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Relevant bibliographies by topics / Nedd4 Family E3 Ligases

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Academic literature on the topic 'Nedd4 Family E3 Ligases'

Author: Grafiati

Published: 4 June 2021

Last updated: 13 February 2022

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Journal articles on the topic "Nedd4 Family E3 Ligases"

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Jiang, Hanjie, Stefani N. Thomas, Zan Chen, Claire Y. Chiang, and Philip A. Cole. "Comparative analysis of the catalytic regulation of NEDD4-1 and WWP2 ubiquitin ligases." Journal of Biological Chemistry 294, no. 46 (October 2, 2019): 17421–36. http://dx.doi.org/10.1074/jbc.ra119.009211.

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NEDD4-1 E3 ubiquitin protein ligase (NEDD4-1) and WW domain-containing E3 ubiquitin ligase (WWP2) are HECT family ubiquitin E3 ligases. They catalyze Lys ubiquitination of themselves and other proteins and are important in cell growth and differentiation. Regulation of NEDD4-1 and WWP2 catalytic activities is important for controlling cellular protein homeostasis, and their dysregulation may lead to cancer and other diseases. Previous work has implicated noncatalytic regions, including the C2 domain and/or WW domain linkers in NEDD4-1 and WWP2, in contributing to autoinhibition of the catalytic HECT domains by intramolecular interactions. Here, we explored the molecular mechanisms of these NEDD4-1 and WWP2 regulatory regions and their interplay with allosteric binding proteins such as Nedd4 family-interacting protein (NDFIP1), engineered ubiquitin variants, and linker phosphomimics. We found that in addition to influencing catalytic activities, the WW domain linker regions in NEDD4-1 and WWP2 can impact product distribution, including the degree of polyubiquitination and Lys-48 versus Lys-63 linkages. We show that allosteric activation by NDFIP1 or engineered ubiquitin variants is largely mediated by relief of WW domain linker autoinhibition. WWP2-mediated ubiquitination of WW domain-binding protein 2 (WBP2), phosphatase and tensin homolog (PTEN), and p62 proteins by WWP2 suggests that substrate ubiquitination can also be influenced by WW linker autoinhibition, although to differing extents. Overall, our results provide a deeper understanding of the intricate and multifaceted set of regulatory mechanisms in the control of NEDD4-1–related ubiquitin ligases.

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Qian, Hao, Ying Zhang, Boquan Wu, Shaojun Wu, Shilong You, Naijin Zhang, and Yingxian Sun. "Structure and function of HECT E3 ubiquitin ligases and their role in oxidative stress." Journal of Translational Internal Medicine 8, no. 2 (June 30, 2020): 71–79. http://dx.doi.org/10.2478/jtim-2020-0012.

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AbstractUbiquitination is a modification after protein transcription that plays a vital role in maintaining the homeostasis of the cellular environment. The Homologous to E6AP C-terminus (HECT) family E3 ubiquitin ligases are a kind of E3 ubiquitin ligases with a C-terminal HECT domain that mediates the binding of ubiquitin to substrate proteins and a variable-length N-terminal extension. HECT-ubiquitinated ligases can be divided into three categories: NEDD4 superfamily, HERC superfamily, and other HECT superfamilies. HECT ubiquitin ligase plays an essential role in the development of many human diseases. In this review, we focus on the physiological and pathological processes involved in oxidative stress and the role of E3 ubiquitin ligase of the HECT family.

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An, Heeseon, David T. Krist, and Alexander V. Statsyuk. "Crosstalk between kinases and Nedd4 family ubiquitin ligases." Mol. BioSyst. 10, no. 7 (2014): 1643–57. http://dx.doi.org/10.1039/c3mb70572b.

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Understanding the interplay between kinase and E3 ligase signaling pathways will allow better understanding of therapeutically relevant pathways and the design of small molecule therapeutics targeting these pathways.

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Ikeda, Akiko, Robert G. Caldwell, Richard Longnecker, and Masato Ikeda. "Itchy, a Nedd4 Ubiquitin Ligase, Downregulates Latent Membrane Protein 2A Activity in B-Cell Signaling." Journal of Virology 77, no. 9 (May 1, 2003): 5529–34. http://dx.doi.org/10.1128/jvi.77.9.5529-5534.2003.

