Relevant bibliographies by topics / Regulation of Cdc42

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Academic literature on the topic 'Regulation of Cdc42'

Author: Grafiati
Published: 25 May 2024

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Journal articles on the topic "Regulation of Cdc42"

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Bassilana, Martine, Julie Hopkins, and Robert A. Arkowitz. "Regulation of the Cdc42/Cdc24 GTPase Module during Candida albicans Hyphal Growth." Eukaryotic Cell 4, no. 3 (March 2005): 588–603. http://dx.doi.org/10.1128/ec.4.3.588-603.2005.

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ABSTRACT The Rho G protein Cdc42 and its exchange factor Cdc24 are required for hyphal growth of the human fungal pathogen Candida albicans. Previously, we reported that strains ectopically expressing Cdc24 or Cdc42 are unable to form hyphae in response to serum. Here we investigated the role of these two proteins in hyphal growth, using quantitative real-time PCR to measure induction of hypha-specific genes together with time lapse microscopy. Expression of the hypha-specific genes examined depends on the cyclic AMP-dependent protein kinase A pathway culminating in the Efg1 and Tec1 transcription factors. We show that strains with reduced levels of CDC24 or CDC42 transcripts induce hypha-specific genes yet cannot maintain their expression in response to serum. Furthermore, in serum these mutants form elongated buds compared to the wild type and mutant budding cells, as observed by time lapse microscopy. Using Cdc24 fused to green fluorescent protein, we also show that Cdc24 is recruited to and persists at the germ tube tip during hyphal growth. Altogether these data demonstrate that the Cdc24/Cdc42 GTPase module is required for maintenance of hyphal growth. In addition, overexpression studies indicate that specific levels of Cdc24 and Cdc42 are important for invasive hyphal growth. In response to serum, CDC24 transcript levels increase transiently in a Tec1-dependent fashion, as do the G-protein RHO3 and the Rho1 GTPase activating protein BEM2 transcript levels. These results suggest that a positive feedback loop between Cdc24 and Tec1 contributes to an increase in active Cdc42 at the tip of the germ tube which is important for hypha formation.
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vandenBerg, Alysia L., Ashraf S. Ibrahim, John E. Edwards, Kurt A. Toenjes, and Douglas I. Johnson. "Cdc42p GTPase Regulates the Budded-to-Hyphal-Form Transition and Expression of Hypha-Specific Transcripts in Candida albicans." Eukaryotic Cell 3, no. 3 (June 2004): 724–34. http://dx.doi.org/10.1128/ec.3.3.724-734.2004.

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ABSTRACT The yeast Candida albicans is a major opportunistic pathogen of immunocompromised individuals. It can grow in several distinct morphological states, including budded and hyphal forms, and the ability to make the dynamic transition between these forms is strongly correlated with virulence. Recent studies implicating the Cdc42p GTPase in hypha formation relied on cdc42 mutations that affected the mitotic functions of the protein, thereby precluding any substantive conclusions about the specific role of Cdc42p in the budded-to-hypha-form transition and virulence. Therefore, we took advantage of several Saccharomyces cerevisiae cdc42 mutants that separated Cdc42p's mitotic functions away from its role in filamentous growth. The homologous cdc42-S26I, cdc42-E100G, and cdc42-S158T mutations in C. albicans Cdc42p caused a dramatic defect in the budded-to-hypha-form transition in response to various hypha-inducing signals without affecting normal budded growth, strongly supporting the conclusion that Cdc42p has an integral function in orchestrating the morphological transition in C. albicans. In addition, the cdc42-S26I and cdc42-E100G mutants demonstrated a reduced ability to damage endothelial cells, a process that is strongly correlated to virulence. The three mutants also had reduced expression of several hypha-specific genes, including those under the regulation of the Efg1p transcription factor. These data indicate that Cdc42p-dependent signaling pathways regulate the budded-to-hypha-form transition and the expression of hypha-specific genes.
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Höfken, Thomas, and Elmar Schiebel. "Novel regulation of mitotic exit by the Cdc42 effectors Gic1 and Gic2." Journal of Cell Biology 164, no. 2 (January 19, 2004): 219–31. http://dx.doi.org/10.1083/jcb.200309080.

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The guanine nucleotide exchange factor Cdc24, the GTPase Cdc42, and the Cdc42 effectors Cla4 and Ste20, two p21-activated kinases, form a signal transduction cascade that promotes mitotic exit in yeast. We performed a genetic screen to identify components of this pathway. Two related bud cortex–associated Cdc42 effectors, Gic1 and Gic2, were obtained as factors that promoted mitotic exit independently of Ste20. The mitotic exit function of Gic1 was dependent on its activation by Cdc42 and on the release of Gic1 from the bud cortex. Gic proteins became essential for mitotic exit when activation of the mitotic exit network through Cdc5 polo kinase and the bud cortex protein Lte1 was impaired. The mitotic exit defect of cdc5-10 Δlte1 Δgic1 Δgic2 cells was rescued by inactivation of the inhibiting Bfa1-Bub2 GTPase-activating protein. Moreover, Gic1 bound directly to Bub2 and prevented binding of the GTPase Tem1 to Bub2. We propose that in anaphase the Cdc42-regulated Gic proteins trigger mitotic exit by interfering with Bfa1-Bub2 GTPase-activating protein function.
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Zigmond, Sally H., Michael Joyce, Jane Borleis, Gary M. Bokoch, and Peter N. Devreotes. "Regulation of Actin Polymerization in Cell-free Systems by GTPγS and Cdc42." Journal of Cell Biology 138, no. 2 (July 28, 1997): 363–74. http://dx.doi.org/10.1083/jcb.138.2.363.

