F-box proteins and DCAF proteins will be the substrate binding subunits of SCF (Skp1-Cul1-F-box protein) and CRL4 (Cul4-RING protein Ligase) ubiquitin ligase complexes respectively. rapid and temporally-controlled proteolysis of key cellular regulators by the ubiquitin-proteasome system (UPS). E3 ubiquitin ligases confer substrate specificity to the UPS. Among the eukaryotic E3s Cullin-RING Ligases (CRLs) constitute the largest family of multi-subunit ubiquitin ligases (Petroski and Deshaies 2005 The archetypes of the CRL family are the CRL1/SCF (Skp1-Cul1-F-box protein) E3s which utilize different F-box proteins (69 in humans) as receptors that bind substrates. Significantly multiple F-box proteins are mutated or display altered expression in a variety of diseases including cancer (Frescas and Pagano 2008 Lipkowitz and Weissman 2011 Skaar et al. 2009 FBXO11 is conserved from nematodes to mammals and both human FBXO11 and its worm ortholog (DRE-1) form functional SCF ubiquitin ligases ...
The F-box domain is a protein structural motif of about 50 amino acids that mediates protein-protein interactions. The F-box protein is one of the four components of the SCF (SKp1, Cullin, F-box protein) complex, which mediates ubiquitination of proteins targeted for degradation by the proteasome, playing an essential role in many cellular processes. Several discoveries have been made on the use of the ubiquitin-proteasome system by viruses of several families to complete their infection cycle. On the other hand, F-box proteins can be used in the defense response by the host. This review describes the role of F-box proteins and the use of the ubiquitin-proteasome system in virus-host interactions.
The F-box domain is a protein structural motif of about 50 amino acids that mediates protein-protein interactions. The F-box protein is one of the four components of the SCF (SKp1, Cullin, F-box protein) complex, which mediates ubiquitination of proteins targeted for degradation by the proteasome, playing an essential role in many cellular processes. Several discoveries have been made on the use of the ubiquitin-proteasome system by viruses of several families to complete their infection cycle. On the other hand, F-box proteins can be used in the defense response by the host. This review describes the role of F-box proteins and the use of the ubiquitin-proteasome system in virus-host interactions.
In response to DNA damage, eukaryotic cells initiate a complex signalling pathway, termed the DNA damage response (DDR), which coordinates cell cycle arrest with DNA repair. Studies have shown that oncogene-induced senescence, which provides a barrier to tumour development, involves activation of the DDR. Using a genome-wide RNA interference (RNAi) screen, we have identified 17 factors required for oncogenic BRAF to induce senescence in primary fibroblasts and melanocytes. One of these factors is an F-box protein, FBXO31, a candidate tumour suppressor encoded in 16q24.3, a region in which there is loss of heterozygosity in breast, ovarian, hepatocellular and prostate cancers. Here we study the cellular role of FBXO31, identify its target substrate and determine the basis for its growth inhibitory activity. We show that ectopic expression of FBXO31 acts through a proteasome-directed pathway to mediate the degradation of cyclin D1, an important regulator of progression from G1 to S phase, resulting in
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F-box proteins are an expanding family of eukaryotic proteins characterized by an approximately 40 aminoacid motif, the F box (so named because cyclin F was one of the first proteins in which this motif was identified) [1]. Some F-box proteins have been shown to be critical for the controlled degradation of cellular regulatory proteins [2] [3]. In fact, F-box proteins are one of the four subunits of ubiquitin protein ligases called SCFs. The other three subunits are the Skp1 protein; one of the cullin proteins (Cul1 in metazoans and Cdc53 or Cul A in the yeast Saccharomyces cerevisiae); and the recently identified Roc1 protein (also called Rbx1 or Hrt1). SCF ligases bring ubiquitin conjugating enzymes (either Ubc3 or Ubc4) to substrates that are specifically recruited by the different F-box proteins. The need for high substrate specificity and the large number of known F-box proteins in yeast and worms [2] [4] suggest the existence of a large family of mammalian F-box proteins. Using Skp1 as a ...