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ABSTRACT Nedd4 family ubiquitin protein ligases (E3s) specifically associate with latent membrane protein 2A (LMP2A) of Epstein-Barr virus. Our previous studies analyzing LMP2A function in vitro have suggested that Nedd4 family E3s regulate LMP2A function. To determine the role of Nedd4 family E3s in LMP2A B-cell signaling, LMP2A transgenic (LMP2A+) mice were crossed with mice with the Itch-deficient (Itch−/−) background. Itchy, a mouse homologue of human AIP4, is a Nedd4 family E3 and is also the most abundant Nedd4 family E3 found in LMP2A affinity precipitates from B cells. There were significantly fewer B-cell receptor-positive B cells in spleen and bone marrow B cells in LMP2A+ Itch−/− mice than in LMP2A+ mice. In addition, LMP2A+ Itch−/− bone marrow B cells formed larger colonies in cultures treated with interleukin-7 (IL-7) than control bone marrow B cells did. Finally, there was a dramatic increase in tyrosine phosphorylation of LMP2A and Syk in IL-7-cultured LMP2A+ Itch−/− B cells. These results indicate that Nedd4 family E3s, in particular Itchy, downmodulate LMP2A activity in B-cell signaling.

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Chen, Ceshi, and Lydia E. Matesic. "The Nedd4-like family of E3 ubiquitin ligases and cancer." Cancer and Metastasis Reviews 26, no. 3-4 (August 29, 2007): 587–604. http://dx.doi.org/10.1007/s10555-007-9091-x.

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Winberg, Gösta, Liudmila Matskova, Fu Chen, Pamela Plant, Daniela Rotin, Gerald Gish, Robert Ingham, Ingemar Ernberg, and Tony Pawson. "Latent Membrane Protein 2A of Epstein-Barr Virus Binds WW Domain E3 Protein-Ubiquitin Ligases That Ubiquitinate B-Cell Tyrosine Kinases." Molecular and Cellular Biology 20, no. 22 (November 15, 2000): 8526–35. http://dx.doi.org/10.1128/mcb.20.22.8526-8535.2000.

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ABSTRACT The latent membrane protein (LMP) 2A of Epstein-Barr virus (EBV) is implicated in the maintenance of viral latency and appears to function in part by inhibiting B-cell receptor (BCR) signaling. The N-terminal cytoplasmic region of LMP2A has multiple tyrosine residues that upon phosphorylation bind the SH2 domains of the Syk tyrosine kinase and the Src family kinase Lyn. The LMP2A N-terminal region also has two conserved PPPPY motifs. Here we show that the PPPPY motifs of LMP2A bind multiple WW domains of E3 protein-ubiquitin ligases of the Nedd4 family, including AIP4 and KIAA0439, and demonstrate that AIP4 and KIAA0439 form physiological complexes with LMP2A in EBV-positive B cells. In addition to a C2 domain and four WW domains, these proteins have a C-terminal Hect catalytic domain implicated in the ubiquitination of target proteins. LMP2A enhances Lyn and Syk ubiquitination in vivo in a fashion that depends on the activity of Nedd4 family members and correlates with destabilization of the Lyn tyrosine kinase. These results suggest that LMP2A serves as a molecular scaffold to recruit both B-cell tyrosine kinases and C2/WW/Hect domain E3 protein-ubiquitin ligases. This may promote Lyn and Syk ubiquitination in a fashion that contributes to a block in B-cell signaling. LMP2A may potentiate a normal mechanism by which Nedd4 family E3 enzymes regulate B-cell signaling.

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Brigui, Amira, Line Hofmann, Camilla Argüelles, Matthieu Sanial, Robert A. Holmgren, and Anne Plessis. "Control of the dynamics and homeostasis of the Drosophila Hedgehog receptor Patched by two C2-WW-HECT-E3 Ubiquitin ligases." Open Biology 5, no. 10 (October 2015): 150112. http://dx.doi.org/10.1098/rsob.150112.

