المؤلفون: Yonglong Chen, Shijie Fan, Xuan Zheng, Chenghua Li, Yougong Peng, Hanbing He

المصدر: FEBS Letters. 592:2334-2340

مصطلحات موضوعية: 0301 basic medicine, Potassium Channels, Ubiquitin-Protein Ligases, Biophysics, Regulator, Biochemistry, 03 medical and health sciences, Structural Biology, Genetics, Humans, Monoubiquitination, Molecular Biology, Cells, Cultured, chemistry.chemical_classification, DNA ligase, Chemistry, Tumor Suppressor Proteins, Ubiquitination, Cell Biology, Cullin Proteins, Potassium channel, Cell biology, HEK293 Cells, 030104 developmental biology, Protein Multimerization, Protein Binding, Transcription Factors

الوصف: Potassium channel tetramerization domain containing 5 (KCTD5) was previously documented as a component of the Cullin3-RING ligase (CRL3). It has been reported that KCTD5 can induce enrichment of polyubiquitinated proteins, and KCTD5-based CRL3 destabilizes several proteins. In our present study, we report that KCTD5 may physically interact with ΔNp63α, which is a member of the p53 family. Our further investigation revealed that Cullin3/KCTD5 can induce monoubiquitination of ΔNp63α. Cullin3/KCTD5 downregulates the DNA-binding affinity of ΔNp63α, impairing either its transactivity or its transinhibitory activity. Functionally, Cullin3/KCTD5 abates the proproliferation activity of ΔNp63α. These findings suggest that KCTD5-based CRL3 may mediate monoubiquitination and is a novel regulator of ΔNp63α.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::123d54596d13ef5913eba69b225475f4Test
https://doi.org/10.1002/1873-3468.13104Test

المؤلفون: Eric S. Fischer, Simone Cavadini, Gondichatnahalli M. Lingaraju, Kerstin Böhm, Andrea Scrima, Nicolas H. Thomä

المصدر: FEBS Letters. 585:2818-2825

مصطلحات موضوعية: DNA Repair, Ultraviolet Rays, DNA damage, DNA repair, Ubiquitin-Protein Ligases, Biophysics, DDB2, Computational biology, CSA, Biochemistry, Genome, DDB1, CUL4, Structural Biology, Genome stability, Genetics, Humans, Receptor, Molecular Biology, Models, Genetic, biology, Genome, Human, Nuclear Proteins, Cell Biology, Cullin Proteins, Ubiquitin ligase, DNA-Binding Proteins, DNA Repair Enzymes, biology.protein, CDT2, Function (biology), DNA Damage, Transcription Factors, Nucleotide excision repair

الوصف: The DDB1–DDB2–CUL4–RBX1 complex serves as the primary detection device for UV-induced lesions in the genome. It simultaneously functions as a CUL4 type E3 ubiquitin ligase. We review the current understanding of this dual function ubiquitin ligase and damage detection complex. The DDB2 damage binding module is merely one of a large family of possible DDB1–CUL4 associated factors (DCAF), most of which are substrate receptors for other DDB1–CUL4 complexes. DDB2 and the Cockayne-syndrome A protein (CSA) function in nucleotide excision repair, whereas the remaining receptors operate in a wide range of other biological pathways. We will examine the modular architecture of DDB1–CUL4 in complex with DDB2, CSA and CDT2 focusing on shared architectural, targeting and regulatory principles.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e6dfe0ae0e3f36b58b26b5ad323ae856Test
https://doi.org/10.1016/j.febslet.2011.04.064Test

المؤلفون: Minsoo Kim, Toru Suzuki, Tadashi Yamamoto, Yoshinori Abe, Sumio Sugano, Yutaka Yoshida, Makoto Watanabe

