Regulation of Cell Polarity by Interactions of Msb3 and Msb4 with Cdc42 and Polarisome Components

Tcheperegine, Serguei E.; Gao, Xiang-Dong; Bi, Erfei

doi:10.1128/mcb.25.19.8567-8580.2005

Cited by 65 publications

(91 citation statements)

References 76 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…In the fungus Cryptococcus neoformans, Cdc42 is mislocalized to the cytoplasm when the Rho GDI homolog is overexpressed (Price et al 2008). This is consistent with published data that recombinant Rdi1 or overexpressed Rdi1 in yeast can extract Rho proteins from the plasma membrane or vacuole membrane (Eitzen et al 2001;Tcheperegine et al 2005;Tiedje et al 2008). Therefore, recycling through GDIs may, like endocytosis, play an important role in the establishment and maintenance of polarity.…”

Section: Polarization Of Cdc42 By Membrane Traffic In Budding Yeastsupporting

confidence: 79%

Membrane Organization and Dynamics in Cell Polarity

Orlando¹,

Guo²

2009

Cold Spring Harbor Perspectives in Biology

View full text Add to dashboard Cite

The establishment and maintenance of cell polarity is important to a wide range of biological processes ranging from chemotaxis to embryogenesis. An essential feature of cell polarity is the asymmetric organization of proteins and lipids in the plasma membrane. In this article, we discuss how polarity regulators such as small GTP-binding proteins and phospholipids spatially and kinetically control vesicular trafficking and membrane organization. Conversely, we discuss how membrane trafficking contributes to cell polarization through delivery of polarity determinants and regulators to the plasma membrane.

show abstract

Section: Polarization Of Cdc42 By Membrane Traffic In Budding Yeastsupporting

confidence: 79%

Membrane Organization and Dynamics in Cell Polarity

Orlando¹,

Guo²

2009

Cold Spring Harbor Perspectives in Biology

View full text Add to dashboard Cite

show abstract

“…Masuda et al (1994) show that high levels of RDI1 result in lethality, although the phenotype of these cells has not been characterized (Masuda et al, 1994). 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).…”

mentioning

confidence: 99%

“…In contrast, most ⌬lte1 cells arrested in anaphase with Cdc14-GFP trapped in the nucleolus ( Figure 2C). ⌬lte1 cells in which either RDI1 or the Cdc42 GAPs were deleted did not arrest in anaphase and released Cdc14 from the nucleolus with the same kinetics as wild-type cells ( Figure 2C).RDI1 overexpression has been reported to either result in lethality (Masuda et al, 1994) or produce slightly rounder cells (Tcheperegine et al, 2005). Therefore, we tested the consequences of higher RDI1 levels in our background.…”

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

“…Msb3p and Msb4p also physically bind Cdc42p, but in its GDP bound form. It has been suggested that this may maintain a pool of Cdc42p-GDP ready to be activated by Cdc24p (Tcheperegine et al, 2005). The exocyst component Sec15p also interacts with the Cdc42p GAP Bem1p, providing a further physical link between vesicle traffic and the establishment of polarity .…”

Section: Control Of Vesicle Trafficmentioning

confidence: 99%

“…Msb3p and Msb4p also physically interact with the polarisome component Spa2p providing a physical bridge between the polarisome and vesicle traffic (Fig. 2) (Tcheperegine et al, 2005). Msb3p and Msb4p also physically bind Cdc42p, but in its GDP bound form.…”

Section: Control Of Vesicle Trafficmentioning

confidence: 99%

Regulation of polarised growth in fungi

Sudbery

2008

Fungal Biology Reviews

View full text Add to dashboard Cite

Polarised growth in fungi occurs through the delivery of secretory vesicles along tracks formed by cytoskeletal elements to specific sites on the cell surface where they dock with a multiprotein structure called the exocyst before fusing with the plasmamembrane. The budding yeast, Saccharomyces cerevisiae has provided a useful model to investigate the mechanisms involved and their control. Cortical markers, provided by bud site selection pathways during budding, the septin ring during cytokinesis or the stimulation of the pheromone response receptors during mating, act through upstream signalling pathways to localise Cdc24, the GEF for the rho family GTPase, Cdc42. Cdc42 in its GTP-bound activates a multiprotein protein complex called the polarisome which nucleates actin cables along which the secretory vesicles are transported to the cell surface. Hyphae can elongate at a rate orders of magnitude faster than the extension of a yeast bud, so understanding hyphal growth will require substantial modification of the yeast paradigm.The rapid rate of hyphal growth is driven by a structure called the Spitzenkörper, located just behind the growing tip and which is rich in secretory vesicles. It is thought that secretory vesicles are delivered to the apical region where they accumulate in the Spitzenkörper. The Spitzenkörper then acts as vesicle supply centre in which vesicles exit the Spitzenkörper in all directions, but because of its proximity, the tip receives a greater concentration of vesicles per unit area than subapical regions. There are no obvious equivalents to the bud site selection pathway to provide a spatial landmark for polarised growth in hyphae. However, an emerging model is the way that the site of polarised growth in the fission yeast, Schizosaccharomyces pombe, is marked by delivery of the kelch repeat protein, Tea1, along microtubules. The relationship of the Spitzenkörper to the polarisome and the mechanisms that promote its formation are key questions that form the focus of current research.3

show abstract

Regulation of Cell Polarity by Interactions of Msb3 and Msb4 with Cdc42 and Polarisome Components

Cited by 65 publications

References 76 publications

Membrane Organization and Dynamics in Cell Polarity

Membrane Organization and Dynamics in Cell Polarity

The Rho GDI Rdi1 Regulates Rho GTPases by Distinct Mechanisms

Regulation of polarised growth in fungi

Contact Info

Product

Resources

About