USP8 prevents aberrant NF-κB and Nrf2 activation by counteracting ubiquitin signals from endosomes

Authors: Akinori Endo, Toshiaki Fukushima, Chikage Takahashi, Hikaru Tsuchiya, Fumiaki Ohtake, Sayaka Ono, Tony Ly, Yukiko Yoshida, Keiji Tanaka, Yasushi Saeki, Masayuki Komada

Source: J Cell Biol

Subject Terms: 0301 basic medicine, 0303 health sciences, Kelch-Like ECH-Associated Protein 1, Endosomal Sorting Complexes Required for Transport/genetics, Endosomal Sorting Complexes Required for Transport, NF-E2-Related Factor 2, Ubiquitin, NF-kappa B/genetics, NF-kappa B, Endosomes/genetics, Endosomes, Ubiquitin/genetics, Article, name=Cell Biology, 03 medical and health sciences, Ubiquitin Thiolesterase/genetics, Kelch-Like ECH-Associated Protein 1/genetics, Humans, NF-E2-Related Factor 2/genetics, Ubiquitin Thiolesterase

File Description: application/pdf

Access URL: https://pubmed.ncbi.nlm.nih.gov/38180476

Six generations of CHMP2B ‐mediated Frontotemporal Dementia: Clinical features, predictive testing, progression, and survival

Authors: Peter Roos, Peter Johannsen, Suzanne G. Lindquist, Jeremy M. Brown, Gunhild Waldemar, Morten Duno, Troels T. Nielsen, Esben Budtz‐Jørgensen, Susanne Gydesen, Ida E. Holm, John Collinge, Adrian M. Isaacs, Jørgen E. Nielsen, Anders Gade, Jette Stokholm, Tove Thusgaard, Elizabeth M.C. Fisher, Elisabet Englund

Source: Roos, P, Johannsen, P, Lindquist, S G, Brown, J M, Waldemar, G, Duno, M, Nielsen, T T, Budtz-Jørgensen, E, Gydesen, S, Holm, I E, Collinge, J, Isaacs, A M, Frontotemporal dementia Research in Jutland Association (FReJA) consortium & Nielsen, J E 2022, 'Six generations of CHMP2B-mediated Frontotemporal Dementia : Clinical features, predictive testing, progression, and survival', Acta Neurologica Scandinavica, vol. 145, no. 5, pp. 529-540. https://doi.org/10.1111/ane.13578

Subject Terms: 2. Zero hunger, 0301 basic medicine, Endosomal Sorting Complexes Required for Transport/genetics, Mutation/genetics, Endosomal Sorting Complexes Required for Transport, CHMP2B, Nerve Tissue Proteins, Hereditary degenerative disorders, 3. Good health, Cohort Studies, Frontotemporal Dementia/genetics, 03 medical and health sciences, 0302 clinical medicine, Frontotemporal Dementia, Mutation, Nerve Tissue Proteins/genetics, Humans, 10. No inequality, Retrospective Studies

Access URL: https://pubmed.ncbi.nlm.nih.gov/34997757

Giant worm-shaped ESCRT scaffolds surround actin-independent integrin clusters

Authors: Femmy C. Stempels, Muwei Jiang, Harry M. Warner, Magda-Lena Moser, Maaike H. Janssens, Sjors Maassen, Iris H. Nelen, Rinse de Boer, William F. Jiemy, David Knight, Julian Selley, Ronan O’Cualain, Maksim V. Baranov, Thomas C.Q. Burgers, Roberto Sansevrino, Dragomir Milovanovic, Peter Heeringa, Matthew C. Jones, Rifka Vlijm, Martin ter Beest, Geert van den Bogaart

Source: J Cell Biol
The journal of cell biology 222(7), e202205130 (2023). doi:10.1083/jcb.202205130
Journal of Cell Biology, 222, 7
Stempels, F C, Jiang, M, Warner, H M, Moser, M L, Janssens, M H, Maassen, S, Nelen, I H, de Boer, R, Jiemy, W F, Knight, D, Selley, J, O’Cualain, R, Baranov, M V, Burgers, T C Q, Sansevrino, R, Milovanovic, D, Heeringa, P, Jones, M C, Vlijm, R, Beest, M & van den Bogaart, G 2023, 'Giant worm-shaped ESCRT scaffolds surround actin-independent integrin clusters', Journal of Cell Biology, vol. 222, no. 7, e202205130. https://doi.org/10.1083/jcb.202205130
Journal of Cell Biology