TY - JOUR. T1 - A proteomic screen reveals the mitochondrial outer membrane protein Mdm34p as an essential target of the F-box protein Mdm30p. AU - Ota, Kazuhisa. AU - Kito, Keiji. AU - Okada, Satoshi. AU - Ito, Takashi. PY - 2008/12/1. Y1 - 2008/12/1. N2 - Ubiquitination plays various critical roles in eukaryotic cellular regulation and is medated by a cascade of enzymes including ubiquitin protein ligase (E3). The Skp1-Cullin-F-box protein complex comprises the largest E3 family, in each member of which a unique F-box protein binds its targets to define substrate specificity. Although genome sequencing uncovers a growing number of F-box proteins, most of them have remained as orphans because of the difficulties in identification of their substrates. To address this issue, we tested a quantitative proteomic approach by combining the stable isotope labeling by amino acids in cell culture (SILAC), parallel affinity purification (PAP) that we had developed for efficient enrichment of ...
This gene encodes a member of the F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein encoded by this gene was previously referred to as FBX30, and belongs to the Fbws class; in addition to an F-box, this protein contains 7 tandem WD40 repeats. This protein binds directly to cyclin E and probably targets cyclin E for ubiquitin-mediated degradation. Mutations in this gene are detected in ovarian and breast cancer cell lines, implicating the genes potential role in the pathogenesis of human cancers. Multiple transcript variants encoding different ...
We report the map-based cloning of the SLY1 gene of Arabidopsis. SLY1 is a positive regulator of GA response. Recessive mutations in SLY1 affect the full range of GA phenotypes, including feedback regulation of the GA3ox1 biosynthetic gene (Figure 1). Thus, the fact that SLY1 encodes a putative F-box protein suggests that the GA signal is transmitted via an SCFSLY1 E3 ubiquitin ligase.. Ubiquitylation controls target protein activity at multiple levels, including proteolysis and the potentiation of transcriptional activation domains (Conaway et al., 2002). Major members of the SCF complex include homologs of SKP1, cullin, and the RING-finger domain protein Rbx1 (Zheng et al., 2002). The F-box subunit directs the interaction of the complex with a specific target for ubiquitylation. The conserved F-box domain allows the protein to interact with the SKP1 subunit of the SCF. SKP1 tethers the F-box protein to the N terminus of cullin. The RING-finger protein Rbx1 binds the C terminus of cullin and ...
Members of the F-box protein family, such as FBXO40, are characterized by an approximately 40-amino acid F-box motif. SCF complexes, formed by SKP1 (MIM 601434), cullin (see CUL1; MIM 603134), and F-box proteins, act as protein-ubiquitin ligases. F-box proteins interact with SKP1 through the F box, and they interact with ubiquitination targets through other protein interaction domains (Jin et al., 2004 [PubMed 15520277]).[supplied by OMIM, Mar 2008 ...
TY - JOUR. T1 - Presenilin modulates EGFR signaling and cell transformation by regulating the ubiquitin ligase Fbw7. AU - Rocher-Ros, V.. AU - Marco, S.. AU - Mao, J. H.. AU - Gines, S.. AU - Metzger, D.. AU - Chambon, P.. AU - Balmain, A.. AU - Saura, C. A.. PY - 2010/5/20. Y1 - 2010/5/20. N2 - The epidermal growth factor receptor (EGFR) and Notch signaling pathways have antagonistic roles during epidermal differentiation and carcinogenesis. The molecular mechanisms regulating the crosstalk between EGFR and Notch during epidermal transformation are largely unknown. We found enhanced EGFR-dependent signaling, proliferation and oncogenic transformation caused by loss of presenilins (PS), the catalytic components of γ-secretase that generates the Notch1 intracellular domain (NICD). The underlying mechanism for abnormal EGFR signaling in PS-deficient cells involves γ-secretase-independent transcriptional upregulation of the E3 ubiquitin ligase Fbw7. Fbw7α, which targets NICD for degradation, ...