المصدر: FEBS Letters. 585:65-70

مصطلحات موضوعية: Immunoprecipitation, Ubiquitin-Protein Ligases, Immunoblotting, Biophysics, Plasma protein binding, Transfection, Biochemistry, Mice, Ubiquitin, Structural Biology, Two-Hybrid System Techniques, Chlorocebus aethiops, Skp1, Genetics, SKP2, Animals, Humans, Tob, Amino Acids, Coronin7, Molecular Biology, E3 ligase, Binding Sites, COS cells, biology, Tumor Suppressor Proteins, Microfilament Proteins, Ubiquitination, Cell Biology, Cullin Proteins, Ubiquitin ligase, Cell biology, HEK293 Cells, COS Cells, biology.protein, Carrier Proteins, Cullin, Protein Binding

الوصف: Tob belongs to the anti-proliferative Tob/BTG family. The level of Tob throughout the cell cycle is regulated by the SCF (Skp1/Cullin/F-box protein)Skp2 ubiquitin ligase (E3) complex. Here, we show that Coronin7 (CRN7) is also involved in Tob degradation. We identified CRN7 as a Tob-interacting molecule. A sequence containing two of the six WD motifs in the middle of CRN7 was responsible for the interaction. CRN7 enhanced the polyubiquitination of Tob in vitro, and overexpression of CRN7 promoted proteasome-dependent degradation of Tob. Furthermore, CRN7 interacted with Cullin1 and Roc1 to form a novel SCF-like E3 complex, suggesting that Tob protein is regulated by multiple ubiquitination machineries. Structured summary Cullin1 physically interacts with CRN7 : shown by anti tag coimmunoprecipitation ( view interaction ) Roc1 physically interacts with CRN7 : shown by anti tag coimmunoprecipitation ( view interaction ) CRN7 physically interacts with Tob1 : shown by anti tag coimmunoprecipitation ( view interaction ) CDC34 physically interacts with CRN7 : shown by anti tag coimmunoprecipitation ( view interaction ) Tob1 and CRN7 colocalize : shown by fluorescence microscopy ( view interaction ) Elongin B physically interacts with CRN7 : shown by anti tag coimmunoprecipitation ( view interaction ) Elongin C physically interacts with CRN7 : shown by anti tag coimmunoprecipitation ( view interaction ) Tob1 physically interacts with CRN7 : shown by two hybrid ( view interaction )

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7853857d0801d36ef6d4023fa5893298Test
https://doi.org/10.1016/j.febslet.2010.11.049Test

المؤلفون: Takaaki Nakamura, Yasuhiko Masuho, Takehiro Nishiyama, Junya Kohroki

المصدر: FEBS letters. 579(30)

مصطلحات موضوعية: ASB, RBX1, Ubiquitin-Protein Ligases, Blotting, Western, DNA Mutational Analysis, Molecular Sequence Data, Biophysics, Suppressor of Cytokine Signaling Proteins, Transfection, Biochemistry, Cell Line, Ligases, Ubiquitin, Structural Biology, Cul5, Genetics, Escherichia coli, Humans, Ligase activity, Amino Acid Sequence, Molecular Biology, chemistry.chemical_classification, DNA ligase, biology, Sequence Homology, Amino Acid, Cell Biology, Rbx2, Cullin Proteins, Precipitin Tests, Recombinant Proteins, Ubiquitin ligase, Ankyrin Repeat, Repressor Proteins, chemistry, SOCS box, Mutation, biology.protein, Ankyrin repeat, Carrier Proteins, CUL5, Cullin