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We have established a cell-free system to investigate pathways that regulate actin polymerization. Addition of GTPγS to lysates of polymorphonuclear leukocytes (PMNs) or Dictyostelium discoideum amoeba induced formation of filamentous actin. The GTPγS appeared to act via a small G-protein, since it was active in lysates ofD. discoideum mutants missing either the α2- or β-subunit of the heterotrimeric G-protein required for chemoattractant-induced actin polymerization in living cells. Furthermore, recombinant Cdc42, but not Rho or Rac, induced polymerization in the cell-free system. The Cdc42-induced increase in filamentous actin required GTPγS binding and was inhibited by a fragment of the enzyme PAK1 that binds Cdc42. In a high speed supernatant, GTPγS alone was ineffective, but GTPγS-loaded Cdc42 induced actin polymerization, suggesting that the response was limited by guanine nucleotide exchange. Stimulating exchange by chelating magnesium, by adding acidic phospholipids, or by adding the exchange factors Cdc24 or Dbl restored the ability of GTPγS to induce polymerization. The stimulation of actin polymerization did not correlate with PIP2 synthesis.
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Gorfer, Markus, Mika T. Tarkka, Mubashir Hanif, Alejandro G. Pardo, Erja Laitiainen, and Marjatta Raudaskoski. "Characterization of Small GTPases Cdc42 and Rac and the Relationship Between Cdc42 and Actin Cytoskeleton in Vegetative and Ectomycorrhizal Hyphae of Suillus bovinus." Molecular Plant-Microbe Interactions® 14, no. 2 (February 2001): 135–44. http://dx.doi.org/10.1094/mpmi.2001.14.2.135.

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This work reports the isolation and molecular characterization of CDC42 and RAC1 cDNAs from the ectomycorrhiza forming filamentous homobasidiomycete Suillus bovinus. Previously, no RAC gene was described from filamentous fungi and no CDC42 gene was described from homobasidiomycetes. Southern hybridization with SbCDC42 and SbRAC1 cDNAs indicated that the S. bovinus genome contains only one CDC42 and one RAC1 gene. The predicted amino acid sequence of SbRac1p is 77% identical with the Rac1B protein of chick, whereas SbCdc42p is most identical with Schizosaccharomyces pombe Cdc42p, showing 88% identity. In the predicted amino acid sequences of SbRac1p and SbCdc42p, the five guanine nucleotide binding regions, switch I and II, and the effector domain are highly identical to those known in other small GTPases. These domain structures suggest that in S. bovinus, SbRac1p and SbCdc42p function as molecular switches regulating the organization of actin cytoskeleton, similar to yeasts and mammals. SbRAC1 and SbCDC42 were expressed in vegetative and ectomycorrhizal hyphae, and SbCdc42p was detected in ectomycorrhiza-forming hyphae if growth and differentiation of the symbiotic hyphae took place. Cdc42p and actin were localized at the tips of S. bovinus vegetative hyphae. Similar to yeast, in filamentous fungi Cdc42p may be necessary to maintain the actin cytoskeleton at hyphal tips, making the polarized growth of the hyphae possible. In developing ectomycorrhiza, Cdc42p and actin were visualized in association with plasma membrane in swollen cells typical to the symbiotic hyphae. The role of Cdc42p and actin in regulation of the growth pattern and morphogenesis of ectomycorrhizal hyphae is discussed.
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Herrington, Kari A., Andrew L. Trinh, Carolyn Dang, Ellen O’Shaughnessy, Klaus M. Hahn, Enrico Gratton, Michelle A. Digman, and Christine Sütterlin. "Spatial analysis of Cdc42 activity reveals a role for plasma membrane–associated Cdc42 in centrosome regulation." Molecular Biology of the Cell 28, no. 15 (July 15, 2017): 2135–45. http://dx.doi.org/10.1091/mbc.e16-09-0665.

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The ability of the small GTPase Cdc42 to regulate diverse cellular processes depends on tight spatial control of its activity. Cdc42 function is best understood at the plasma membrane (PM), where it regulates cytoskeletal organization and cell polarization. Active Cdc42 has also been detected at the Golgi, but its role and regulation at this organelle are only partially understood. Here we analyze the spatial distribution of Cdc42 activity by moni­toring the dynamics of the Cdc42 FLARE biosensor using the phasor approach to FLIM-FRET. Phasor analysis revealed that Cdc42 is active at all Golgi cisternae and that this activity is controlled by Tuba and ARHGAP10, two Golgi-associated Cdc42 regulators. To our surprise, FGD1, another Cdc42 GEF at the Golgi, was not required for Cdc42 regulation at the Golgi, although its depletion decreased Cdc42 activity at the PM. Similarly, changes in Golgi morphology did not affect Cdc42 activity at the Golgi but were associated with a substantial reduction in PM-associated Cdc42 activity. Of interest, cells with reduced Cdc42 activity at the PM displayed altered centrosome morphology, suggesting that centrosome regulation may be mediated by active Cdc42 at the PM. Our study describes a novel quantitative approach to determine Cdc42 activity at specific subcellular locations and reveals new regulatory principles and functions of this small GTPase.
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Rincón, Sergio A., Yanfang Ye, M. Antonia Villar-Tajadura, Beatriz Santos, Sophie G. Martin, and Pilar Pérez. "Pob1 Participates in the Cdc42 Regulation of Fission Yeast Actin Cytoskeleton." Molecular Biology of the Cell 20, no. 20 (October 15, 2009): 4390–99. http://dx.doi.org/10.1091/mbc.e09-03-0207.

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Rho GTPases regulate the actin cytoskeleton in all eukaryotes. Fission yeast Cdc42 is involved in actin cable assembly and formin For3 regulation. We isolated cdc42-879 as a thermosensitive strain with actin cable and For3 localization defects. In a multicopy suppressor screening, we identified pob1+as suppressor of cdc42-879 thermosensitivity. Pob1 overexpression also partially restores actin cables and localization of For3 in the mutant strain. Pob1 interacts with Cdc42 and this GTPase regulates Pob1 localization and/or stability. The C-terminal pleckstrin homology (PH) domain of Pob1 is required for Cdc42 binding. Pob1 also binds to For3 through its N-terminal sterile alpha motif (SAM) domain and contributes to the formin localization at the cell tips. The previously described pob1-664 mutant strain (Mol. Biol. Cell. 10, 2745–2757, 1999), which carries a mutation in the PH domain, as well as pob1 mutant strains in which Pob1 lacks the N-terminal region (pob1ΔN) or the SAM domain (pob1ΔSAM), have cytoskeletal defects similar to that of cdc42-879 cells. Expression of constitutively active For3DAD* partially restores actin organization in cdc42-879, pob1-664, pob1ΔN, and pob1ΔSAM. Therefore, we propose that Pob1 is required for For3 localization to the tips and facilitates Cdc42-mediated relief of For3 autoinhibition to stimulate actin cable formation.
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Oceguera-Yanez, Fabian, Kazuhiro Kimura, Shingo Yasuda, Chiharu Higashida, Toshio Kitamura, Yasushi Hiraoka, Tokuko Haraguchi, and Shuh Narumiya. "Ect2 and MgcRacGAP regulate the activation and function of Cdc42 in mitosis." Journal of Cell Biology 168, no. 2 (January 10, 2005): 221–32. http://dx.doi.org/10.1083/jcb.200408085.