Subject Terms: genetics [Integrins], Integrins, metabolism [Actins], Endosomal Sorting Complexes Required for Transport/genetics, Endosomal Sorting Complexes Required for Transport, Protein Conformation, Macrophages, Cell Membrane, metabolism [Endosomal Sorting Complexes Required for Transport], Radboud University Medical Center, Radboudumc 2: Cancer development and immune defence Tumorimmunology, chemistry [Phospholipids], Dendritic Cells, Fibroblasts, Integrins/genetics, Article, Actins, Phospholipids/chemistry, Protein Transport, Actins/metabolism, ddc:570, metabolism [Integrins], Humans, genetics [Endosomal Sorting Complexes Required for Transport], Phospholipids

Access URL: https://pubmed.ncbi.nlm.nih.gov/37200023
https://research.manchester.ac.uk/en/publications/74b1ed1e-3425-4383-8ae9-08f7c838107d
https://doi.org/10.1083/jcb.202205130
https://hdl.handle.net/11370/a14171fe-8634-42a9-8e93-28317064efb3
https://research.rug.nl/en/publications/a14171fe-8634-42a9-8e93-28317064efb3
https://doi.org/10.1083/jcb.202205130
https://repository.ubn.ru.nl//bitstream/handle/2066/292891/292891.pdf
https://hdl.handle.net/2066/292891
https://research.manchester.ac.uk/en/publications/74b1ed1e-3425-4383-8ae9-08f7c838107d
https://doi.org/10.1083/jcb.202205130
http://www.scopus.com/inward/record.url?scp=85164416129&partnerID=8YFLogxK

Ubiquitin-specific protease 2-45 (Usp2-45) binds to epithelial Na+ channel (ENaC)-ubiquitylating enzyme Nedd4-2.

Authors: Oberfeld, B., Ruffieux-Daidié, D., Vitagliano, J.J., Pos, K.M., Verrey, F., Staub, O.

Subject Terms: Animals, Blotting, Western, Catalysis, DNA/genetics, Endopeptidases/biosynthesis, Endopeptidases/genetics, Endosomal Sorting Complexes Required for Transport/biosynthesis, Endosomal Sorting Complexes Required for Transport/genetics, Epithelial Sodium Channel/metabolism, Escherichia coli/metabolism, Glutathione/metabolism, HEK293 Cells, Humans, Immunoprecipitation, Kinetics, Mice, Oocytes/metabolism, Patch-Clamp Techniques, Protein Binding, Recombinant Proteins/chemistry, Recombinant Proteins/metabolism, Transfection, Ubiquitin-Protein Ligases/biosynthesis, Ubiquitin-Protein Ligases/genetics, Xenopus laevis

Relation: American Journal of Physiology - Renal Physiology; https://iris.unil.ch/handle/iris/184667; serval:BIB_996B8468C1F8; 000292641000026

Availability: https://iris.unil.ch/handle/iris/184667
https://doi.org/10.1152/ajprenal.00487.2010

Alternatively spliced proline-rich cassettes link WNK1 to aldosterone action.

Authors: Roy, A., Al-Qusairi, L., Donnelly, B.F., Ronzaud, C., Marciszyn, A.L., Gong, F., Chang, Y.P., Butterworth, M.B., Pastor-Soler, N.M., Hallows, K.R., Staub, O., Subramanya, A.R.

Subject Terms: Aldosterone/pharmacology, Alternative Splicing/drug effects, Alternative Splicing/physiology, Animals, Endosomal Sorting Complexes Required for Transport/genetics, Endosomal Sorting Complexes Required for Transport/metabolism, Enzyme Activation/drug effects, Enzyme Activation/physiology, Gene Expression Regulation, Enzymologic/drug effects, Enzymologic/physiology, HEK293 Cells, Humans, Intracellular Signaling Peptides and Proteins/biosynthesis, Intracellular Signaling Peptides and Proteins/genetics, Mice, Knockout, Minor Histocompatibility Antigens, Nedd4 Ubiquitin Protein Ligases, Protein Serine-Threonine Kinases/biosynthesis, Protein Serine-Threonine Kinases/genetics, Protein Serine-Threonine Kinases/metabolism, Signal Transduction/drug effects, Signal Transduction/physiology, Ubiquitin-Protein Ligases/genetics, Ubiquitin-Protein Ligases/metabolism, WNK Lysine-Deficient Protein Kinase 1