الوصف: The ankyrin repeat and SOCS box (ASB) family is composed of 18 proteins from ASB1 to ASB18 and belongs to the suppressor of cytokine signaling (SOCS) box protein superfamily. ASB2 was recently shown to interact with a certain Cul–Rbx module to form an E3 ubiquitin (Ub) ligase complex, but the functional composition of the ASB-containing E3 Ub ligase complexes remains to be characterized. Here, we show that ASB proteins interact with Cul5–Rbx2 but neither Cul2 nor Rbx1 in cells. Mutational analysis revealed that the highly conserved amino acid sequences of the BC box and Cul5 box in the SOCS box of ASB proteins were essential for the interaction with Cul5–Rbx2. Although ASB proteins show slight divergences from the consensus sequences of the BC box and Cul5 box, all five tested ASB proteins bound to Cul5–Rbx2. Furthermore, all three tested ASB complexes containing Cul5–Rbx2 were found to have E3 Ub ligase activity. These findings suggest that the ASB family proteins interact with Cul5–Rbx2 to form E3 Ub ligases and play significant roles via a ubiquitination-mediated pathway.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b33de4f8515f154288416ea6e9f85309Test
https://pubmed.ncbi.nlm.nih.gov/16325183Test

المؤلفون: Mamoru Fukuda, Hirotaka Koizumi, Tomohiko Ohta, Ichiro Maeda

المصدر: FEBS letters. 494(3)

مصطلحات موضوعية: Cyclin E, Macromolecular Substances, Cyclin D, Ubiquitin-Protein Ligases, Cyclin A, Biophysics, Cyclin B, SKP1–CUL1(CDC53)–F-box protein complex, Cell Cycle Proteins, Antigen-Antibody Complex, Biochemistry, Anaphase-Promoting Complex-Cyclosome, Cullin, Cell Line, Ligases, Cyclin D1, Structural Biology, Genetics, Humans, Molecular Biology, Ubiquitins, biology, Ubiquitin-Protein Ligase Complexes, Zinc Fingers, Cell Biology, ROC1, Cullin Proteins, Molecular biology, Precipitin Tests, Ubiquitin ligase, Protein Subunits, Mutation, Ubiquitin-Conjugating Enzymes, biology.protein, Cyclin-dependent kinase complex, Cyclin A2, Protein Binding

الوصف: Overexpression of cyclin D1 has been implicated in a variety of tumors, such as breast cancers, gastrointestinal cancers and lymphomas. Both gene amplification and protein degradation mediated by ubiquitin (Ub)-dependent proteolysis regulate the abundance of cyclin D1. Here we report that ROC1 interacted with all three D type cyclins in vivo but did not bind to other cyclins tested. The ROC1–CUL1 and ROC1–CUL3, but not ROC1–CUL2, –CUL3 and –CUL4, immunocomplexes promoted polyubiquitination of bacterially purified cyclin D1 in vitro. RING finger mutations of ROC1 eliminated the Ub ligase activity toward cyclin D1. In all cases the ubiquitination of cyclin D1 was accompanied by autoubiquitination of the cullins. The results suggest the involvement of ROC1–cullin ligases in cyclin D1 ubiquitination and a potential mechanism whereby the cullin subunit is ubiquitinated itself while ubiquitinating a substrate.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::72fa362ef3a7761f1ee2d9a8c7e5f267Test
https://pubmed.ncbi.nlm.nih.gov/11311237Test

المؤلفون: H, Suzuki, M, Kobayashi, M, Takeuchi, K, Furuichi, T, Chiba, K, Tanaka

المصدر: FEBS letters. 458(3)

مصطلحات موضوعية: SKP Cullin F-Box Protein Ligases, Tumor Necrosis Factor-alpha, Blotting, Western, Cell Cycle Proteins, Cullin Proteins, Precipitin Tests, Neoplasm Proteins, DNA-Binding Proteins, NF-KappaB Inhibitor alpha, Humans, I-kappa B Proteins, Salts, Peptide Synthases, Phosphorylation, S-Phase Kinase-Associated Proteins, Ubiquitins, HeLa Cells, Protein Binding

