scholarly journals The F-box protein Grr1 regulates the stability of Ccn1, Cln3 and Hof1 and cell morphogenesis in Candida albicans

2006 ◽  
Vol 62 (1) ◽  
pp. 212-226 ◽  
Author(s):  
Wan Jie Li ◽  
Yan Ming Wang ◽  
Xin De Zheng ◽  
Qing Mei Shi ◽  
Ting Ting Zhang ◽  
...  
Keyword(s):  
Candida Albicans ◽  
Cell Morphogenesis ◽  
The Stability ◽  
F Box Protein

scholarly journals Differential Regulation of White-Opaque Switching by Individual Subunits of Candida albicans Mediator

2013 ◽  
Vol 12 (9) ◽  
pp. 1293-1304 ◽  
Author(s):  
Anda Zhang ◽  
Zhongle Liu ◽  
Lawrence C. Myers
Keyword(s):  
Candida Albicans ◽  
Ectopic Expression ◽  
Small Subset ◽  
Content Type ◽  
Impaired Ability ◽  
Transcriptional Effect ◽  
Environmental Induction ◽  
Gene Regulatory ◽  
The Stability ◽  
Negative Gene

ABSTRACT The multisubunit eukaryotic Mediator complex integrates diverse positive and negative gene regulatory signals and transmits them to the core transcription machinery. Mutations in individual subunits within the complex can lead to decreased or increased transcription of certain subsets of genes, which are highly specific to the mutated subunit. Recent studies suggest a role for Mediator in epigenetic silencing. Using white-opaque morphological switching in Candida albicans as a model, we have shown that Mediator is required for the stability of both the epigenetic silenced (white) and active (opaque) states of the bistable transcription circuit driven by the master regulator Wor1. Individual deletions of eight C. albicans Mediator subunits have shown that different Mediator subunits have dramatically diverse effects on the directionality, frequency, and environmental induction of epigenetic switching. Among the Mediator deletion mutants analyzed, only Med12 has a steady-state transcriptional effect on the components of the Wor1 circuit that clearly corresponds to its effect on switching. The MED16 and MED9 genes have been found to be among a small subset of genes that are required for the stability of both the white and opaque states. Deletion of the Med3 subunit completely destabilizes the opaque state, even though the Wor1 transcription circuit is intact and can be driven by ectopic expression of Wor1. The highly impaired ability of the med3 deletion mutant to mate, even when Wor1 expression is ectopically induced, reveals that the activation of the Wor1 circuit can be decoupled from the opaque state and one of its primary biological consequences.

scholarly journals The human F box protein β-Trcp associates with the Cul1/Skp1 complex and regulates the stability of β-catenin

Oncogene ◽  
1999 ◽  
Vol 18 (4) ◽  
pp. 849-854 ◽  
Author(s):  
E Latres ◽  
D S Chiaur ◽  
M Pagano
Keyword(s):  
The Stability ◽  
F Box Protein

scholarly journals Divalent Cations Affect the Stability and Structure of Dad2p, a Subunit of the Candida Albicans Kinetochore Dam1 Complex

2016 ◽  
Vol 6 (1) ◽  
pp. 26
Author(s):  
Jennifer Turner Waldo ◽  
Tsering Dolma ◽  
Emily Rouse
Keyword(s):  
Candida Albicans ◽  
Mitotic Spindle ◽  
Divalent Cations ◽  
Dynamic Structure ◽  
Biochemical Properties ◽  
Differential Scanning Fluorimetry ◽  
A Subunit ◽  
Dam1 Complex ◽  
The Stability ◽  
Shed Light

<p class="1Body">The heterodecameric Dam1 complex is involved in establishing and maintaining the connection between the kinetochore and the mitotic spindle during mitosis. Biochemical studies of the reconstituted complex have shed light upon how it interacts with microtubules. However, little information about the biochemical properties of the isolated subunits has been available. This report examines the stability and structure of Dad2p, one of the Dam1 complex subunits isolated from <em>Candida albicans</em>. By employing differential scanning fluorimetry, protease protection and hydrodynamic analyses, we show that Dad2p is specifically responsive to the presence of divalent cations. This observation may be important for understanding the dynamic structure and regulation of the Dam1 complex in fungal cells.</p>

scholarly journals The F-box protein Ppa is a common regulator of core EMT factors Twist, Snail, Slug, and Sip1

2011 ◽  
Vol 194 (1) ◽  
pp. 17-25 ◽  
Author(s):  
Rachel Lander ◽  
Kara Nordin ◽  
Carole LaBonne
Keyword(s):  
Structural Diversity ◽  
Ubiquitin Proteasome System ◽  
Common Mechanism ◽  
Rich Domain ◽  
Transcriptional Regulatory ◽  
Snail Family ◽  
Ubiquitin Proteasome ◽  
Snail Proteins ◽  
The Stability ◽  
F Box Protein

A small group of core transcription factors, including Twist, Snail, Slug, and Sip1, control epithelial–mesenchymal transitions (EMTs) during both embryonic development and tumor metastasis. However, little is known about how these factors are coordinately regulated to mediate the requisite behavioral and fate changes. It was recently shown that a key mechanism for regulating Snail proteins is by modulating their stability. In this paper, we report that the stability of Twist is also regulated by the ubiquitin–proteasome system. We found that the same E3 ubiquitin ligase known to regulate Snail family proteins, Partner of paired (Ppa), also controlled Twist stability and did so in a manner dependent on the Twist WR-rich domain. Surprisingly, Ppa could also target the third core EMT regulatory factor Sip1 for proteasomal degradation. Together, these results indicate that despite the structural diversity of the core transcriptional regulatory factors implicated in EMT, a common mechanism has evolved for controlling their stability and therefore their function.