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Although Rho regulates cytokinesis, little was known about the functions in mitosis of Cdc42 and Rac. We recently suggested that Cdc42 works in metaphase by regulating bi-orient attachment of spindle microtubules to kinetochores. We now confirm the role of Cdc42 by RNA interference and identify the mechanisms for activation and down-regulation of Cdc42. Using a pull-down assay, we found that the level of GTP-Cdc42 elevates in metaphase, whereas the level of GTP-Rac does not change significantly in mitosis. Overexpression of dominant-negative mutants of Ect2 and MgcRacGAP, a Rho GTPase guanine nucleotide exchange factor and GTPase activating protein, respectively, or depletion of Ect2 by RNA interference suppresses this change of GTP-Cdc42 in mitosis. Depletion of Ect2 also impairs microtubule attachment to kinetochores and causes prometaphase delay and abnormal chromosomal segregation, as does depletion of Cdc42 or expression of the Ect2 and MgcRacGAP mutants. These results suggest that Ect2 and MgcRacGAP regulate the activation and function of Cdc42 in mitosis.
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Shitara, Akiko, Lenka Malec, Seham Ebrahim, Desu Chen, Christopher Bleck, Matthew P. Hoffman, and Roberto Weigert. "Cdc42 negatively regulates endocytosis during apical membrane maintenance in live animals." Molecular Biology of the Cell 30, no. 3 (February 2019): 324–32. http://dx.doi.org/10.1091/mbc.e18-10-0615.

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Lumen establishment and maintenance are fundamental for tubular organs physiological functions. Most of the studies investigating the mechanisms regulating this process have been carried out in cell cultures or in smaller organisms, whereas little has been done in mammalian model systems in vivo. Here we used the salivary glands of live mice to examine the role of the small GTPase Cdc42 in the regulation of the homeostasis of the intercellular canaliculi, a specialized apical domain of the acinar cells, where protein and fluid secretion occur. Depletion of Cdc42 in adult mice induced a significant expansion of the apical canaliculi, whereas depletion at late embryonic stages resulted in a complete inhibition of their postnatal formation. In addition, intravital subcellular microscopy revealed that reduced levels of Cdc42 affected membrane trafficking from and toward the plasma membrane, highlighting a novel role for Cdc42 in membrane remodeling through the negative regulation of selected endocytic pathways.
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Bruurs, Lucas J. M., Lisa Donker, Susan Zwakenberg, Fried J. Zwartkruis, Harry Begthel, A. S. Knisely, George Posthuma, Stan F. J. van de Graaf, Coen C. Paulusma, and Johannes L. Bos. "ATP8B1-mediated spatial organization of Cdc42 signaling maintains singularity during enterocyte polarization." Journal of Cell Biology 210, no. 7 (September 28, 2015): 1055–63. http://dx.doi.org/10.1083/jcb.201505118.

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During yeast cell polarization localization of the small GTPase, cell division control protein 42 homologue (Cdc42) is clustered to ensure the formation of a single bud. Here we show that the disease-associated flippase ATPase class I type 8b member 1 (ATP8B1) enables Cdc42 clustering during enterocyte polarization. Loss of this regulation results in increased apical membrane size with scattered apical recycling endosomes and permits the formation of more than one apical domain, resembling the singularity defect observed in yeast. Mechanistically, we show that to become apically clustered, Cdc42 requires the interaction between its polybasic region and negatively charged membrane lipids provided by ATP8B1. Disturbing this interaction, either by ATP8B1 depletion or by introduction of a Cdc42 mutant defective in lipid binding, increases Cdc42 mobility and results in apical membrane enlargement. Re-establishing Cdc42 clustering, by tethering it to the apical membrane or lowering its diffusion, restores normal apical membrane size in ATP8B1-depleted cells. We therefore conclude that singularity regulation by Cdc42 is conserved between yeast and human and that this regulation is required to maintain healthy tissue architecture.
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Dissertations / Theses on the topic "Regulation of Cdc42"

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Ravichandran, Yamini. "Cdc42 isoforms : localization, functions and regulation." Electronic Thesis or Diss., Sorbonne université, 2020. http://www.theses.fr/2020SORUS405.