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FUNCTION: [Summary is not available for the mouse gene. This summary is for the human ortholog.] This gene encodes a member of the cyclin family. Cyclins are important regulators of cell cycle transitions through their ability to bind and activate cyclin-dependent protein kinases. This member also belongs to the F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of the ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein encoded by this gene belongs to the Fbxs class and it was one of the first proteins in which the F-box motif was identified. [provided by RefSeq, Jul 2008 ...
Description: This gene encodes a member of the F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein encoded by this gene belongs to the Fbws class and, in addition to an F-box, contains multiple WD40 repeats. This gene contains at least 14 exons, and its alternative splicing generates 3 transcript variants diverging at the presence/absence of two alternate exons ...
the evolutionary conserved f-box motifs can be found in various organisms ranging from fungi, insects, fish, and mammals to plants. f-box proteins are subunits of SCF-type E3 ubiquitin ligases and selectively recruit target proteins via their protein-protein interaction domain for ubiquitination and subsequent proteasomal degradation. the arabidopsis genome encodes appr. 700 f-box proteins which makes this gene superfamily one of the largest in eukaryotes. however, a biological function has been assigned to less than 30 genes/proteins of the 700 members. We are generally interested in the evolution and selection patterns acting on f-box proteins (see Schumann et al., 2011 in press) and study a small sub-family to understand the molecular functions of each member. ...
FBXO4 Full-Length MS Protein Standard (NP_036308), Labeled with [U- 13C6, 15N4]-L-Arginine and [U- 13C6, 15N2]-L-Lysine, was produced in human 293 cells (HEK293) with fully chemically defined cell culture medium to obtain incorporation efficiency at Creative-Proteomics. This gene encodes a member of the F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of the ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein encoded by this gene belongs to the Fbxs class. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
FUNCTION: [Summary is not available for the mouse gene. This summary is for the human ortholog.] This gene encodes a member of the F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein encoded by this gene belongs to the Fbls class and, in addition to an F-box, contains several tandem leucine-rich repeats and is localized in the nucleus. [provided by RefSeq, Jul 2008 ...
Gene Information This gene encodes a member of the F-box protein family which is characterized by an approximately 40 amino acid motif the F-box. The F-box proteins constitute one of the four subunits of the ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box) which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing WD-40 domains Fbls containing leucine-rich repeats and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein encoded by this gene belongs to the Fbxs class. This protein is similar to xenopus early mitotic inhibitor-1 (Emi1) which is a mitotic regulator that interacts with Cdc20 and inhibits the anaphase promoting complex. Alternatively spliced transcript variants encoding different isoforms have been identified. [provided by RefSeq Dec 2008]. ...
This gene encodes a member of the F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein encoded by this gene belongs to the Fbxs class. Alternative splicing of this gene generates 2 transcript variants. [provided by RefSeq, Jul 2008] ...
Members of the F-box protein family, such as FBXL18, are characterized by an approximately 40-amino acid F-box motif. SCF complexes, formed by SKP1 (MIM 601434), cullin (see CUL1; MIM 603134), and F-box proteins, act as protein-ubiquitin ligases. F-box proteins interact with SKP1 through the F box, and they interact with ubiquitination targets through other protein interaction domains (Jin et al., 2004 [PubMed 15520277]).[supplied by OMIM, Mar 2008]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data because no single transcript was available for the full length of the gene. The extent of this transcript is supported by transcript alignments and orthologous data ...
FBXW7 (F-box and WD40 repeat domain containing 7, also known as FBW7, hCDC4), a tumour suppressor gene, is mutated in many human malignancies.1 FBXW7 encodes the substrate recognition component of a Skp, Cullin, F-box-containing (SCF)-E3 ubiquitin ligase complex and negatively regulates multiple proteins with established roles in the control of cell division and growth, including cyclin E, c-Jun, c-Myc, mTor and Notch. There are several excellent reviews of the growing knowledge of FBXW7.2-5. As it became apparent that FBXW7 regulates many oncoproteins, it was hypothesised that mutations in FBXW7 may cause tumorigenesis. FBXW7 mutations were initially identified by Spruck et al in ovarian and breast cancer cell lines.6 ,7 Since then many studies have assessed FBXW7 mutation status in a range of cancer types, including both solid tumours and haematological neoplasms. A study by Akhoondi et al8 significantly contributed to this collection, as extensive genetic screening of over 500 primary tumours ...