الوصف: Destruction of IkappaB by ubiquitinylation is required for signal-dependent activation of NF-kappaB. The IkappaB alpha ubiquitin-ligase activity associated with phosphorylated IkappaB alpha (pIkappaB alpha) in HeLa cells was almost completely lost by washing under stringent conditions including 1 M NaCl; nevertheless, an SCF(betaTrCP) complex containing Skp1, Cullin-1, and F-box/WD40 protein betaTrCP was still bound to pIkappaB alpha, suggesting the existence of a putative factor that is loosely associated with pIkappaB alpha and may collaborate with SCF(betaTrCP). The factor was named IkappaB alphaE3-F1 and was partially purified from HeLa cells. Gel filtration analysis revealed that IkappaB alphaE3-F1 has an apparent molecular mass of approximately 300 kDa.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=pmid________::f484b5f9130419c658faffb8322330f4Test
https://pubmed.ncbi.nlm.nih.gov/10570937Test

المؤلفون: Cain H. Yam, Randy Yat Choi Poon, Raymond Wai Man Ng, Talha Arooz, Iris W.Y. Chan, Anita Wan Sze Lau

المصدر: FEBS letters. 438(3)

مصطلحات موضوعية: Repetitive Sequences, Amino Acid, Protein Conformation, Recombinant Fusion Proteins, Biophysics, Cell Cycle Proteins, Biochemistry, F-box protein, Cell Line, Ligases, Degradation, Ubiquitin, Structural Biology, Cyclin-dependent kinase, Skp1, Genetics, Animals, Humans, Molecular Biology, S-Phase Kinase-Associated Proteins, Gene Library, Mammals, biology, Kinetochore, Cell Cycle, Ubiquitination, Cell Biology, Cell cycle, Cullin Proteins, Cyclin, Recombinant Proteins, Kinetics, biology.protein, Chromatography, Gel, Dimerization, Function (biology), Cullin

الوصف: Skp1 interacts with cullins, F-box containing proteins, and forms a complex with cyclin A-Cdk2 in mammalian cells. Skp1 is also involved in diverse biological processes like degradation of key cell cycle regulators, glucose sensing, and kinetochore function. However, little is known about the structure and exact function of Skp1. Here we characterized the interaction between Skp1 and the F-box protein Skp2. We show that Skp1 can bind to Skp2 in vitro using recombinant proteins, and in vivo using the yeast two-hybrid system. Deletion analysis of Skp1 indicated that most of the Skp1 protein is required for binding to Skp2. In mammalian cell extracts, a large portion of Skp1 appears to associate with proteins other than Skp2. Biochemical analysis indicated that Skp1 is likely to be a flexible, non-spherical protein, and is capable of forming dimers.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c6782386dd0c42070ef74876d5a23a16Test
https://pubmed.ncbi.nlm.nih.gov/9827542Test

المؤلفون: David Girdwood, Morag Robertson, Colin Gordon

المصدر: FEBS Letters. (10):1522-1528

مصطلحات موضوعية: Molecular Sequence Data, Biophysics, macromolecular substances, Biochemistry, NEDD8, Pcu1, Ligases, Uba3, Ubiquitin, Structural Biology, Schizosaccharomyces, Genetics, Ligase activity, Molecular Biology, DNA Primers, Base Sequence, biology, Cullin Proteins, fungi, Cell Biology, biology.organism_classification, enzymes and coenzymes (carbohydrates), Schizosaccharomyces pombe, embryonic structures, biology.protein, Schizosaccharomyces pombe Proteins, Neddylation, Cullin-RING-Ligase, Cullin

الوصف: In fission yeast, the only known essential function of Ned8p is the modification of the cullin, Pcu1p, and subsequent Cullin-RING-Ligase (CRL) activation and substrate ubiquitination. We show here that a functional Pcu1p mutant, deleted for its C-terminal autoinhibitory domain, which negates the requirement of neddylation for ligase activity, is unable to rescue the loss of neddylation. These findings suggest that the neddylation of non-cullin substrate(s) are required for Schizosaccharomyces pombe viability.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1bf854de504288e1bab7c0ef3197da1bTest