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Les mutations sont responsables de diverses pathologies du développement, en particulier chez les patients atteints de maladies rares ou pour lesquels il n’y a pas de diagnostic clinique clair. Cdc42 est une protéine clé pour la polarité cellulaire, une étape cruciale de nombreux processus cellulaires, comme la migration cellulaire, la division cellulaire ou la réponse immunitaire. Les mutations de Cdc42 entrainent une variété de pathologies, par exemple des dérégulations de la croissance ou de la morphologie faciale ainsi que des anomalies immunologiques, hématologiques et du développement neuronal. Les fonctions de Cdc42 reposent en grande partie sur la localisation de cette protéine dans la cellule. La comparaison des différentes formes de Cdc42 et de certaines formes mutantes montrent que les derniers acides aminés de la protéine jouent un rôle clé dans sa localisation et donc dans sa fonction. Nous avons centré notre étude sur l’identification : 1) des acides aminés essentiels à la localisation de la protéine ; et 2) de nouveaux mécanismes de régulation de Cdc42 responsables de sa localisation intracellulaire. Nous avons aussi montré que les deux isoformes jouent des rôles différents au cours de la migration cellulaire. Ce travail devrait nous permettre de mieux comprendre les pathologies liées aux mutations de Cdc42
Mutations in proteins cause diverse developmental disorders, particularly for individuals with rare diseases or for whom a unifying clinical diagnosis is unknown. Cdc42 is one such protein; vital for establishing cell polarity, a crucial step in many biological processes such as cell migration, division and immune responses. Not surprisingly, mutations in Cdc42 cause a range of diseases such as growth dysregulation, facial dysmorphism and neurodevelopmental, immunological, and hematological abnormalities. In vertebrates there are two isoforms of Cdc42. The first being the ubiquitous isoform, has almost exclusively been studied and the role of the second isoform, being the brain isoform, is largely unknown. We have shown that the two isoforms are localized differently in cells. The ubiquitous isoform is mostly found in the cell cytoplasm and at the plasma membrane, while the Brain isoform localizes at the Golgi apparatus and on intracellular vesicles. We have also shown that the two isoforms carry out different functions during cell migration, suggesting that the differences between these two isoforms which only differs by the last 10 amino acids are responsible for their distinct localisation and function. Interestingly, a mutation in the C-ter sequence of Cdc42 ubiquitous isoform alters Cdc42 localisation and causes a generalized pustular psoriasis disease. Two main objectives have been studied in this project 1) the impact of the last amino acids of the protein in Cdc42 localization; and 2) new regulatory mechanisms of Cdc42 responsible for its intracellular localization. These findings will bring a better understanding of pathologies related to Cdc42 mutations
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Lu, Ruifeng, and Jean M. Wilson. "Rab14 specifies the apical membrane through Arf6-mediated regulation of lipid domains and Cdc42." NATURE PUBLISHING GROUP, 2016. http://hdl.handle.net/10150/622499.

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The generation of cell polarity is essential for the development of multi-cellular organisms as well as for the function of epithelial organs in the mature animal. Small GTPases regulate the establishment and maintenance of polarity through effects on cytoskeleton, membrane trafficking, and signaling. Using short-term 3-dimensional culture of MDCK cells, we find that the small GTPase Rab14 is required for apical membrane specification. Rab14 knockdown results in disruption of polarized lipid domains and failure of the Par/aPKC/Cdc42 polarity complex to localize to the apical membrane. These effects are mediated through tight control of lipid localization, as overexpression of the phosphatidylinositol 4-phosphate 5-kinase a [PtdIns(4) P5K] activator Arf6 or PtdIns(4) P5K alone, or treatment with the phosphatidylinositol 3-kinase (PtdInsI3K) inhibitor wortmannin, rescued the multiple-apical domain phenotype observed after Rab14 knockdown. Rab14 also co-immunoprecipitates and colocalizes with the small GTPase Cdc42, and Rab14 knockdown results in increased Cdc42 activity. Furthermore, Rab14 regulates trafficking of vesicles to the apical domain, mitotic spindle orientation, and midbody position, consistent with Rab14' s reported localization to the midbody as well as its effects upon Cdc42. These results position Rab14 at the top of a molecular cascade that regulates the establishment of cell polarity.
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Murali, Arun [Verfasser]. "Role of XIAP in ubiquitin mediated regulation of Cdc42 and other Rho GTPases / Arun Murali." Mainz : Universitätsbibliothek Mainz, 2019. http://d-nb.info/1191286649/34.

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Francis, Monika K. "Regulation of GRAF1 membrane sculpting function during cell movement." Doctoral thesis, Umeå universitet, Institutionen för medicinsk kemi och biofysik, 2015. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-111213.

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All eukaryotic cells rely on endocytic events to satisfy a constant need for nutrient and fluid uptake from their surroundings. Endocytosis-dependent turnover of cell surface constituents also serves to control signal transduction and establish morphological changes in response to extracellular stimuli. During endocytosis, distinct protein machineries re-sculpt the plasma membrane into vesicular carriers that enclose molecules that are to be taken up into the cell. Besides those produced from the canonical clathrin-mediated endocytic machinery, it is becoming increasingly clear that other membrane carriers exist. The indisputable connection between the function of these uptake systems and various disease states, highlights why it is so important to increase our knowledge about the underlying molecular machineries. The aim of this thesis was therefore to characterise the function of GRAF1, a protein suggested to be a tumour suppressor due to that the gene has been found to be mutated in certain cancer patients. My work focused on understanding how this protein operates during formation of clathrin-independent carriers, with possible implications for disease development. Previous in vitro studies showed that GRAF1 harbours a GTPase activating domain to inactivate Rho GTPase Cdc42, a major actin cytoskeleton regulator. Herein, microscopy based approaches used to analyse HeLa cells demonstrated the importance of a transient interaction between GRAF1 and Cdc42 for proper processing of GRAF1-decorated carriers. Although GRAF1-mediated inactivation of Cdc42 was not vital for the budding of carriers from the plasma membrane, it was important for carrier maturation. In addition, studies of purified GRAF1 and its association with lipid bilayers identified a membrane scaffolding-dependent oligomerisation mechanism, with the ability to sculpt membranes. This was consistent with the assumption that GRAF1 possesses an inherent banana shaped membrane binding domain. Remarkably, this function was autoinhibited and in direct competition with the Cdc42 interaction domain. Finally, other novel GRAF1 interaction partners were identified in this study. Interestingly, many of these partners are known to be associated with protein complexes involved in cell adherence, spreading and migration. Although never actually seen localising to mature focal adhesions that anchor cells to their growth surface, dynamic GRAF1 carriers were captured travelling to and from such locations. Moreover, GRAF1 was recruited specifically to smaller podosome-like structures. Consistent with this, the tracking of GRAF1 in live cells uncovered a clear pattern of dynamic carrier formation at sites of active membrane turnover – notably protrusions at the cell periphery. Furthermore, the silencing of GRAF1 gave rise to cells defective in spreading and migration, indicating a targeting of GRAF1-mediated endocytosis to aid in rapid plasma membrane turnover needed for morphological changes that are a prerequisite for cell movement. Since these cells exhibited an increase in active Rab8, a GTPase responsible for polarised vesicle transport, the phenotype could also be explained by a defect in Rab8 trafficking that results in hyperpolarisation. Taken together, the spatial and temporal regulation of GRAF1 membrane sculpting function is likely to be accomplished via its membrane binding propensity, in concert with various protein interactions. The importance of GRAF1 in aiding membrane turnover during cell movement spans different functional levels – from its local coordination of membrane and actin dynamics by interacting with Cdc42, to its global role in membrane lipid trafficking.
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Mutavchiev, Delyan Rumenov. "Regulation of fission yeast cell polarity by stress-response pathways." Thesis, University of Edinburgh, 2017. http://hdl.handle.net/1842/29006.