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F-box family protein; FUNCTIONS IN: molecular_function unknown; INVOLVED IN: biological_process unknown; LOCATED IN: cellular_component unknown; EXPRESSED IN: 22 plant structures; EXPRESSED DURING: 13 growth stages; CONTAINS InterPro DOMAIN/s: Cyclin-like F-box (InterPro:IPR001810); BEST Arabidopsis thaliana protein match is: F-box family protein (TAIR:AT2G16300.1); Has 77 Blast hits to 74 proteins in 7 species: Archae - 0; Bacteria - 0; Metazoa - 0; Fungi - 0; Plants - 73; Viruses - 0; Other Eukaryotes - 4 (source: NCBI BLink ...
Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Mediates the polyubiquitination and proteasomal degradation of CAMK1 leading to disruption of cyclin D1/CDK4 complex assembly which results in G1 cell cycle arrest in lung epithelia.
Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Role in neural transmission (By similarity).
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0.0001 with respect to handle conditions for early apoptosis, and p0.01 with respect to control circumstances for late apoptosis/secondary necrosis. (C)
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
I have studied the mechanism through which cells sense and respond to DNA damage and regulate the cell cycle. My lab uncovered a signal transduction pathway that is activated when DNA is broken or DNA polymerases are stalled. The generation of ssDNA is sensed and results in activation of a protein kinase cascade that activates gene expression and causes cell cycle arrest. This pathway is important for preventing cancer-causing mutations.. I also study how the cell cycle is regulated and discovered a family of Cdk inhibitors, CKIs, which organisms use to control cell proliferation during development and to prevent cancer. Through investigations of how CKIs are regulated, we discovered a modular pathway called the SCF through which proteins are marked for destruction. The SCF has a replaceable adaptor called an F-box protein that works like a socket wrench. When a particular F-box protein is in the SCF it recognizes one set of proteins to destroy, when another is present a different set is ...
The apaG domain is a ~125 amino acids domain present in bacterial apaG proteins and in eukaryotic F-box proteins. The domain is named after the bacterial apaG protein, of which it forms the core. The domain also occurs in the C-terminal part of eukaryotic proteins with an N-terminal F-box domain (see ,PDOC50181,). The Salmonella typhimurium apaG domain protein corD is involved in Co(2+) resistance and Mg(2+) efflux. Tertiary structures from different apaG proteins show a fold of several β-sheets (see ,PDB:1XVS,). The apaG domain may be involved in protein-protein interactions which could be implicated in substrate-specificity [1,2,3,4]. Some proteins known to contain an apaG domain: ...
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Complete information for METTL16 gene (Protein Coding), Methyltransferase Like 16, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
These animations show what happens to unfolded proteins when they meet one another. If the proteins reconfigure (wiggle around) at the same rate that they collide they will stick together (green strings), which can lead to diseases such as Parkinsons or Alzheimers. But if they reconfigure slower (blue) or faster (red) they are able to escape sticking. Some small molecules can stick to the protein and make them reconfigure faster to prevent sticking (changing green to red), potentially becoming drugs for these diseases ...
FBXL10b, 0.4 ml. This gene encodes a member of the F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box.
Complete information for FBXO48 gene (Protein Coding), F-Box Protein 48, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
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Core component of multiple cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of…
TY - JOUR. T1 - p107 inhibits G1 to S phase progression by down-regulating expression of the F-box protein Skp2. AU - Rodier, Geneviève. AU - Makris, Constantin. AU - Coulombe, Philippe. AU - Scime, Anthony. AU - Nakayama, Keiko. AU - Nakayama, Keiichi I.. AU - Meloche, Sylvain. PY - 2005/1/3. Y1 - 2005/1/3. N2 - Cell cycle progression is negatively regulated by the pocket proteins pRb, p107, and p130. However, the mechanisms responsible for this inhibition are not fully understood. Here, we show that overexpression of p107 in fibroblasts inhibits Cdk2 activation and delays S phase entry. The inhibition of Cdk2 activity is correlated with the accumulation of p27, consequent to a decreased degradation of the protein, with no change of Thr187 phosphorylation. Instead, we observed a marked decrease in the abundance of the F-box receptor Skp2 in p107-overexpressing cells. Reciprocally, Skp2 accumulates to higher levels in p107-/- embryonic fibroblasts. Ectopic expression of Skp2 restores p27 ...
