TFS1: A suppressor of cdc25 mutations in Saccharomyces cerevisiae

Robinson, Lucy C.; Tatchell, Kelly

doi:10.1007/bf00290674

Cited by 56 publications

(55 citation statements)

References 54 publications

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“…In S. cerevisiae, Tfs1 was discovered as a multicopy suppressor of the cdc25-1 mutation with a connection to the Ras/cAMP signaling pathway (61) and is a highaffinity inhibitor of carboxypeptidase Y (13). The role of Tfs1 may be conserved in fungal pathogens; recently, the C. neoformans TFS1 homologue, OVA1, was shown to be upregulated in the pka1 mutant by SAGE (serial analysis of gene expression) analysis and to negatively regulate the cAMP pathway (31).…”

Section: Resultsmentioning

confidence: 99%

Genome-Wide Transcriptional Profiling of the Cyclic AMP-Dependent Signaling Pathway during Morphogenic Transitions of Candida albicans

et al. 2007

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Candida albicans is an opportunistic human fungal pathogen that causes systemic candidiasis as well as superficial mucosal candidiasis. In response to the host environment, C. albicans transitions between yeast and hyphal forms. In particular, hyphal growth is important in facilitating adhesion and invasion of host tissues, concomitant with the expression of various hypha-specific virulence factors. In previous work, we showed that the cyclic AMP (cAMP) signaling pathway plays a crucial role in morphogenic transitions and virulence of C. albicans by studying genes encoding adenylate cyclase-associated protein ( Here, microarrays were probed with RNA from strains with hypoactive (cap1/cap1 null mutant), hyperactive (pde2/pde2 null mutant), and wild-type cAMP signaling pathways to provide insight into the molecular mechanisms of virulence that are regulated by cAMP and that are related to the morphogenesis of C. albicans. Genes controlling metabolic specialization, cell wall structure, ergosterol/lipid biosynthesis, and stress responses were modulated by cAMP during hypha formation. Phenotypic traits predicted to be regulated by cAMP from the profiling results correlated with the relative strengths of the mutants when tested for resistance to azoles and subjected to heat shock stress and oxidative/nitrosative stress. The results from this study provide important insights into the role of the cAMP signaling pathway not only in morphogenic transitions of C. albicans but also for adaptation to stress and for survival during host infections.

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Section: Resultsmentioning

confidence: 99%

Genome-Wide Transcriptional Profiling of the Cyclic AMP-Dependent Signaling Pathway during Morphogenic Transitions of Candida albicans

et al. 2007

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“…A family of RKIP-related proteins with 29 to 55% sequence identity to the mammalian proteins have also been identified in Drosophila, Caenorhabditis elegans, Saccharomyces cerevisiae, several parasites, including Onchocerca volvulus and Toxocara canis, and the flowering plants Antirrhinum and Arabidopsis (5,6,16,18,56,59,64). Despite limited sequence conservation between mammalian RKIP and some of these orthologues, recent studies of the crystal structures of two mammalian RKIPs and Antirrhinum CEN revealed that they displayed an almost identical novel ␤-fold topology (3,4,65).…”

Section: Discussionmentioning

confidence: 99%

Raf Kinase Inhibitor Protein Interacts with NF-κB-Inducing Kinase and TAK1 and Inhibits NF-κB Activation