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The conserved Hedgehog (HH) signals control animal development, adult stem cell maintenance and oncogenesis. In Drosophila , the HH co-receptor Patched (PTC) controls both HH gradient formation and signalling. PTC is post-translationally downregulated by HH, which promotes its endocytosis and destabilization, but the mechanisms of PTC trafficking and its importance in the control of PTC remain to be understood. PTC interacts with E3 Ubiquitin (UB)-ligases of the C2-WW-HECT family; two of them—SMURF and NEDD4—are known to regulate its levels. We demonstrate that mutation of the PTC PY motif, which mediates binding of C2-WW-HECT family members, inhibits its internalization but not its autonomous and non-autonomous signalling activities. In addition, we show that the two related UB-C2-WW-HECT ligases NEDD4 and SU(DX) regulate PTC trafficking and finely tune its accumulation through partially redundant but distinct functions. While both NEDD4 and SU(DX) promote PTC endocytosis, only SU(DX) is able to induce its lysosomal targeting and degradation. In conclusion, PTC trafficking and homeostasis are tightly regulated by a family of UB-ligases.

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Yao, Weiyi, Zelin Shan, Aihong Gu, Minjie Fu, Zhifeng Shi, and Wenyu Wen. "WW domain–mediated regulation and activation of E3 ubiquitin ligase Suppressor of Deltex." Journal of Biological Chemistry 293, no. 43 (September 13, 2018): 16697–708. http://dx.doi.org/10.1074/jbc.ra118.003781.

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The Nedd4 family E3 ligases Itch and WWP1/2 play crucial roles in the regulation of cell cycle progression and apoptosis and are closely correlated with cancer development and metastasis. It has been recently shown that the ligase activities of Itch and WWP1/2 are tightly regulated, with the HECT domain sequestered intramolecularly by a linker region connecting WW2 and WW3. Here, we show that a similar autoinhibitory mechanism is utilized by the Drosophila ortholog of Itch and WWP1/2, Suppressor of Deltex (Su(dx)). We show that Su(dx) adopts an inactive steady state with the WW domain region interacting with the HECT domain. We demonstrate that both the linker and preceding WW2 are required for the efficient binding and regulation of Su(dx) HECT. Recruiting the multiple-PY motif–containing adaptor dNdfip via WW domains relieves the inhibitory state of Su(dx) and leads to substrate (e.g. Notch) ubiquitination. Our study demonstrates an evolutionarily conservative mechanism governing the regulation and activation of some Nedd4 family E3 ligases. Our results also suggest a dual regulatory mechanism for specific Notch down-regulation via dNdfip–Su(dx)–mediated Notch ubiquitination.

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Kotorashvili, Adam, Scott J. Russo, Surafel Mulugeta, Susan Guttentag, and Michael F. Beers. "Anterograde Transport of Surfactant Protein C Proprotein to Distal Processing Compartments Requires PPDY-mediated Association with Nedd4 Ubiquitin Ligases." Journal of Biological Chemistry 284, no. 24 (April 14, 2009): 16667–78. http://dx.doi.org/10.1074/jbc.m109.002816.

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Biosynthesis of surfactant protein C (SP-C) by alveolar type 2 cells requires proteolytic processing of a 21-kDa propeptide (proSP-C21) in post-Golgi compartments to yield a 3.7-kDa mature form. Scanning alanine mutagenesis, binding assays, and co-immunoprecipitation were used to characterize the proSP-C targeting domain. Delivery of proSP-C21 to distal processing organelles is dependent upon the NH2-terminal cytoplasmic SP-C propeptide, which contains a conserved PPDY motif. In A549 cells, transfection of EGFP/proSP-C21 constructs containing polyalanine substitution for Glu11–Thr18, 13PPDY16, or 14P,16Y produced endoplasmic reticulum retention of the fusion proteins. Protein-protein interactions of proSP-C with known WW domains were screened using a solid-phase array that revealed binding of the proSP-C NH2 terminus to several WW domains found in the Nedd4 family of E3 ligases. Specificity of the interaction was confirmed by co-immunoprecipitation of proSP-C and Nedd4 or Nedd4-2 in epithelial cell lines. By Western blotting and reverse transcription-PCR, both forms were detected in primary human type 2 cells. Knockdown of Nedd4-2 by small interference RNA transfection of cultured human type 2 cells blocked processing of 35S-labeled proSP-C21. Mutagenesis of potential acceptor sites for ubiquitination in the cytosolic domain of proSP-C (Lys6, Lys34, or both) failed to inhibit trafficking of EGFP/proSP-C21. These results indicate that PPDY-mediated interaction with Nedd4 E3-ligases is required for trafficking of proSP-C. We speculate that the Nedd4/proSP-C tandem is part of a larger protein complex containing a ubiquitinated component that further directs its transport.