From NCBI Gene:. This gene encodes a member of the F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein encoded by this gene belongs to the Fbxs class. It can function as an arginine methyltransferase that symmetrically dimethylates arginine residues, and it acts as an adaptor protein to mediate the neddylation of p53, which leads to the suppression of p53 function. This gene is known to be down-regulated in melanocytes from patients with vitiligo, a skin disorder that results in depigmentation. Polymorphisms in this gene are associated with chronic ...
SCF ubiquitin ligases regulate the ubiquitin-dependent proteolysis of a myriad of substrate proteins, including p27, Cyclin E, and IkBa. To further gain insight into SCF regulation and function, we purified SCF from mammalian cells and found the Cop9 Signalosome associated with SCF. Interestingly, deletion of the CSN in S. pombe resulted in the hypermodification of Cul1 with Nedd8 in vivo. Furthermore, we found that the CSN can promote the removal of Nedd8 from Cul1 in vitro, suggesting CSN regulates SCF through deneddylation. To investigate the basis of CSN-dependent deneddylation activity, we analyzed the CSN and the 26S proteasome for conserved sequences that could be representative of a catalytic motif. We identified the JAMM motif in Csn5 and Rpn11 of the proteasome. Mutations in JAMM eliminated CSN-dependent deneddylating activity. Moreover, mutations in JAMM reduce the restrictive temperature of several SCF temperature sensitive mutants, suggesting that CSN acts positively on SCF ...
The hormone gibberellin (GA) tightly regulates many growth and developmental processes throughout the life cycle of a plant. The important roles of GA are illustrated by the dramatic defects of GA biosynthetic and signaling mutants in germination, leaf expansion, stem elongation, apical dominance, floral development, and fertility (Davies, 1995). The DELLA proteins are highly conserved negative regulators of GA signaling in Arabidopsis thaliana and several crop plants, including barley (Hordeum vulgare), grape (Vitis vinifera), maize (Zea mays), rice (Oryza sativa), and wheat (Triticum aestivum) (Boss and Thomas, 2002; Olszewski et al., 2002). These DELLA proteins were named after a conserved amino acid motif near their N termini (Olszewski et al., 2002; Peng and Harberd, 2002). The DELLA proteins form a subfamily within a family of putative transcriptional regulators known as GRAS (for GA INSENSITIVE [GAI], REPRESSOR OF ga1-3 [RGA], and SCR) (Pysh et al., 1999). In addition to GA signaling, ...
Protein target information for F-box protein YLR352W (Saccharomyces cerevisiae S288C). Find diseases associated with this biological target and compounds tested against it in bioassay experiments.
ArabidopsisAuxin is a pivotal plant hormone that controls many aspects of plant growth and development. Perceived by a small family of F-box proteins including transport inhibitor response 1 (TIR1), auxin regulates gene expression by promoting SCF ubiquitin-ligase-catalysed degradation of the Aux/IAA transcription repressors, but how the TIR1 F-box protein senses and becomes activated by auxin remains unclear. Here we present the crystal structures of the TIR1-ASK1 complex, free and in complexes with three different auxin compounds and an Aux/IAA substrate peptide. These structures show that the leucine-rich repeat domain of TIR1 contains an unexpected inositol hexakisphosphate co-factor and recognizes auxin and the Aux/IAA polypeptide substrate through a single surface pocket. Anchored to the base of the TIR1 pocket, auxin binds to a partially promiscuous site, which can also accommodate various auxin analogues. Docked on top of auxin, the Aux/IAA substrate peptide occupies the rest of the TIR1 ...