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Cell polarisation is a key biological process crucial for the functioning of essentially all cells. Regulation of cell polarity is achieved through various processes determined by both internal and external factors. An example of the latter is that cell polarity can be disrupted or lost as a consequence of a variety of external stresses. When facing such stresses, cells adapt to unfavourable conditions by activating a range of molecular signalling pathways, collectively termed ‘stress response’. Despite the connections between external stress and cell polarity, whether stress-response signalling regulates cell polarisation and what the molecular basis for such regulation remains an open question. The fission yeast Schizosaccharomyces pombe presents an excellent biological platform to study the complexity of cell polarity regulation on a systematic level. This study is aimed at understanding the functional relationship between stress-response signalling and maintenance of cell polarity in this model organism. The findings presented in this thesis set the basis for establishing a functional link between the activation of the S.pombe stress-response pathway and the activity of the master regulator of cell polarity- the Rho GTPase Cdc42. Here, I describe experiments that identify an active involvement of the stress-response mitogen-activated kinase (MAPK) Sty1 in the dispersal of active Cdc42 from the sites of growth. This new role for Sty1 occurs independently from its involvement in transcription regulation and other previously identified signalling pathways involving Sty1. Furthermore, I also find that Sty1’s involvement in Cdc42 regulation has direct implications for fission yeast physiology as it is essential for the maintenance of cellular quiescence upon nitrogen starvation. This thesis also focuses on identifying the targets of Sty1 orchestrating the active Cdc42 disruption. Here, I describe a candidate-based approach, where I investigate the role of proteins from the Cdc42 regulatory network during Sty1 activation. Additionally, I present a global phospho-proteomics approach to identify novel targets of Sty1 and offer preliminary findings which might explain Sty1’s involvement in Cdc42 regulation.
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Langer, Torben [Verfasser]. "Der Einfluss des Tumorsuppressorproteins Merlin auf die Regulation der beiden Rho-GTPasen Rac2 und Cdc42 / Torben Langer." Ulm : Universität Ulm. Medizinische Fakultät, 2013. http://d-nb.info/1036215121/34.

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Ye, Xiangcang. "Role of a CDC42 homologous gene in the regulation of cell polarity and morphogenic transitions in Wangiella dermatitidis /." Digital version accessible at:, 1998. http://wwwlib.umi.com/cr/utexas/main.

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Primeau, Martin. "Novel mechanisms of regulation of the Cdc42 GTPase- activating protein CdGAP/ARHGAP31, a protein involved in cell migration and adhesion." Thesis, McGill University, 2011. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=96901.

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The Rho GTPases form a family of enzymes that control numerous cellular processes including cell migration and proliferation through effects on the cytoskeleton, membrane trafficking and cell adhesion. The activity of these molecular switches is modulated by GTPase-activating proteins (GAPs), a group of negative-regulators which includes Cdc42-GTPase-Activating Protein (CdGAP). This protein specifically negatively-regulates the Rho GTPases Cdc42 and Rac1. In this study, we show that CdGAP is regulated by lipid-, protein- and intramolecular-interactions. First, we demonstrate that a polybasic region (PBR) of CdGAP preceding the GAP domain and found in numerous Rho family GAPs is required for CdGAP specific association with phosphatidilinositol-3,4,5-trisphosphate (PI(3,4,5)P3). We show that the binding of PI(3,4,5)P3 is required for CdGAP-mediated GAP activity in vitro, and that an intact PBR is required for its CdGAP-mediated GAP activity in vivo. Second, we characterize the binding site for the negative-regulator of CdGAP Intersectin-1 located in the Basic-Rich (BR) domain of CdGAP. We present evidence that this interaction mediated by the SH3D domain of Intersectin requires one to three lysine residues located in the Basic-Rich (BR) domain of CdGAP. Thirdly, we show that CdGAP is negatively-regulated by its C-terminal domain. This observation is part of a study that links two human CdGAP gene mutations to a syndrome which presents a combination of aplasia cutis congenita (ACC) and terminal transverse limb defects (TTLD). In this syndrome, the deletion-mutant gene products which lack the residual amino-acid of CdGAP at its C-terminus have an increased activity compared to wild-type proteins. We show that this C-terminus can bind to the GAP domain of CdGAP, providing a model to explain how the absence of the C-terminus induces this syndrome. In summary, this work provides novel insight into understanding the mechanisms of regulation of CdGAP, a protein involved in cell migration and adhesion with unexpected roles related to human diseases.
Les Rho GTPases forment une famille d'enzymes qui contrôlent de nombreux processus cellulaires, tels que la migration cellulaire et la prolifération, grâce à leurs effets sur le cytosquelette, le trafic membranaire et l'adhésion cellulaire. L'activité de ces interrupteurs moléculaires est modulée par les protéines activatrices de GTPases (GAPs), un groupe de régulateurs négatifs qui inclu CdGAP (Cdc42-GTPase activating protein). Cette protéine régule négativement les Rho GTPases Cdc42 et Rac1 de façon spécifique. Dans la présente étude, nous montrons que CdGAP est régulée par des interactions lipidiques, protéiques et intramoléculaire. Premièrement, nous démontrons qu'une région polybasique (PBR), précédant le domaine GAP et retrouvée dans plusieurs GAP de la famille Rho, est requise pour l'association spécifique de CdGAP avec le phosphatidilinositol-3,4,5-trisphosphate (PI(3,4,5)P3). Nos résultats suggèrent que l'activation des GAP requiert la liaison du PI(3,4,5)P3 à CdGAP dans un contexte in vitro et un PBR intact pour que CdGAP provoque ses effets GAP-dépendants dans un contexte in vivo. Deuxièmement, nous caractérisons le site de liaison du régulateur négatif de CdGAP Intersectin-1. Ce site est localisé dans le domaine riche en résidus basiques (BR) de CdGAP. Nous suggérons que cette interaction, médiée par le domaine SH3D d'Intersectin, requiert de un à trois résidus lysine dans le domaine BR de CdGAP. Troisièmement, nous montrons que CdGAP est régulé de manière négative par son propre domaine C-terminal. Cette observation fait partie d'une étude qui associe deux mutations humaines du gène CdGAP à un syndrôme présentant une combinaison d'aplasie cutis congenita (ACC) et de malformation des doigts et des orteils (TTLD). Les gènes mutants produisent des protéines tronquées qui ont une activité GAP supérieure à la protéine de type sauvage. Nous montrons que ce C-terminal peut lier le domaine GAP de CdGAP, supportant un modèle expliquant comment l'absence du C-terminal induit ce syndrome. En bref, ce travail présente un nouvel aperçu des mécanismes de régulation de CdGAP, une protéine impliquée dans la migration cellulaire et dans l'adhésion des cellules en plus d'être directement impliquée dans une maladie humaine.
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Ofo, Enyinnaya. "Flourescent biosensor-based, Cdc42 activity imaging for understanding the regulation of Epidermal Growth Receptor (EGFR) signalling in head and neck cancer." Thesis, King's College London (University of London), 2012. https://kclpure.kcl.ac.uk/portal/en/theses/flourescent-biosensorbased-cdc42-activity-imaging-for-understanding-the-regulation-of-epidermal-growth-receptor-egfr-signalling-in-head-and-neck-cancer(32081fef-10f1-4a3e-ac33-67afbbf78376).html.