Relation: The Journal of Clinical Investigation; https://iris.unil.ch/handle/iris/167752; serval:BIB_689620E22F3F; 000362303600021

Availability: https://iris.unil.ch/handle/iris/167752
https://doi.org/10.1172/JCI75245

Intracellular ubiquitylation of the epithelial Na+ channel controls extracellular proteolytic channel activation via conformational change.

Authors: Ruffieux-Daidié, D., Staub, O.

Subject Terms: Amino Acid Motifs, Chymotrypsin/pharmacology, Endopeptidases/genetics, Endopeptidases/metabolism, Endosomal Sorting Complexes Required for Transport/genetics, Endosomal Sorting Complexes Required for Transport/metabolism, Epithelial Sodium Channel/genetics, Epithelial Sodium Channel/metabolism, Furin/genetics, Furin/metabolism, HEK293 Cells, Humans, Mutation, Signal Transduction/drug effects, Signal Transduction/physiology, Trypsin/pharmacology, Ubiquitin-Protein Ligases/genetics, Ubiquitin-Protein Ligases/metabolism, Ubiquitination/drug effects, Ubiquitination/physiology

Relation: Journal of Biological Chemistry; https://iris.unil.ch/handle/iris/145751; serval:BIB_A490D71A413D; 000286464300005

Availability: https://iris.unil.ch/handle/iris/145751
https://doi.org/10.1074/jbc.M110.176156

Renal tubular NEDD4-2 deficiency causes NCC-mediated salt-dependent hypertension.

Authors: Ronzaud, C., Loffing-Cueni, D., Hausel, P., Debonneville, A., Malsure, S.R., Fowler-Jaeger, N., Boase, N.A., Perrier, R., Maillard, M., Yang, B., Stokes, J.B., Koesters, R., Kumar, S., Hummler, E., Loffing, J., Staub, O.

Subject Terms: Animals, Blood Pressure, Disease Models, Animal, Endosomal Sorting Complexes Required for Transport/deficiency, Endosomal Sorting Complexes Required for Transport/genetics, Epithelial Sodium Channels/metabolism, Humans, Hypertension/etiology, Hypertension/genetics, Kidney Tubules/physiopathology, Liddle Syndrome/etiology, Liddle Syndrome/genetics, Mice, Knockout, Potassium/blood, Potassium/urine, Potassium Channels, Inwardly Rectifying/metabolism, Receptors, Drug/metabolism, Sodium/blood, Sodium/urine, Sodium, Dietary/administration & dosage, Dietary/adverse effects, Symporters/metabolism, Ubiquitin-Protein Ligases/deficiency, Ubiquitin-Protein Ligases/genetics

File Description: application/pdf

Relation: The Journal of Clinical Investigation; https://iris.unil.ch/handle/iris/115046; serval:BIB_218B3682F156; 000314553600022

Availability: https://iris.unil.ch/handle/iris/115046
https://doi.org/10.1172/JCI61110

Frontotemporal dementia caused by CHMP2B mutation is characterised by neuronal lysosomal storage pathology

Authors: Clayton, EL, Mizielinska, S, Edgar, JR, Nielsen, TT, Marshall, S, Norona, FE, Robbins, M, Damirji, H, Holm, IE, Johannsen, P, Nielsen, JE, Asante, EA, Collinge, J, FReJA consortium, ., Isaacs, AM

Contributors: DSpace at Cambridge pro (8.1)

Source: Acta Neuropathol
Clayton, E L, Mizielinska, S, Edgar, J R, Nielsen, T T, Marshall, S, Norona, F E, Robbins, M, Damirji, H, Holm, I E, Johannsen, P, Nielsen, J E, Asante, E A, Collinge, J & Isaacs, A M 2015, ' Frontotemporal dementia caused by CHMP2B mutation is characterised by neuronal lysosomal storage pathology ', Acta Neuropathologica, vol. 130, no. 4, pp. 511-523 . https://doi.org/10.1007/s00401-015-1475-3
2015, ' Frontotemporal dementia caused by CHMP2B mutation is characterised by neuronal lysosomal storage pathology ', Acta Neuropathologica, vol. 130, no. 4, pp. 511-523 . https://doi.org/10.1007/s00401-015-1475-3