Insulin resistance is a critical factor in the development of metabolic disorders, including type 2 diabetes (T2DM). However, its molecular mechanisms remain incompletely understood. In the present study, we found that F-box only protein 2 (FBXO2), a substrate recognition component of SKP1-Cullin1-F-box protein (SCF) E3 ubiquitin ligase complex, were up-regulated in livers of obese mice. Furthermore, using a protein purification approach combined with high performance liquid chromatography/tandem mass spectrometry (HPLC/MS/MS), we carried out a system-wide screening of FBXO2 substrates, in which insulin receptor (IR) was identified as a substrate for FBXO2. SCFFBXO2 acts as an E3 ligase targeting the IR for ubiquitin-dependent degradation to regulate insulin signaling integrity. As a result, adenovirus-mediated overexpression of FBXO2 in healthy mice led to hyperglycemia, glucose intolerance and insulin resistance, while ablation of FBXO2 alleviated diabetic phenotypes in obese mice. Therefore, ...
Several experimental points support the proposal that p45SKP2 is a component of a potential human SCF‐type E3 ligase. First, two yeast F‐box proteins, CDC4 and GRR1, were shown to complex independently with CDC53 and SKP1 and function as specific SIC1 and CLN receptors, respectively (Skowyra et al., 1997). In fact, purified CDC4-CDC53-SKP1 complexes mixed together with CDC34 and an E1 were found to be necessary and sufficient for the multi‐ubiquitination of SIC1 in vitro. We found that p45SKP2 also interacts with a member of the cullin family, CUL‐1, in vivo. Association was established by direct co‐immunoprecipitation in vitro and in vivo (Figures 2 and 3). In addition, p45SKP2 was capable of relocalizing CUL‐1 to the nucleus when both proteins were co‐synthesized (Figure 2F). Although the exact function(s) of cullins remain to be determined, the yeast homolog of CUL‐1, CDC53, has been clearly implicated in the degradation of critical cell cycle regulatory proteins. Genetic ...
Cul1 and Cul3 mouse knockout experiments have revealed their indispensable roles in cell cycle progression and early embryogenesis (Table 3). The role of CUL1 in cell cycle control is understood in considerable detail. It was the pioneering work using the budding and fission yeast systems that led to the discovery of cullins and other CRL components and their role in cell cycle control (reviewed in [19]). Work in C. elegans and Drosophila has demonstrated the requirement of CUL1 for cell cycle progression (Table 3). Mechanistically, it is believed that the CUL1-based SCF regulates the mammalian cell cycle, at least in part, by using the Skp2 F-box protein, which directs the ubiquitin-dependent degradation of p27 and p21 (inhibitors of cyclin-dependent kinases), thereby activating cyclin-dependent kinases [20]. SCF malfunction has been linked to malignancy, as mutations in the Fbw7 F-box protein are frequently found in a variety of human cancers [21].. Studies with Cul4 deletion in C. elegans ...
The ubiquitin-proteasome pathway is one of the most important proteolytic pathways in eukaryotes. In this pathway, the small protein ubiquitin is attached to protein substrates, and the ubiquitin-protein conjugates are recognized and degraded by the 26S proteasome (Fang and Weissman, 2004). The SCF complexes are a major class of ubiquitin ligase enzyme (Gagne et al., 2002; Petroski and Deshaies, 2005). In this complex, the F-box protein plays a critical role in the determination of substrate specificity (Petroski and Deshaies, 2005). The plant hormone auxin directly induces rapid degradation of the Aux/IAA family of transcriptional repressors by SCFTIR1/AFB E3 ubiquitin ligase (Gray et al., 2001; Dharmasiri et al., 2005a, 2005b; Kepinski and Leyser, 2005; Tan et al., 2007). In Arabidopsis, TIR1 is a member of a small group of F-box proteins that also includes AFB1 through AFB5 and the jasmonic acid receptor CORONATINE INSENSITIVE1 (COI1; Dharmasiri et al., 2005b). The TIR1 protein plays a ...