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Ingham, Robert J., Gerald Gish, and Tony Pawson. "The Nedd4 family of E3 ubiquitin ligases: functional diversity within a common modular architecture." Oncogene 23, no. 11 (March 2004): 1972–84. http://dx.doi.org/10.1038/sj.onc.1207436.

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Dissertations / Theses on the topic "Nedd4 Family E3 Ligases"

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Ruetalo, Buschinger Natalia [Verfasser], and Silke [Akademischer Betreuer] Wiesner. "Mechanisms underlying the regulation of Nedd4-family E3 Ubiquitin ligases / Natalia Ruetalo Buschinger ; Betreuer: Silke Wiesner." Tübingen : Universitätsbibliothek Tübingen, 2020. http://d-nb.info/1202774091/34.

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Escobedo, Pascual Albert. "Structural Insights into Substrate Binding and Regulation of E3 Ubiquitin Ligases in the Nedd4 Family using NMR Spectroscopy." Doctoral thesis, Universitat de Barcelona, 2014. http://hdl.handle.net/10803/284605.

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Nedd4L is a HECT-type E3 ubiquitin ligase (it covalently binds ubiquitin molecules before transferring them to the final substrate). Ubiquitination is a posttranslational modification (PTM) that labels proteins for a variety of fates, the most relevant one being proteasome-mediated degradation. Nedd4L is responsible for the regulation of the turnover of the sodium channel ß-ENaC as well as Smad2/3, mediator proteins of the signalling pathway activated by TGF-ß-like cytokines. It also targets the TGF-ß receptor itself. Defects in its function have been related to hereditary hypertension (Liddle’s syndrome), and could be relevant in certain sorts of cancer and metastasis. CDK8/9 and GSK3-ß are two kinases that regulate the phosphorylation of the Smads, enabling them to carry out their function in cooperation with transcription factors and other partner proteins. At the same time, they label the Smads for their recognition by ubiquitin ligases. This provides the cell with a mechanism to give a transient response to the cytokines of the TGF-ß type. In order to identify the residues and the phosphorylation patterns that are relevant for the interactions of the Smads with both the transcription factors and the ubiquitin ligases, we have prepared a set of phosphopeptides corresponding to the sequences of Smad1 and Smad3. Like all other members of the Nedd4 family, Nedd4L has a multi-domain architecture of the type C2-WW-HECT. Several ligases of the family exist in a latent conformation established through inter-domain contacts that occlude the catalytic site in the HECT domain, involving either the C2 domain (Smurf1, Smurf2, WWP2, Nedd4, Nedd4L) or the central segment where the WW domains are located (Itch). Certain cellular events displace these contacts, inducing the transition to the active conformation. In the case of Nedd4L, increases of the intracellular levels of Ca2+ activate the ligase. The hydrolysis of the membrane phospholipid phosphatidylinositol 4,5-bisphosphate (PIP2) delivers into the cytosol the inositol 1,4,5-triphosphate (IP3), a second messenger that mobilizes the intracellular Ca2+ reserves. The C2 domain of Nedd4L interacts both with Ca2+ ions and with IP3. Using a structural and biophysical approach based on Nuclear Magnetic Resonance (NMR) we have described the specific interactions between the HECT and C2 domains that inhibit the catalytic function. Ca2+ binds the C2 domain with high affinity using the same binding surface and compromises these contacts. In addition, it mediates the interaction with IP3. These results provide the structural fundament for the activation and the relocation to the plasma membrane of Nedd4L mediated by Ca2+. The HECT domain has a highly conserved PY site (HECT-PY). The PY motifs are the sequences recognized by WW domains. Central to this recognition is the coordination of the tyrosine residue in the PY motif by the WW domain. In the crystallographic structure of