Subject Terms: Male, 0301 basic medicine, Lysosomal storage disorder, Neurons/metabolism, Clinical Neurology, Mice, Transgenic, Nerve Tissue Proteins, Lysosomes/metabolism, Transgenic, Pathology and Forensic Medicine, ESCRT, Microglia/metabolism, Mice, Frontotemporal Dementia/genetics, Cellular and Molecular Neuroscience, 03 medical and health sciences, 80 and over, Brain/metabolism, Nerve Tissue Proteins/genetics, Animals, Humans, Aged, Aged, 80 and over, Neurons, 2. Zero hunger, Original Paper, 0303 health sciences, Endosomal Sorting Complexes Required for Transport/genetics, Endosomal Sorting Complexes Required for Transport, Animal, CHMP2B, Brain, FTD, Middle Aged, Lysosome, 3. Good health, Disease Models, Animal, Frontotemporal Dementia, Disease Models, Mutation, Disease Progression, Female, Microglia, Protein Multimerization, Lysosomes

File Description: application/pdf

Access URL: https://link.springer.com/content/pdf/10.1007%2Fs00401-015-1475-3.pdf
https://pubmed.ncbi.nlm.nih.gov/26358247
https://www.ncbi.nlm.nih.gov/pubmed/26358247
http://discovery.ucl.ac.uk/1473300/
https://link.springer.com/article/10.1007/s00401-015-1475-3
https://paperity.org/p/74136493/frontotemporal-dementia-caused-by-chmp2b-mutation-is-characterised-by-neuronal-lysosomal
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4575387/
https://discovery.ucl.ac.uk/id/eprint/1473300
https://curis.ku.dk/ws/files/174350185/s00401_015_1475_3.pdf
https://kclpure.kcl.ac.uk/ws/files/122615092/Frontotemporal_dementia_caused_by_Acc2Sept2015Epub10Sept2015_GOLD_VoR_CC_BY_.pdf
https://discovery-pp.ucl.ac.uk/id/eprint/1473300/

STAM2, a member of the endosome-associated complex ESCRT-0 is highly expressed in neurons

Authors: Kapuralin, Katarina, Ćurlin, Marija, Mitrečić, Dinko, Kosi, Nina, Schwarzer, Christoph, Glavan, Gordana, Gajović, Srećko

Source: Molecular and Cellular Neurosciences

Subject Terms: Male, 0301 basic medicine, Cytoplasm, brain, neurons, Stam2, Hippocampus, ESCRT, Cellular and Molecular Neuroscience, Mice, 03 medical and health sciences, Cerebellum / metabolism, Cytoplasm / metabolism, Cerebellum, expression, Animals, Olfactory Bulb / metabolism, endosome, Molecular Biology, Cells, Cultured, Adaptor Proteins, Signal Transducing, Cell Nucleus, Neurons, 0303 health sciences, Endosomal Sorting Complexes Required for Transport, Cell Nucleus / metabolism, Neurons / metabolism, nucleus, Cell Biology, Phosphoproteins, Olfactory Bulb, Mice, Inbred C57BL, Protein Transport, Hippocampus / metabolism, Organ Specificity, Phosphoproteins / genetics, Endosomal Sorting Complexes Required for Transport / metabolism, Phosphoproteins / metabolism, Adaptor Proteins, Signal Transducing / genetics, STAM2, Adaptor Proteins, Signal Transducing / metabolism, Endosomal Sorting Complexes Required for Transport / genetics

File Description: text/url; application/pdf

Access URL: https://pubmed.ncbi.nlm.nih.gov/26101075
https://core.ac.uk/display/33324206
https://www.sciencedirect.com/science/article/pii/S1044743115000974
https://europepmc.org/article/MED/26101075
https://www.bib.irb.hr/809976
https://pubmed.ncbi.nlm.nih.gov/26101075/
https://repozitorij.uni-lj.si/IzpisGradiva.php?id=83354
https://doi.org/10.1016/j.mcn.2015.06.009
https://hdl.handle.net/20.500.12556/RUL-83354
https://urn.nsk.hr/urn:nbn:hr:105:983995
https://doi.org/10.1016/j.mcn.2015.06.009