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Cyclin E, one of the activators of the cyclin-dependent kinase Cdk2, is expressed near the G1-S phase transition and is thought to be critical for the initiation of DNA replication and other S-phase functions. Accumulation of cyclin E at the G1-S boundary is achieved by periodic transcription couple …
Auxin regulates a host of plant developmental and physiological processes, including embryogenesis, vascular differentiation, organogenesis, tropic growth, and root and shoot architecture. Genetic and biochemical studies carried out over the past decade have revealed that much of this regulation involves the SCFTIR1/AFB-mediated proteolysis of the Aux/IAA family of transcriptional regulators. With the recent finding that the TRANSPORT INHIBITOR RESPONSE1 (TIR1)/AUXIN SIGNALING F-BOX (AFB) proteins also function as auxin receptors, a potentially complete, and surprisingly simple, signaling pathway from perception to transcriptional response is now before us. However, understanding how this seemingly simple pathway controls the myriad of specific auxin responses remains a daunting challenge, and compelling evidence exists for SCFTIR1/AFB-independent auxin signaling pathways ...
The Fbw7 subunit of a Skp1-Cullin-F-box (SCF) type E3 ligase complex recognizes substrates that are subsequently ubiquitylated and degraded by the proteasome. Several substrates of this SCF complex are oncoproteins, and decreased abundance of Fbw7 is seen in various cancers. Min et al. found that the prolyl isomerase Pin1 acts on a phosphorylated residue in Fbw7, thus disrupting Fbw7 dimerization and causing Fbw7 to ubiquitylate itself. The abundance of Fbw7 was inversely correlated to that of Pin1 in colon cancer samples, and the abundance of Fbw7 was higher in Pin1-/- mouse embryonic fibroblasts (MEFs) than in wild-type MEFs. The abundance of ectopically expressed Fbw7 was increased by the proteasome inhibitor MG132, and this stabilization by MG132 was not seen with a form of Fbw7 lacking the F-box motif, which is necessary for ubiquitylation, suggesting that Fbw7 may auto-ubiquitylate. Fbw7 bound to the WW domain of Pin1, an interaction that required the phosphorylation of Thr205 in Fbw7. The ...
Several events during the normal development of the mammalian neocortex depend on N-cadherin, including the radial migration of immature projection neurons into the cortical plate. Remarkably, radial migration requires the N-cadherin extracellular domain but not N-cadherin-dependent homophilic cell-cell adhesion, suggesting that other N-cadherin-binding proteins may be involved. We used proximity ligation and affinity purification proteomics to identify N-cadherin-binding proteins. Both screens detected MycBP2 and SPRY domain protein Fbxo45, two components of an intracellular E3 ubiquitin ligase. Fbxo45 appears to be secreted by a nonclassical mechanism, not involving a signal peptide and not requiring transport from the endoplasmic reticulum to the Golgi apparatus. Fbxo45 binding requires N-cadherin SPRY motifs that are not involved in cell-cell adhesion. SPRY mutant N-cadherin does not support radial migration in vivo. Radial migration was similarly inhibited when Fbxo45 expression was ...
The phytohormone gibberellin (GA) controls growth and development in plants. Previously, we identified a rice F-box protein, gibberellin-insensitive dwarf2 (GID2), which is essential for GA-mediated DELLA protein degradation. In this study, we analyzed the biological and molecular biological propert …
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Predicted to be involved in positive regulation of neuron projection development. Localizes to the cytoplasm and nucleus. Orthologous to human FBXO38 (F-box protein 38 ...
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Expression of FBXW11 (BTRC2, BTRCP2, Fbw11, Fbw1b, FBXW1B, Hos, KIAA0696) in heart muscle tissue. Antibody staining with HPA072204 in immunohistochemistry.
Expression of FBXW11 (BTRC2, BTRCP2, Fbw11, Fbw1b, FBXW1B, Hos, KIAA0696) in stomach 1 tissue. Antibody staining with HPA072204 in immunohistochemistry.
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