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The Epidermal Growth Factor Receptor (EGFR) is overexpressed in several solid tumours including squamous cell carcinoma of the head & neck (SCCHN). Drugs that directly block the action of EGFR are currently available. However, a major unanswered question is; how best to select patients most likely to respond to these new treatments, as the response rate to EGFR-targeted mono-therapy in SCCHN, as well as other solid tumours, such as lung and colorectal cancer, is very low. Resistance to EGFR therapy may stem from aberrant receptor trafficking. Cdc42 is known to affect EGFR downregulation by sequestering c-Cbl, preventing it from catalyzing receptor ubiquitination. The aim of this project is to determine the role of Cdc42 in mediating cancer cell response to EGFR and ErbB-family targeted therapy. Using optical imaging techniques such as, Fluorescence Resonance Energy Transfer (FRET) and Fluorescence Lifetime Imaging Microscopy (FUM) I have analysed Cdc42 activity in Squamous Carcinoma Cell Lines after EGFR tyrosine kinase inhibitor (TKI) treatment, using the FRET biosensor Raichu-Cdc42. I have demonstrated that conversely, Raichu-Cdc42, and consequently endogenous Cdc42 activity increases significantly following EGFR TKI treatment. Further investigation revealed that the serine/threonine kinase, c-Jun NH2 Terminal Kinase 1 (JNK1) may modulate Cdc42 activity via a negative feedback mechanism, and JNK1 in turn regulates EGFR ubiquitination and downregulation. I have also demonstrated for the first time protein-protein interactions in pathological SCCHN tissue between members of the ErbB receptor family (EGFR and HER2) and between PKCa and Ezrin, using FRET and FUM. The novel results from this thesis provides further knowledge on factors influencing EGFR downregulation in SCCHN, that could account for the resistance to EGFR targeted therapies observed in a clinical setting. In addition the optical proteomic assays could be translated into new diagnostic/predictive tests, potentially allowing us to improve the outcome for head and neck cancer patients.
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Bretou, Marine. "Regulation of the dynamics of the fusion pore : importance of the SNARE protein synaptobrevin 2 and of the Rho GTPase Cdc42." Paris 7, 2010. http://www.theses.fr/2010PA077157.

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L'exocytose nécessite la formation d'un pore de fusion. Le pore initial est étroit ; seules de petites molécules sont libérées. Quand le pore s'élargit les macromolécules sont libérées. J'ai étudié le rôle de deux protéines sur la dilatation du pore: la protéine SNARE synaptobrévine 2 (Syb2), et la Rhô GTPase Cdc42. L'assemblage des SNAREs fournirait l'énergie nécessaire à la fusion. L'insertion d'un espacer dans le domaine juxtamembranaire de Syb2 ne modifie pas la fréquence des événements d'exocytose détectés par ampérométrie à 1|jM [Ca2+], mais empêche l'apparition d'une composante de sécrétion à de plus fortes [Ca2+]. Les événements peuvent être classés en deux groupes, liés à la vitesse et au degré de dilatation des pores; l'allongement de Syb2 réduit la population de pics rapides, mais n'affecte pas celle des pics lents. Les événements lents seraient dus à un assemblage partiel des SNAREs, alors que ceux dits rapides résulteraient d'un assemblage plus serré, assurant ainsi une dilatation rapide du pore. Cdc42 contrôle la dynamique de l'actine. Diminuer son expression dans les cellules BON réduit le nombre de granules fusionnant complètement avec la membrane, mais n'affecte pas leur recrutement et leur liaison à la membrane. Réduire l'expression de Cdc42 diminue le nombre de hauts pics dus à une dilatation rapide et complète des pores, et augmente le nombre de pieds seuls, dus à des pores ne s'élargissant pas. L'augmentation de tension de la membrane corrige les effets dus à l'absence de Cdc42 ; sa diminution par dépolymérisation de l'actine imite les effets obtenus en son absence. Cdc42 contrôlerait la dilatation du pore en modulant la tension de membrane
Exocytosis ends with the formation of a fusion pore. The initial pore is narrow, only small molecules flow through it. The pore then enlarges, releasing larger secretory products. I studied the role of two proteins on the dilation of the pore: the SNARE protein synaptobrevin 2 (Syb2), and the Rho GTPase Cdc42. Zippering of SNAREs in opposed membranes might give energy to catalyze fusion. Inserting a linker between the SNARE core and the transmembrane domain of Syb2 did not modify the frequency of exocytotic events detected by amperometry at 1|jM free [Ca2+] but prevented the occurrence of an extra component of release at higher [Ca2+]. Analysis of these events led to their classification into two groups, due to the rate and extent of dilation of the pore; lengthening Syb2 reduced the population of fast spikes, leaving the slow one unchanged. Slow fusion events might be due to a partial zippering of the SNAREpin while fast fusion events require a tight one, i. E. A short intermembrane distance to assure rapid dilation of the pore. Cdc42 controls actin dynamics. TIRFM experiments showed that its silencing in BON cells reduced the number of granules undergoing full fusion, with little effect on their recruitment and docking at the membrane. Using amperometry, we showed that this silencing reduced the number of high spikes due to fast and complete dilation of the pore, and increased stand-alone foot signals reflecting pores failing to enlarge. Increasing membrane tension rescued the effects of silencing while decreasing it through actin depolymerization mimicked Cdc42 silencing. Cdc42 might control fusion pore dilation by modulating membrane tension
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Book chapters on the topic "Regulation of Cdc42"