Dlg3 Trafficking and Apical Tight Junction Formation Is Regulated by Nedd4 and Nedd4-2 E3 Ubiquitin Ligases

Authors: Daniel Krappmann, Heiko Lickert, Seth G. N. Grant, Moritz Gegg, Claude Van Campenhout, Christian Johannes Gloeckner, Heide Oller, Marius Ueffing, Patrizia Giallonardo, Andrea C. Eitelhuber

Source: Dev Cell
Developmental Cell; Vol 21
Van Campenhout, C A, Eitelhuber, A, Gloeckner, C J, Giallonardo, P, Gegg, M, Oller, H, Grant, S G N, Krappmann, D, Ueffing, M & Lickert, H 2011, ' Dlg3 Trafficking and Apical Tight Junction Formation Is Regulated by Nedd4 and Nedd4-2 E3 Ubiquitin Ligases ', Developmental Cell, vol. 21, no. 3, pp. 479-491 . https://doi.org/10.1016/j.devcel.2011.08.003
Dev. Cell 21, 479-491 (2011)

Subject Terms: Male, 0301 basic medicine, POLARIZATION, Guanylate Kinase -- metabolism, Knockout, Nedd4 Ubiquitin Protein Ligases, Ubiquitin-Protein Ligases, Molecular Sequence Data, EXOCYST COMPLEX, Inbred C57BL, Article, Tight Junctions, Tight Junctions -- metabolism, Mice, 03 medical and health sciences, PROTEIN PHOSPHATASE-1, SEC6/8 COMPLEX, MAMMALIAN EPITHELIAL-CELLS, Animals, Cell Polarity -- physiology, Membrane Proteins -- metabolism, Amino Acid Sequence, Inner -- metabolism, Endosomal Sorting Complexes Required for Transport -- genetics -- metabolism, Mice, Knockout, 0303 health sciences, Endosomal Sorting Complexes Required for Transport, Ubiquitin-Protein Ligases -- genetics -- metabolism, MOUSE EMBRYO, Cell Polarity, Membrane Proteins, Ear, Sciences bio-médicales et agricoles, Mice, Inbred C57BL, DROSOPHILA, MICE, Protein Transport, PLANAR POLARITY, Ear, Inner, NMDA RECEPTOR, Female, Guanylate Kinases, Developmental Biology

File Description: application/pdf; 1 full-text file(s): application/pdf

Access URL: http://www.cell.com/article/S1534580711003157/pdf
https://pubmed.ncbi.nlm.nih.gov/21920314
https://difusion.ulb.ac.be/vufind/Record/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/133205/Details
https://www.cell.com/developmental-cell/pdf/S1534-5807(11)00315-7.pdf
https://www.research.ed.ac.uk/portal/en/publications/dlg3-trafficking-and-apical-tight-junction-formation-is-regulated-by-nedd4-and-nedd42-e3-ubiquitin-ligases(643e0ad5-1fc5-436b-9b90-02d980a92621)/export.html
https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21920314/
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4452538/
https://www.ncbi.nlm.nih.gov/pubmed/21920314
https://hdl.handle.net/20.500.11820/643e0ad5-1fc5-436b-9b90-02d980a92621
https://www.pure.ed.ac.uk/ws/files/9849565/Dlg3_Trafficking_and_Apical_Tight_Junction_Formation_Is_Regulated_by_Nedd4_and_Nedd4_2_E3_Ubiquitin_Ligases.pdf
https://push-zb.helmholtz-muenchen.de/frontdoor.php?source_opus=5611

The ubiquitin code of yeast permease trafficking

Authors: Lauwers, Elsa, Erpapazoglou, Zoi, Haguenauer-Tsapis, Rosine, André, Bruno