المؤلفون: Taka aki Tamura, Jong Bok Yoon, Jiwon Hwang, Kyoeng Woo Min

المصدر: FEBS Letters. (1-3):102-108

مصطلحات موضوعية: NEDD8 Protein, Macromolecular Substances, Ubiquitin-Protein Ligases, Biophysics, Cell Cycle Proteins, Biochemistry, NEDD8, Ligases, CUL1, Skp1-Cdc53/cullin-F box, Structural Biology, Skp1, Genetics, Humans, Neddylation, Molecular Biology, Ubiquitins, Binding Sites, biology, Ubiquitin, Cullin Proteins, Cell Biology, Ubiquitin ligase, Cell biology, Protein Structure, Tertiary, Nedd8, E3 ubiquitin ligase, biology.protein, Carrier Proteins, Cullin, HeLa Cells, Protein Binding, Transcription Factors

الوصف: The cullin-containing E3 ubiquitin ligases play an important role in regulating the abundance of key proteins involved in cellular processes such as cell cycle and cytokine signaling. We recently identified TIP120A as a cullin-interacting protein and found that TIP120A functions as a negative regulator of a ubiquitin ligase by interfering with the binding of Skp1 and an F box protein to CUL1. Here we show that TIP120A binds to the unneddylated CUL1 but not the neddylated one. The association of TIP120A with CUL1 requires both the N-terminal stalk and the C-terminal globular domain of CUL1. TIP120A efficiently inhibits neddylation of CUL1 but does not affect substrate-independent ubiquitination by CUL1/Rbx1, implying that it blocks the access of Nedd8 to the conjugation site but does not interfere with the interaction of the ubiquitin-conjugating enzyme with Rbx1. Our data suggest that the association/dissociation of TIP120A coupled to neddylation/deneddylation of CUL1 may play an important role in assembly and disassembly of Skp1-Cdc53/cullin-F box ubiquitin ligases.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33f44c9a339616e3a81191b878741e69Test

المؤلفون: Atsushi Higashitani, Yohei Sasagawa, Teru Ogura, Shusei Sato

المصدر: FEBS Letters. (1):145-150

مصطلحات موضوعية: Ubiquitin-Protein Ligases, Mutant, Biophysics, Protein Serine-Threonine Kinases, Cullin-5/VCAM-1, Biochemistry, Oogenesis, Animals, Genetically Modified, Structural Biology, Genetics, medicine, Animals, RNA, Small Interfering, Caenorhabditis elegans, Caenorhabditis elegans Proteins, Molecular Biology, Mitogen-Activated Protein Kinase 1, cul-5, biology, rbx-2, Cell Biology, Cullin Proteins, Oocyte, Phenotype, Yeast, cul-2, Ubiquitin ligase, Cell biology, Enzyme Activation, medicine.anatomical_structure, Multiprotein Complexes, Mitogen-activated protein kinase, Mutation, Oocytes, biology.protein, Female, Pachytene Stage, Ovoviviparity, CUL5

الوصف: Cul5-based complex is a member of ECS (Elongin B/C-Cul2/Cul5-SOCS-box protein) ubiquitin ligase family. The cellular function of the Cul5-based complex is poorly understood. In this study, we found that oocyte septum formation and egg production did not occur in either cul-5- or rbx-2-depleted cul-2 homozygotes, although control cul-2 homozygotes laid approximately 50 eggs. These phenotypes are reminiscent of those caused by the MAP kinase mpk-1 depletion. In fact, activation of MPK-1 was significantly inhibited in cul-5-depleted cul-2 mutant and cul-2-depleted cul-5 mutant. Yeast two-hybrid analysis and RNAi-knockdown experiments suggest that oocyte maturation from pachytene exit and MPK-1 activation are redundantly controlled by the RBX-2-CUL-5- and RBX-1-CUL-2-based complexes.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::58bbdaf03e14356415b1b0525adb735cTest