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Hart, M. J., D. Leonard, Y. Zheng, K. Shinjo, T. Evans, and R. A. Cerione. "The Mammalian Homolog of the Yeast Cell-Division-Cycle Protein, CDC42: Evidence for the Involvement of a Rho-Subtype GTPase in Cell Growth Regulation." In GTPases in Biology I, 579–95. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-78267-1_37.

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Draetta, Giulio. "Biochemical Regulation of the CDC2 Protein Kinase." In Cellular Regulation by Protein Phosphorylation, 363–73. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-75142-4_46.

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Nigg, E. A., W. Krek, and P. Gallant. "Regulation of the Mitotic CDC2 Protein Kinase." In DNA Replication and the Cell Cycle, 147–55. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-77040-1_11.

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Marcote, M. Jesús, Michele Pagano, and Giulio Draetta. "Cdc2 Protein Kinase: Structure-Function Relationships." In Ciba Foundation Symposium 170 - Regulation of the Eukaryotic Cell Cycle, 30–49. Chichester, UK: John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470514320.ch4.

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Berry, Lynne D., and Kathleen L. Gould. "Regulation of Cdc2 activity by phosphorylation at T14/Y15." In Progress in Cell Cycle Research, 99–105. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4615-5873-6_10.

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Lehner, Christian F., Gabriele Ried, Bodo Stern, and Jürgen A. Knoblich. "Cyclins and Cdc2 Kinases in Drosophila: Genetic Analyses in a Higher Eukaryote." In Ciba Foundation Symposium 170 - Regulation of the Eukaryotic Cell Cycle, 97–114. Chichester, UK: John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470514320.ch7.

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Kishimoto, Takeo, and Eiichi Okumura. "In vivo regulation of the entry into M-phase: initial activation and nuclear translocation of cyclin B/Cdc2." In Progress in Cell Cycle Research, 241–49. Boston, MA: Springer US, 1997. http://dx.doi.org/10.1007/978-1-4615-5371-7_19.

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Knapp, Stefan. "3D Structure and Physiological Regulation of PAKs." In Paks, Rac/Cdc42 (p21)-activated Kinases, 137–48. Elsevier, 2013. http://dx.doi.org/10.1016/b978-0-12-407198-8.00008-4.

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Gorski, Jerome L. "FGD1 and Faciogenital Dysplasia (Aarskog–Scott Syndrome)." In Inborn Errors Of Development, 1289–98. Oxford University PressNew York, NY, 2008. http://dx.doi.org/10.1093/oso/9780195306910.003.0145.

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Abstract FGD1 mutations result in faciogenital dysplasia (FGDY; Aarskog–Scott syndrome), an X-linked recessive multiple congenital anomaly syndrome. Skeletal anomalies dominate the FGDY phenotype. Cardinal clinical features include a characteristic set of craniofacial and skeletal anomalies, disproportionate acromelic short stature, delayed skeletal maturation, and urogenital malformations. FGD1 encodes a guanine nucleotide exchange factor (GEF) that speci’cally activates Cdc42, a Rho guanosine triphosphatase (GTPase) that is involved in cell signaling and the regulation of the actin cytoskeleton, vesicular transport, and gene expression. The FGD1 protein is composed of multiple signaling motifs including a Src homology 3–binding domain, a GEF domain, a zinc-’nger FYVE domain, and two pleckstrin homology (PH) domains. By activating Cdc42, FGD1 stimulates cells to reorganize their actin cytoskeleton and form ‘lopodia, cytoskeletal elements involved in cellular signaling, adhesion, and migration. Through Cdc42, FGD1 also activates the c-Jun N-terminal kinase (JNK) signaling cascade, a pathway that regulates cell growth, apoptosis, and cellular differentiation.
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Pines, Jonathon, and Tony Hunter. "Cyclin-dependent kinases: an entbarrassntent of riches?" In Cell Cycle Control, 144–76. Oxford University PressOxford, 1995. http://dx.doi.org/10.1093/oso/9780199634118.003.0006.

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Abstract One of the most exciting advances in our understanding of the cell cycle has been the identification in multicellular organisms of a family of protein kinases that are involved in the regulation of different checkpoints. These protein kinases are related both in their primary structure, and because they bind and are activated by the cyclin family of proteins. The latter property has led to this family of protein kinases being called the ‘cyclin-dependent kinases’, or cdks. The cyclins are a family of structurally related proteins that typically vary in amount during the cell cycle in a programmed manner (the cyclins are reviewed in Chapter 5). The first two cyclins to be isolated, cyclins A and B, were called mitotic cyclins, because they were specifically destroyed in mitosis, implicating them in the regulation of the G2/M transition. Subsequently, another class of cyclins was discovered in yeast that have roles in the Gl/S transition, and are called Gl cyclins. More than ten different cyclins have been identified in humans and in budding yeast, and the different cyclin/cdk complexes are involved in regulating several different check –points throughout the cell cycle. Furthermore, it now appears that some cyclin –cdk complexes regulate processes quite separate from the cell cycle. The paradigm for the cyclin-cdk interaction is that between cdc2 and cyclin B (reviewed in Chapter 5). Therefore, in this article we will only outline the salient points.
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Conference papers on the topic "Regulation of Cdc42"

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Soliman, Mario, Chunhua Song, Jonathon L. Payne, Zheng Ge, Chandrika Gowda, Yali Ding, Kimberly J. Payne, and Sinisa Dovat. "Abstract 1512: Regulation of the CDC42 signaling pathway by IKZF1 in T-cell acute lymphoblastic leukemia." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-1512.