Contributors: Kropfinger, Antonia

Source: Trends in Cell Biology. 20:196-204

Subject Terms: Enzymologic, Ubiquitin-Protein Ligase Complexes -- genetics -- metabolism, 0301 basic medicine, Saccharomyces cerevisiae -- enzymology -- genetics -- metabolism, Saccharomyces cerevisiae Proteins, Vacuoles -- metabolism, Saccharomyces cerevisiae, Gene Expression Regulation, Enzymologic, 03 medical and health sciences, Ubiquitin -- metabolism, Animals, Humans, [SDV.BC] Life Sciences [q-bio]/Cellular Biology, Endosomal Sorting Complexes Required for Transport -- genetics -- metabolism, Protein Transport -- physiology, 0303 health sciences, Endosomal Sorting Complexes Required for Transport, Ubiquitin, Multivesicular Bodies, Biologie moléculaire, Membrane Proteins, Membrane Transport Proteins, Ubiquitin-Protein Ligase Complexes, Membrane Transport Proteins -- genetics -- metabolism, Endocytosis, Protein Transport, Gene Expression Regulation, Membrane Proteins -- genetics -- metabolism, Vacuoles, Multivesicular Bodies -- metabolism, Saccharomyces cerevisiae Proteins -- genetics -- metabolism

File Description: 1 full-text file(s): application/pdf

Access URL: https://pubmed.ncbi.nlm.nih.gov/20138522
https://hal.science/hal-00488077v1
https://doi.org/10.1016/j.tcb.2010.01.004
https://www.ncbi.nlm.nih.gov/pubmed/20138522
https://difusion.ulb.ac.be/vufind/Record/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/98873/Details
https://hal.archives-ouvertes.fr/hal-00488077
https://www.scienceopen.com/document?vid=c53f7142-94dc-4c05-b01d-4673e54fe0ea
https://www.sciencedirect.com/science/article/pii/S096289241000005X
http://www.sciencedirect.com/science/article/pii/S096289241000005X

SHIP2 (SH2 Domain-containing Inositol Phosphatase 2) SH2 Domain Negatively Controls SHIP2 Monoubiquitination in Response to Epidermal Growth Factor

Authors: De Schutter, Julie, Guillabert, Aude, Imbault, Virginie, Degraef, Chantal, Erneux, Christophe, Communi, David, Pirson, Isabelle

Source: The Journal of biological chemistry, 284 (52

Subject Terms: 0301 basic medicine, Protein Structure, Tertiary -- physiology, Proteasome Endopeptidase Complex, Time Factors, Nedd4 Ubiquitin Protein Ligases, Ubiquitin-Protein Ligases, Amino Acid Motifs, Epidermal Growth Factor -- pharmacology, Models, Biological, Cercopithecus aethiops, Ubiquitination -- physiology, Proteasome Endopeptidase Complex -- metabolism, 03 medical and health sciences, Proteasome Endopeptidase Complex -- genetics, Models, Protein Structure, Tertiary -- physiology, Chlorocebus aethiops, Animals, Humans, Proto-Oncogene Proteins c-cbl, Proto-Oncogene Proteins c-cbl -- metabolism, Epidermal Growth Factor -- metabolism, Endosomal Sorting Complexes Required for Transport -- metabolism, Endosomal Sorting Complexes Required for Transport, Epidermal Growth Factor, Ubiquitination -- drug effects, Ubiquitination, Amino Acid Motifs -- physiology, Sciences bio-médicales et agricoles, Phosphoric Monoester Hydrolases -- genetics, Ubiquitin-Protein Ligases -- metabolism, Biological, Phosphoric Monoester Hydrolases, Protein Structure, Tertiary, Proto-Oncogene Proteins c-cbl -- genetics, Endosomal Sorting Complexes Required for Transport -- genetics, Ubiquitin-Protein Ligases -- genetics, Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases, COS Cells, Phosphoric Monoester Hydrolases -- metabolism

File Description: 2 full-text file(s): application/pdf; application/pdf

Access URL: http://www.jbc.org/content/284/52/36062.full.pdf
https://pubmed.ncbi.nlm.nih.gov/19880507
https://www.jbc.org/article/S0021-9258(20)37417-2/fulltext
https://www.ncbi.nlm.nih.gov/pubmed/19880507
https://www.jbc.org/content/284/52/36062.full.pdf
https://www.sciencedirect.com/science/article/pii/S0021925820374172
https://difusion.ulb.ac.be/vufind/Record/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/53754/Details
https://europepmc.org/articles/PMC2794722/
http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/53754

t(11;15)(q23;q14) KMT2A/ZFYVE19

Authors: Huret, Jean-Loup

Contributors: Genetics, Dept Medical Information, University of Poitiers, CHU Poitiers Hospital, F-86021 Poitiers, France