Yeung

Rose

Dhillon

et al. 2001

Molecular and Cellular Biology

353

320

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The transcriptional activator nuclear factor kappa B (NF-B) is required for the upregulation of a large number of genes in response to inflammation, viral and bacterial infection, and other stress stimuli. Genes that respond to NF-B encode a variety of cytokines, cell adhesion molecules, and acute-phase response proteins as well as apoptotic suppressor and effector proteins. It is believed that this reprogramming of gene expression is essential for cell survival during situations of physiological crisis (61). The activation of NF-B in response to stimulation by the proinflammatory cytokines tumor necrosis factor alpha (TNF-␣) and interleukin 1 beta (IL-1␤) has been extensively studied (17, 30); however, the mechanisms that modulate and eventually limit these responses are still poorly understood (61).We report here that the recently discovered protein kinase inhibitor protein RKIP (Raf kinase inhibitor protein) acts to inhibit NF-B activation. RKIP was first identified as an interacting partner of Raf-1 and shown to function as a negative regulator of the mitogen-activated protein (MAP) kinase (MAPK) cascade initiated by 76). The Raf-1-initiated pathway is comprised of three sequentially acting protein kinases: a MAP kinase kinase kinase (MAPKKK), a MAP kinase kinase (MAPKK), and a MAPK. This basic relationship has now been found to be conserved in several protein kinase pathways. In the Raf-1 pathway the MAPK is ERK1/2 (extracellular signal-regulated kinase 1 and 2), the MAPKK is MEK1 (MAP/ERK kinase 1), and the MAPKKK is Raf-1 itself. Functional studies using both gain-of-function and loss-of-function approaches demonstrated that RKIP disrupts the interaction between 76). Depletion of endogenous RKIP upregulated Raf-1 kinase activity and MAPK signaling, whereas ectopic expression of RKIP suppressed Raf-1 kinase activity and MAPK signaling as well as v-Raf-mediated transformation. Biochemical studies showed that RKIP efficiently dissociated preformed Raf/MEK complexes and behaved kinetically as a competitive inhibitor of MEK phosphorylation. In vivo, the association of endogenous RKIP with Raf-1 correlated inversely with Raf-1 kinase activity during serum stimulation of quiescent cells.Active NF-B is a dimer that can be assembled from several members of the Rel family of transcription factors, and some form of NF-B is expressed in most cell types (61). In unstimulated cells, NF-B is retained in the cytoplasm in an inactive form bound to a family of inhibitory proteins known as IB (inhibitors of B). Activation of NF-B requires the phosphorylation and degradation of IB, which allows the NF-B dimer to translocate into the nucleus. Virtually all of the many stimuli that can activate NF-B cause the phosphorylation of IB on

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“…Other members of the PEBP family include the putative odorant-binding protein in Drosophila (29), the putative PEBP of the malaria parasite Plasmodium falciparum (30), and the Ov-16 antigen of Onchocera volvulus (31) and the toxocara excretory-secretory antigen 26 of Toxocara canis (32), two parasitic nematodes. A dosage-dependent suppressor of CDC25 mutations in Saccharomyces cerevisiae, TFS1 (33), and several proteins in flowering plants (Arabidopsis thaliana (Refs. 34 -36) and Antirrhinum (Ref.…”

Section: Discussionmentioning

confidence: 99%

The Phosphatidylethanolamine-binding Protein Is the Prototype of a Novel Family of Serine Protease Inhibitors

Hengst

Albrecht

Heß

et al. 2001

Journal of Biological Chemistry

173

145

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Serine proteases are involved in many processes in the nervous system and specific inhibitors tightly control their proteolytic activity. Thrombin is thought to play a role in tissue development and homeostasis. To date, protease nexin-1 is the only known endogenous protease inhibitor that specifically interferes with thrombotic activity and is expressed in the brain. In this study, we report the detection of a novel thrombin inhibitory activity in the brain of protease nexin-1 (؊/؊) mice. Purification and subsequent analysis by tandem mass spectrometry identified this protein as the phosphatidylethanolamine-binding protein (PEBP). We demonstrate that PEBP exerts inhibitory activity against several serine proteases including thrombin, neuropsin, and chymotrypsin, whereas trypsin, tissue type plasminogen activator, and elastase are not affected. Since PEBP does not share significant homology with other serine protease inhibitors, our results define it as the prototype of a novel class of serine protease inhibitors. PEBP immunoreactivity is found on the surface of Rat-1 fibroblast cells and although its sequence contains no secretion signal, PEBP-H 6 can be purified from the conditioned medium upon recombinant expression.

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TFS1: A suppressor of cdc25 mutations in Saccharomyces cerevisiae

Cited by 56 publications

References 54 publications

Genome-Wide Transcriptional Profiling of the Cyclic AMP-Dependent Signaling Pathway during Morphogenic Transitions of Candida albicans

Genome-Wide Transcriptional Profiling of the Cyclic AMP-Dependent Signaling Pathway during Morphogenic Transitions of Candida albicans

Raf Kinase Inhibitor Protein Interacts with NF-κB-Inducing Kinase and TAK1 and Inhibits NF-κB Activation

The Phosphatidylethanolamine-binding Protein Is the Prototype of a Novel Family of Serine Protease Inhibitors

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