor-2, fetal liver LKB-interacting protein, osteoblast-specific factor 2, glucosidase II, cyclin-dependent kinase 3, endoplasmin precursor and glutathione synthetase. TNFalpha down-regulated proteins that were up-regulated in the presence of ALA were keratin 19, eukaryotic translation elongation factor and Rho GDP dissociation inhibitor alpha. Gene expression analysis using DNA microarray tools confirmed the up-regulation or down-regulation of some, but not all, of the proteins observed in ALA challenged, TNFalpha-treated cells. This data should provide valuable information about the underlying mechanisms of atherosclerosis.

show abstract

Association of the Rho family small GTP-binding proteins with Rho GDP dissociation inhibitor (Rho GDI) in Saccharomyces cerevisiae

Cited by 62 publications

References 24 publications

Rho GDP dissociation inhibitor α interacts with estrogen receptor α and influences estrogen responsiveness

Rho GDP dissociation inhibitor α interacts with estrogen receptor α and influences estrogen responsiveness

The Rho GDI Rdi1 Regulates Rho GTPases by Distinct Mechanisms

Analysis of proteome and transcriptome of tumor necrosis factor α stimulated vascular smooth muscle cells with or without alpha lipoic acid

Contact Info

Product

Resources

About