Subject Terms: Leukaemia Section, Aurora Kinase B/genetics/*metabolism, Cell Cycle Checkpoints, Chromatin/metabolism, Chromosome Aberrations, Chromosome Segregation, Cytokinesis, Endosomal Sorting Complexes Required for Transport/genetics/*metabolism, Enzyme Activation, HeLa Cells, Humans, Luminescent Proteins/genetics/metabolism, Oncogene Proteins/genetics/*metabolism, Phosphorylation, Protein Transport, RNA Interference, Signal Transduction, Time Factors, Transfection, Vacuolar Proton-Translocating ATPases/genetics/*metaboli

Relation: Atlas of Genetics and Cytogenetics in Oncology and Haematology; http://AtlasGeneticsOncology.org/Anomalies/t1115q23q14ID1421.html; Jean-Loup, Huret. t(11;15)(q23;q14) KMT2A/ZFYVE19. Atlas of Genetics and Cytogenetics in Oncology and Haematology, 2016, 2, p. 94-95; http://hdl.handle.net/2042/62519; https://doi.org/10.4267/2042/62519

Availability: http://hdl.handle.net/2042/62519
https://doi.org/10.4267/2042/62519

Extracellular vesicle sorting of α-Synuclein is regulated by sumoylation.

Authors: Kunadt, Marcel, Eckermann, Katrin, Krumova, Petranka, Oliveira, Luis M A, Bähr, Mathias, Möbius, Wiebke, Levin, Johannes, Giese, Armin, Kruse, Niels, Mollenhauer, Brit, Geiss-Friedlander, Ruth, Ludolph, Albert C, Stuendl, Anne, Freischmidt, Axel, Feiler, Marisa S, Danzer, Karin M, Zweckstetter, Markus, Jovin, Thomas M, Simons, Mikael, Weishaupt, Jochen H, Schneider, Anja, Gong, Jing, Russo, Belisa, Strauss, Katrin, Rai, Surya, Kügler, Sebastian, Falomir Lockhart, Lisandro, Schwalbe, Martin

Source: Acta neuropathologica 129(5), 695-713 (2015). doi:10.1007/s00401-015-1408-1

Subject Terms: info:eu-repo/classification/ddc/610, Animals, Cell Culture Techniques, Cell Line, Tumor, Endosomal Sorting Complexes Required for Transport: genetics, Endosomal Sorting Complexes Required for Transport: metabolism, Extracellular Vesicles: genetics, Extracellular Vesicles: metabolism, Mice, Oligodendroglia: cytology, Oligodendroglia: metabolism, SUMO-1 Protein: genetics, SUMO-1 Protein: metabolism, Signal Transduction: genetics, Signal Transduction: physiology, Sumoylation: physiology, alpha-Synuclein: genetics, alpha-Synuclein: metabolism, Endosomal Sorting Complexes Required for Transport, SUMO-1 Protein, alpha-Synuclein

Subject Geographic: DE

Relation: info:eu-repo/semantics/altIdentifier/pmid/pmid:25778619; info:eu-repo/semantics/altIdentifier/issn/1432-0533; info:eu-repo/semantics/altIdentifier/issn/0001-6322; https://pub.dzne.de/record/137883

Availability: https://pub.dzne.de/record/137883
https://pub.dzne.de/search?p=id:%22DZNE-2020-04205%22

TDP-43 loss of function inhibits endosomal trafficking and alters trophic signaling in neurons.

Authors: Schwenk, Benjamin M, Hartmann, Hannelore, Schreiber, Franziska, Haupt, Simone, Peitz, Michael, Brüstle, Oliver, Küpper, Clemens, Klopstock, Thomas, Otto, Markus, Ludolph, Albert C, Arzberger, Thomas, Kuhn, Peer-Hendrik, Serdaroglu, Alperen, Edbauer, Dieter, Schludi, Martin H, Hornburg, Daniel, Meissner, Felix, Orozco, Denise, Colombo, Alessio, Tahirovic, Sabina, Michaelsen, Meike