the Nedd4L HECT domain the tyrosine residue of the HECT-PY motif appears buried in the hydrophobic core and not accessible for binding. It has been shown that the WW domains of Nedd4L recognize the HECT-PY motif of the ligase only after the unfolding of the HECT domain. We raised the hypothesis that the recognition of the HECT-PY motif by one of Nedd4L WW domains may play a role in the auto-ubiquitination mechanism of the ligase. Our data confirm that only when the fold of the HECT domain is partially damaged, the PY site is accessible for being recognized by the WW domains. We present the NMR solution structure of the complex between the WW3 domain and the HECT-PY motif. The site is protected in functional Nedd4L molecules, which are able to recognize it in damaged molecules and label them with ubiquitin for degradation.
Nedd4L és una E3 ubiquitín lligasa responsable de la regulació de la vida mitja del canal de sodi ß-ENaC i de Smad2/3, proteïnes mediadores de la ruta de senyalització activada per citocines TGF-ß. Defectes en la seva funció han estat relacionats amb la hipertensió hereditària (Síndrome de Liddle), i podrien ser rellevants en determinats tipus de càncer i metàstasi. CDK8/9 i GSK3-ß són dues quinases que regulen l’estat de fosforilació de les Smads, habilitant-les per dur a terme llur funció en cooperació amb factors de transcripció al mateix temps que les marquen per ser reconegudes per ubiquitín lligases. Amb l’objectiu d’identificar els residus i els patrons de fosforilació rellevants hem preparat un set de fosfopèptids que corresponen a les seqüències de Smad1/3. Nedd4L presenta una arquitectura multi-domini C2-WW-HECT. Diverses lligases de la família de Nedd4 existeixen en una conformació latent en què contactes inter-domini oclouen el lloc catalític en el domini HECT, involucrant bé el domini C2 (Smurf1/2, WWP2, Nedd4, Nedd4L) o la zona central amb els dominis WW (Itch). Certs esdeveniments cel•lulars desplacen aquests contactes, induint la transició a la conformació activa. L’increment dels nivells intracel•lulars de Ca2+ activa Nedd4L. La hidròlisi del fosfolípid de membrana PIP2 allibera l’IP3 provocant aquest increment. El domini C2 de Nedd4L interacciona tant amb el Ca2+ com amb l’IP3. Utilitzant l’RMN hem descrit els contactes HECT-C2 en la conformació latent i hem observat que el Ca2+ s’uneix al domini C2 amb alta afinitat utilitzant el mateix lloc d’unió, a més d’afavorir la interacció amb l’IP3. Així, hem aportat el fonament estructural per a l’activació i relocalització a la membrana cel•lular de Nedd4L. El domini HECT presenta un lloc PY altament conservat (HECT-PY). Els motius PY són reconeguts pels dominis WW. Proposem que el reconeixement del motiu HECT-PY per part d’un dels dominis WW de Nedd4L estigui implicat en l’auto-ubiquitinació. Hem observat que només quan el plegament del domini HECT està compromès, el lloc PY és accessible. Presentem l’estructura per RMN del complex WW3-HECT-PY. El motiu està protegit en molècules funcionals de Nedd4L, capaces de reconèixer-lo en molècules danyades i ubiquitinar-les.

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Altas, Bekir [Verfasser], Nils [Akademischer Betreuer] Brose, Judith [Gutachter] Stegmüller, and Dirk [Gutachter] Goerlich. "Roles of the Nedd4 Family E3 Ligases in Glial Function and Nerve Cell Development / Bekir Altas ; Gutachter: Judith Stegmüller, Dirk Goerlich ; Betreuer: Nils Brose." Göttingen : Niedersächsische Staats- und Universitätsbibliothek Göttingen, 2017. http://d-nb.info/1131875710/34.

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Takeda, Michiko [Verfasser], Hiroshi [Akademischer Betreuer] Kawabe, Nils [Akademischer Betreuer] Brose, and Andreas [Akademischer Betreuer] Stumpner. "The Role of the E3 Ubiquitin Ligases Nedd4-1 and Nedd4-2 in Synaptic Transmission and Plasticity / Michiko Takeda. Gutachter: Nils Brose ; Andreas Stumpner. Betreuer: Hiroshi Kawabe." Göttingen : Niedersächsische Staats- und Universitätsbibliothek Göttingen, 2013. http://d-nb.info/104430779X/34.