The F‐box Protein FBXL16 Upregulates the Stability of c‐myc Oncoprotein by Antagonizing FBW7 Function

2020 ◽  
Vol 34 (S1) ◽  
pp. 1-1
Author(s):  
Marion Morel ◽  
Krushangi Shah ◽  
Weiwen Long
Keyword(s):  
The Stability ◽  
F Box Protein

scholarly journals Reconstitution of the Jasmonate Signaling Pathway in Plant Protoplasts

Cells ◽  
2019 ◽  
Vol 8 (12) ◽  
pp. 1532 ◽  
Author(s):  
Ning Li ◽  
Joachim F. Uhrig ◽  
Corinna Thurow ◽  
Li-Jun Huang ◽  
Christiane Gatz
Keyword(s):  
Signaling Pathway ◽  
Function Analysis ◽  
Luciferase Reporter ◽  
Luciferase Reporter Gene ◽  
Protein Levels ◽  
Activation Of Transcription ◽  
Subsequent Degradation ◽  
The Stability ◽  
F Box Protein ◽  
Ja Signaling

The phytohormone jasmonic acid (JA) plays an important role in various plant developmental processes and environmental adaptations. The JA signaling pathway has been well-elucidated in the reference plant Arabidopsis thaliana. It starts with the perception of the active JA derivative, jasmonoyl-isoleucine (JA-Ile), by the F-box protein COI1 which is part of the E3-ligase SCFCOI1. Binding of JA-Ile enables the interaction between COI1 and JAZ repressor proteins. Subsequent degradation of JAZ proteins leads to the activation of transcription factors like e.g., MYC2. Here we demonstrate that the pathway can be reconstituted in transiently transformed protoplasts. Analysis of the stability of a JAZ1-fLuc fusion protein as a function of COI1 transiently expressed in coi1 protoplasts allows structure function analysis of both JAZs and COI1. Using this system, we found that conserved cysteines in COI1 influence steady state COI1 protein levels. Using a luciferase reporter gene under the control of the JAZ1 promoter enable to address those features of JAZ1 that are required for MYC2 repression. Interestingly, the conserved TIFY-motif previously described to interact with NINJA to recruit the corepressor TOPLESS is not necessary for repression. This result is in favor of the alternative repression mode that proposes a direct competition between repressive JAZs and promotive MEDIATOR25 at MYC2. Finally, using protoplasts from the aos coi1 double mutant, which is deficient in JA synthesis and perception, we provide a system that has the potential to study the activity of different COI1 variants in the presence of different ligands.

Role of CaECM25 in cell morphogenesis, cell growth and virulence in Candida albicans

2008 ◽  
Vol 51 (4) ◽  
pp. 362-372 ◽  
Author(s):  
TingTing Zhang ◽  
WanJie Li ◽  
Di Li ◽  
Yue Wang ◽  
JianLi Sang
Keyword(s):  
Candida Albicans ◽  
Cell Growth ◽  
Cell Morphogenesis

Pathogenic mutations in the ALS gene CCNF cause cytoplasmic mislocalization of Cyclin F and elevated VCP ATPase activity

2019 ◽  
Vol 28 (20) ◽  
pp. 3486-3497 ◽  
Author(s):  
Yujiao Yu ◽  
Tadashi Nakagawa ◽  
Akane Morohoshi ◽  
Makiko Nakagawa ◽  
Noriko Ishida ◽  
...  
Keyword(s):  
Atpase Activity ◽  
Progressive Decline ◽  
Ubiquitin Ligase Complex ◽  
The Stability ◽  
F Box Protein ◽  
Cyclin F ◽  
Als Patients ◽  
Lateral Sclerosis

Abstract Amyotrophic lateral sclerosis (ALS) is an adult-onset motor neuron disease characterized by a progressive decline in motor function. Genetic analyses have identified several genes mutated in ALS patients, and one of them is Cyclin F gene (CCNF), the product of which (Cyclin F) serves as the substrate-binding module of a SKP1–CUL1–F-box protein (SCF) ubiquitin ligase complex. However, the role of Cyclin F in ALS pathogenesis has remained unclear. Here, we show that Cyclin F binds to valosin-containing protein (VCP), which is also reported to be mutated in ALS, and that the two proteins colocalize in the nucleus. VCP was found to bind to the NH2-terminal region of Cyclin F and was not ubiquitylated by SCFCyclin F in transfected cells. Instead, the ATPase activity of VCP was enhanced by Cyclin F in vitro. Furthermore, whereas ALS-associated mutations of CCNF did not affect the stability of Cyclin F or disrupt formation of the SCFCyclin F complex, amino acid substitutions in the VCP binding region increased the binding ability of Cyclin F to VCP and activity of VCP as well as mislocalization of the protein in the cytoplasm. We also provided evidence that the ATPase activity of VCP promotes cytoplasmic aggregation of transactivation responsive region (TAR) DNA-binding protein 43, which is commonly observed in degenerating neurons in ALS patients. Given that mutations of VCP identified in ALS patients also increase its ATPase activity, our results suggest that Cyclin F mutations may contribute to ALS pathogenesis by increasing the ATPase activity of VCP in the cytoplasm, which in turn increases TDP-43 aggregates.

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