Source: The EMBO journal 35(21), 2350-2370 (2016). doi:10.15252/embj.201694221

Subject Terms: info:eu-repo/classification/ddc/570, ATPases Associated with Diverse Cellular Activities, Adenosine Triphosphatases: genetics, Adenosine Triphosphatases: metabolism, Amyotrophic Lateral Sclerosis: genetics, Amyotrophic Lateral Sclerosis: metabolism, Animals, Cells, Cultured, DNA-Binding Proteins: genetics, DNA-Binding Proteins: metabolism, Endosomal Sorting Complexes Required for Transport: genetics, Endosomal Sorting Complexes Required for Transport: metabolism, Endosomes: metabolism, Frontotemporal Lobar Degeneration: genetics, Frontotemporal Lobar Degeneration: metabolism, Gene Knockdown Techniques, Hippocampus: cytology, Humans, Neurons: metabolism, Protein Transport, Rats, Receptor, ErbB-4: genetics, ErbB-4: metabolism, Fibroblast Growth Factor, Type 1: metabolism, Signal Transduction, CHMP2B protein, human

Subject Geographic: DE

Relation: info:eu-repo/semantics/altIdentifier/issn/1460-2075; info:eu-repo/semantics/altIdentifier/issn/0261-4189; info:eu-repo/semantics/altIdentifier/pmid/pmid:27621269; https://pub.dzne.de/record/138865

Availability: https://pub.dzne.de/record/138865
https://pub.dzne.de/search?p=id:%22DZNE-2020-05187%22

Dlg3 trafficking and apical tight junction formation is regulated by nedd4 and nedd4-2 e3 ubiquitin ligases.

Authors: Van Campenhout, Claude, Eitelhuber, Andrea, Gloeckner, Christian J, Giallonardo, Patrizia, Gegg, Moritz, Oller, Heide, Grant, Seth G N, Krappmann, Daniel, Ueffing, Marius, Lickert, Heiko

Source: Developmental cell, 21 (3

Subject Terms: Sciences bio-médicales et agricoles, Amino Acid Sequence, Animals, Cell Polarity -- physiology, Ear, Inner -- metabolism, Endosomal Sorting Complexes Required for Transport -- genetics -- metabolism, Female, Guanylate Kinase -- metabolism, Male, Membrane Proteins -- metabolism, Mice, Inbred C57BL, Knockout, Molecular Sequence Data, Protein Transport, Tight Junctions -- metabolism, Ubiquitin-Protein Ligases -- genetics -- metabolism

File Description: 1 full-text file(s): application/pdf

Relation: uri/info:doi/10.1016/j.devcel.2011.08.003; uri/info:pmid/21920314; https://dipot.ulb.ac.be/dspace/bitstream/2013/133205/1/Elsevier_115558.pdf

Availability: http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/133205
https://dipot.ulb.ac.be/dspace/bitstream/2013/133205/1/Elsevier_115558.pdf

Nedd4-induced monoubiquitination of IRS-2 enhances IGF signalling and mitogenic activity.

Additional Titles: Nedd4-induced monoubiquitination of IRS-2 enhances IGF signalling and mitogenic activity

Authors: Fukushima, Toshiaki, Yoshihara, H., Furuta, H., Kamei, H., Hakuno, F., Luan, J., Duan, C., Saeki, Y., Tanaka, K., Iemura, S., Natsume, T., Chida, K., Nakatsu, Y., Kamata, H., Asano, T., Takahashi, S.

Index Terms: Adaptor Proteins, Vesicular Transport/metabolism, Animals, Cell Line, Cell Line, Tumor, Cell Proliferation/*genetics, Cyclic AMP/metabolism, Endosomal Sorting Complexes Required for Transport/*genetics, HEK293 Cells, Humans, Insulin Receptor Substrate Proteins/*metabolism, Insulin-Like Growth Factor I/*metabolism, Male, Mitosis/*genetics, Phosphorylation, Prostatic Neoplasms/genetics, Rats, Receptor, IGF Type 1/metabolism, Somatomedins, Ubiquitin-Protein Ligases/*genetics, Ubiquitination, Zebrafish, Zebrafish Proteins/genetics, Journal Article., NA.

URL: http://t2r2.star.titech.ac.jp/cgi-bin/publicationinfo.cgi?q_publication_content_number=CTT100786930
https://doi.org/10.1038/ncomms7780