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Napolitano, Luisa Maria Rosaria. "The TRIM (TRipartite Motif) family as a novel class of ubiquitin E3 ligases." Thesis, Open University, 2011. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.543857.

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Hsia, Hung-En [Verfasser], Hiroshi [Akademischer Betreuer] Kawabe, Nils [Akademischer Betreuer] Brose, Judith [Akademischer Betreuer] Stegmüller, and Andreas [Akademischer Betreuer] Wodarz. "Roles of the HECT-Type Ubiquitin E3 Ligases of the Nedd4 and WWP Subfamilies in Neuronal Development / Hung-En Hsia. Gutachter: Nils Brose ; Judith Stegmüller ; Andreas Wodarz. Betreuer: Hiroshi Kawabe." Göttingen : Niedersächsische Staats- und Universitätsbibliothek Göttingen, 2015. http://d-nb.info/1071713493/34.

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Malbert-Colas, Laurence. "Recherche et identification de partenaires du canal épithélial à sodium ENaC : étude du rôle potentiel de ces partenaires dans la régulation de l'activité de ENaC." Paris 7, 2003. http://www.theses.fr/2003PA077168.

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Gabrielli, Lisa Marie. "Regulation of the 3BP2 Adaptor Protein by the Nedd4 Family of HECT E3 Ubiquitin Ligases." Thesis, 2009. http://hdl.handle.net/1807/18292.

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3BP2 has been previously described as the protein mutated in the osteoporotic disorder, Cherubism. The gain of function mutation that characterizes Cherubism is the result of an uncoupling of its interaction with Tankyrase 2, which has been reported to stimulate 3BP2 ubiquitination. Here we describe an attempt at identifying the E3 ligase responsible for mediating this ubiquitination using four candidate members from the Nedd4 family. Based on their respective abilities to bind and ubiquitinate 3BP2, as well as their sensitivity to the presence of Tankyrase 2 and to 3BP2 mutations (including Cherubism mutations and mutations within the 3BP2 PPxY motif thought to confer binding to the Nedd4 proteins), we have determined that Smurf1 best fits our model. Further supporting these findings, we have seen an elevation in 3BP2 protein levels in macrophages derived from Smurf1-/-/Smurf2+/- mice. This work supports a role for the Nedd4 family member, Smurf1, in mediating 3BP2 ubiquitination.

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Altas, Bekir. "Roles of the Nedd4 Family E3 Ligases in Glial Function and Nerve Cell Development." Doctoral thesis, 2016. http://hdl.handle.net/11858/00-1735-0000-0023-3E3B-D.

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Takeda, Michiko. "The Role of the E3 Ubiquitin Ligases Nedd4-1 and Nedd4-2 in Synaptic Transmission and Plasticity." Doctoral thesis, 2012. http://hdl.handle.net/11858/00-1735-0000-001D-AE3A-7.

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Nervenzellen sind hochspezialisierte Zellen, die an Synapsen miteinander verbunden sind, was die Übertragung von neuronalen Informationen erlaubt. Die Entwicklung von Synapsen und die Informationsverarbeitung und Gedächtnisbildung bei reifen Synapsen erfordert eine dynamische Umorganisation von neuronalen Netzwerken. Das beinhaltet die Bildung und Entfernung von Synapsen, Umsatz von synaptischen Proteinen und die Veränderung und Anpassung von synaptischer Erregungsübertragung. U. a. Ubiquitinierung, als regulatorische, posttranslationale Modifikation von Proteinen, könnte eine entscheidende Rolle für solche komplexe, synaptische Umorganisationen spielen. Nedd4-1, eine HECT-Typ E3 Ubiquitin Ligase, reguliert und fördert die Entwicklung von Nervenzellfortsätzen durch die Ubiquitinierung von Rap2. Um die Bedeutung von Nedd4-abhänginger Ubiquitinierung im entwickelten Gehirn zu untersuchen, wurden Mausmodelle generiert und analysiert, in denen Nedd4-1 und dessen nächstes Homolog Nedd4-2, speziell in Nervenzellen ausgeschaltet wurde. Ich habe herausgefunden, dass Nedd4-1 und Nedd4-2 wichtige regulatorische Proteine für die neuronale Morphogenese und die synaptische Plastizität, insbesondere die Aufrechterhaltung von LTP, darstellen. Desweiteren habe ich festgestellt, dass Synaptopodin (SYNPO), ein Prolin-reiches, Aktin-assoziiertes Protein, von Nedd4-1 und Nedd4-2 in vitro ubiquitiniert wird. Dieses Ergebnis deutet daraufhin, dass SYNPO in dem Mechanismus eine Rolle spielt, durch den Nedd4-1 und Nedd4-2 LTP aufrechterhalten. Diese Studie wirft ein neues Licht auf die funktionelle Rolle von Nedd4-abhänginger Ubiquitinierung bei höheren Funktionen des Gehirns von Säugetieren sowie der neuronalen Entwicklung.