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Nandy, Sushmita B., Alexis Orozco, Gautham Prabhakar, Viktoria Stewart, Stephanie Jones, Paloma Munoz, Ramadevi Subramani, Diego Pedroza, and Rajkumar Lakshmanaswamy. "Abstract 1461: miR-424-cdc42, key signaling axis in hyperglycemic regulation of stemness in triple negative breast cancer." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-1461.

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Li, G., S. S. Nair, S. J. Lees, and F. W. Booth. "Regulation of G2/M Transition in Mammalian Cells by Oxidative Stress." In ASME 2005 International Mechanical Engineering Congress and Exposition. ASMEDC, 2005. http://dx.doi.org/10.1115/imece2005-82349.

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The regulation of the G2/M transition for the mammalian cell cycle has been modeled using 19 states to investigate the G2 checkpoint dynamics in response to oxidative stress. A detailed network model of G2/M regulation is presented and then a “core” subsystem is extracted from the full network. An existing model of Mitosis control is extended by adding two important pathways regulating G2/M transition in response to DNA damage induced by oxidative stress. Model predictions indicate that the p53 dependent pathway is not required for initial G2 arrest as the Chk1/Cdc25C pathway can arrest the cell in G2 right after DNA damage. However, p53 and p21 expression is important for a more sustained G2 arrest by inhibiting the Thr161 phosphorylation by CAK. By eliminating the phosphorylation effect of Chk1 on p53, two completely independent pathways are obtained and it is shown that it does not affect the G2 arrest much. So the p53/p21 pathway makes an important, independent contribution to G2 arrest in response to oxidative stress, and any defect in this pathway may lead to genomic instability and predisposition to cancer. Such strict control mechanisms probably provide protection for survival in the face of various environmental changes. The controversial issue related to the mechanism of inactivation of Cdc2 by p21 is addressed and simulation predictions indicate that G2 arrest would not be affected much by considering the direct binding of p21 to Cdc2/Cyclin B given that the inhibition of CAK by p21 is already present if the binding efficiency is within a certain range. Lastly, we show that the G2 arrest time in response to oxidative stress is sensitive to the p53 synthesis rate.
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Zhang, Xiao, and Nan Gao. "Abstract 918: Cdc42 is crucial for intestinal stem cells survival by regulating Wnt and YAP signaling." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-918.

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Zhang, Wenwu, Rong Zhao, and Susan J. Gunst. "RhoA Regulates N-WASp And Arp2/3 Mediated Actin Polymerization And Airway Smooth Muscle (ASM) Contraction By Regulating The Activation Of Cdc42 And P21-activated Kinase (PAK)." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a5303.

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Reports on the topic "Regulation of Cdc42"

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Irazoqui, Javier E. Regulation of Cdc42/Rac Signaling in the Establishment of Cell Polarity and Control of Cell Motility. Fort Belvoir, VA: Defense Technical Information Center, August 2004. http://dx.doi.org/10.21236/ada434009.

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Irazoqui, Javier E., and Daniel J. Lew. Regulation of Cdc42/Rac Signaling in the Establishment of Cell Polarity and Control of Cell Motility. Fort Belvoir, VA: Defense Technical Information Center, August 2002. http://dx.doi.org/10.21236/ada410349.

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Irazoqui, Javier E. Regulation of Cdc42/Rac Signaling in the Establishment of Cell Polarity and Control of Cell Motility. Fort Belvoir, VA: Defense Technical Information Center, August 2003. http://dx.doi.org/10.21236/ada420886.

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4

Delmer, Deborah P., Douglas Johnson, and Alex Levine. The Role of Small Signal Transducing Gtpases in the Regulation of Cell Wall Deposition Patterns in Plants. United States Department of Agriculture, August 1995. http://dx.doi.org/10.32747/1995.7570571.bard.

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The combined research of the groups of Delmer, Levine and Johnson has led to a number of interesting findings with respect to the function of the small GTPase Rac in plants and also opened up new leads for future research. The results have shown: 1) The Rac13 protein undergoes geranylgeranlyation and is also translocated to the plasma membrane as found for Rac in mammals; 2) When cotton Rac13 is highly- expressed in yeast, it leads to an aberrant phenotype reminiscent of mutants impaired in actin function, supporting a role for Rac13 in cytoskeletal organization; 3) From our searches, there is no strong evidence that plants contain homologs of the related CDC42 genes found in yeast and mammals; 4) We have identified a rather unique Rac gene in Arabidopsis that has unusual extensions at both the N- and C-terminal portions of the protein; 5) New evidence was obtained that an oxidative burst characterized by substantial and sustained production of H202 occurs coincident with the onset of secondary wall synthesis in cotton fibers. Further work indicates that the H202 produced may be a signal for the onset of this phase of development and also strongly suggests that Rac plays an important role in signaling for event. Since the secondary walls of plants that contain high levels of lignin and cellulose are the major source of biomass on earth, understanding what signals control this process may well in the future have important implications for manipulating the timing and extent of secondary wall deposition. 6) When the cotton Rac13 promoter is fused to the reporter gene GUS, expression patterns in Arabidopsis indicate very strong and specific expression in developing trichomes and in developing xyelm. Since both of these cell types are engaged in secondary wall synthesis, this further supports a role for Rac in signaling for onset of this process. Since cotton fibers are anatomically defined as trichomes, these data may also be quite useful for future studies in which the trichomes of Arabidopsis may serve as a model for cotton fiber development; the Rac promoter can therefore be useful to drive expression of other genes proposed to affect fiber development and study the effects on the process; 7) The Rac promoter has also been shown to be the best so far tested for use in development of a system for transient transformation of developing cotton fibers, a technique that should have many applications in the field of cotton biotechnology; 8) One candidate protein that may interact with Rac13 to be characterized further in the future is a protein kinase that may be analogous to the PAK kinase that is known to interact with Rac in mammals.
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