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Book chapters on the topic "Nedd4 Family E3 Ligases"

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Butt, Ghazala, Ilhan Yaylim, Rukset Attar, Aliye Aras, Mirna Azalea Romero, Muhammad Zahid Qureshi, Jelena Purenovic, and Ammad Ahmad Farooqi. "NEDD4 Family of E3 Ubiquitin Ligases in Breast Cancer: Spotlight on SMURFs, WWPs and NEDD4." In Advances in Experimental Medicine and Biology, 365–75. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-20301-6_19.

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Nguyen, Khai M., and Luca Busino. "The Biology of F-box Proteins: The SCF Family of E3 Ubiquitin Ligases." In Advances in Experimental Medicine and Biology, 111–22. Singapore: Springer Singapore, 2020. http://dx.doi.org/10.1007/978-981-15-1025-0_8.

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I. Kane, Emma, and Donald E. Spratt. "New Discoveries on the Roles of “Other” HECT E3 Ubiquitin Ligases in Disease Development." In Ubiquitin - Proteasome Pathway. IntechOpen, 2020. http://dx.doi.org/10.5772/intechopen.91770.

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HECT E3 ubiquitin ligases selectively recognize, bind, and ubiquitylate their substrate proteins to target them for 26S proteasomal degradation. There is increasing evidence that HECT E3 ubiquitin ligase dysfunction due to misfolding and/or the gene encoding the protein being mutated is responsible for the development of different diseases. Apart from the more prominent and well-characterized E6AP and members of the NEDD4 family, new studies have begun to reveal how other members of the HECT E3 ubiquitin ligase family function as well as their links to disease and developmental disorders. This chapter provides a comprehensive discussion on the more mysterious members of the HECT E3 ubiquitin ligase family and how they control intracellular processes. Specifically, AREL1, HACE1, HECTD1, HECTD4, G2E3, and TRIP12 will be examined as these enzymes have recently been identified as contributors to disease development.

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Conference papers on the topic "Nedd4 Family E3 Ligases"

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Knudsen, LM, A. Sveen, CH Bergsland, MB Five, NL Rasmussen, MZ Totland, PW Eide, J. Bruun, RA Lothe, and E. Leithe. "PO-127 Role of the NEDD4 family of E3 ubiquitin ligases in colorectal cancer pathogenesis and their potential as biomarkers." In Abstracts of the 25th Biennial Congress of the European Association for Cancer Research, Amsterdam, The Netherlands, 30 June – 3 July 2018. BMJ Publishing Group Ltd, 2018. http://dx.doi.org/10.1136/esmoopen-2018-eacr25.168.

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Sciver, Robert E. Van, Yajun Cao, Atique U. Ahmed, and Amy H. Tang. "Abstract 83: The critical role of seven-in-absentia (SINA) family E3 ligases in normal development and oncogenic K-RAS-driven human cancer." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-83.

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Sciver, Robert E. Van, Yajun Cao, Atique U. Ahmed, and Amy H. Tang. "Abstract 83: The critical role of seven-in-absentia (SINA) family E3 ligases in normal development and oncogenic K-RAS-driven human cancer." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-83.

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