Analysis of CARD10 and CARD11 Somatic Mutations in Patients with Ovarian Endometriosis
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Hypomorphic CARD11 Mutations Associated with Diverse Immunologic Phenotypes with Or Without Atopic Disease
This is a repository copy of Hypomorphic CARD11 mutations associated with diverse immunologic phenotypes with or without atopic disease.. White Rose Research Online URL for this paper: http://eprints.whiterose.ac.uk/135712/ Version: Accepted Version Article: Dorjbal, B, Stinson, JR, Ma, CA et al. (52 more authors) (2019) Hypomorphic CARD11 mutations associated with diverse immunologic phenotypes with or without atopic disease. The Journal of Allergy and Clinical Immunology, 143 (4). pp. 1482-1495. ISSN 0091-6749 https://doi.org/10.1016/j.jaci.2018.08.013 Published by Elsevier Inc. on behalf of the American Academy of Allergy, Asthma & Immunology. Licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International http://creativecommons.org/licenses/by-nc-nd/4.0/ Reuse This article is distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs (CC BY-NC-ND) licence. This licence only allows you to download this work and share it with others as long as you credit the authors, but you can’t change the article in any way or use it commercially. More information and the full terms of the licence here: https://creativecommons.org/licenses/ Takedown If you consider content in White Rose Research Online to be in breach of UK law, please notify us by emailing [email protected] including the URL of the record and the reason for the withdrawal request. [email protected] https://eprints.whiterose.ac.uk/ Accepted Manuscript Hypomorphic CARD11 mutations associated with diverse immunologic phenotypes with or without atopic disease Batsukh Dorjbal, PhD, Jeffrey R. Stinson, PhD, Chi A. -
Lymphomagenic CARD11/BCL10/MALT1 Signaling Drives Malignant B-Cell Proliferation Via Cooperative NF-Κb and JNK Activation
Lymphomagenic CARD11/BCL10/MALT1 signaling drives malignant B-cell proliferation via cooperative NF-κB and JNK activation Nathalie Kniesa, Begüm Alankusa, Andre Weilemannb,c, Alexandar Tzankovd, Kristina Brunnera, Tanja Ruffa, Marcus Kremere, Ulrich B. Kellerf, Georg Lenzb,c, and Jürgen Rulanda,g,h,1 aInstitut für Klinische Chemie und Pathobiochemie, Klinikum Rechts der Isar, Technische Universität München, 81675 Munich, Germany; bTranslational Oncology, Department of Medicine A, University Hospital Münster, 48149 Münster, Germany; cCells in Motion, Cluster of Excellence EXC 1003, 48149 Münster, Germany; dInstitute of Pathology, University Hospital Basel, 4031 Basel, Switzerland; eInstitut für Pathologie, Klinikum Harlaching, 81545 Munich, Germany; fDepartment of Medicine III, Klinikum Rechts der Isar, Technische Universität München, 81675 Munich, Germany; gGerman Cancer Consortium, 69120 Heidelberg, Germany; and hGerman Center for Infection Research, 81675 München, Germany Edited by Tak W. Mak, The Campbell Family Institute for Breast Cancer Research at Princess Margaret Cancer Centre, University Health Network, Toronto, ON, Canada, and approved November 12, 2015 (received for review April 16, 2015) The aggressive activated B cell-like subtype of diffuse large B-cell (PI3K) (reviewed in ref. 8). The key link to the IKK complex is lymphoma is characterized by aberrant B-cell receptor (BCR) signal- the scaffolding molecule caspase recruitment domain-containing ing and constitutive nuclear factor kappa-B (NF-κB) activation, which protein 11 (CARD11), which is inactive in resting cells due to an is required for tumor cell survival. BCR-induced NF-κBactivationre- intramolecular inhibitory interaction between its linker region quires caspase recruitment domain-containing protein 11 (CARD11), and its coiled-coil domain (9). -
PRKCQ / PKC-Theta Antibody (Aa640-690) Rabbit Polyclonal Antibody Catalog # ALS16240
10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 PRKCQ / PKC-Theta Antibody (aa640-690) Rabbit Polyclonal Antibody Catalog # ALS16240 Specification PRKCQ / PKC-Theta Antibody (aa640-690) - Product Information Application WB, IHC Primary Accession Q04759 Reactivity Human, Mouse, Rat Host Rabbit Clonality Polyclonal Calculated MW 82kDa KDa PRKCQ / PKC-Theta Antibody (aa640-690) - Additional Information Gene ID 5588 Other Names Protein kinase C theta type, 2.7.11.13, Western blot of PKC (N670) pAb in extracts nPKC-theta, PRKCQ, PRKCT from A549 cells. Target/Specificity Human PKC Theta Reconstitution & Storage Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze-thaw cycles. Precautions PRKCQ / PKC-Theta Antibody (aa640-690) is for research use only and not for use in diagnostic or therapeutic procedures. Anti-PRKCQ / PKC-Theta antibody IHC staining of human brain, cerebellum. PRKCQ / PKC-Theta Antibody (aa640-690) - Protein Information PRKCQ / PKC-Theta Antibody (aa640-690) - Name PRKCQ Background Synonyms PRKCT Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent Function serine/threonine-protein kinase that mediates Calcium-independent, phospholipid- and non- redundant functions in T-cell receptor diacylglycerol (DAG)- dependent (TCR) signaling, including T-cells activation, serine/threonine-protein kinase that proliferation, differentiation and survival, by mediates non-redundant functions in T-cell mediating activation of multiple transcription receptor (TCR) signaling, including T-cells factors such as NF-kappa-B, JUN, NFATC1 and activation, proliferation, differentiation and NFATC2. In TCR-CD3/CD28-co-stimulated Page 1/3 10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 survival, by mediating activation of multiple T-cells, is required for the activation of transcription factors such as NF-kappa-B, NF-kappa-B and JUN, which in turn are JUN, NFATC1 and NFATC2. -
NIH Public Access Author Manuscript Mol Psychiatry
NIH Public Access Author Manuscript Mol Psychiatry. Author manuscript; available in PMC 2014 July 01. NIH-PA Author ManuscriptPublished NIH-PA Author Manuscript in final edited NIH-PA Author Manuscript form as: Mol Psychiatry. 2013 July ; 18(7): 781–787. doi:10.1038/mp.2013.24. Whole-exome sequencing and imaging genetics identify functional variants for rate of change in hippocampal volume in mild cognitive impairment K Nho1, JJ Corneveaux2, S Kim1,3, H Lin3, SL Risacher1, L Shen1,3, S Swaminathan1,4, VK Ramanan1,4, Y Liu3,4, T Foroud1,3,4, MH Inlow5, AL Siniard2, RA Reiman2, PS Aisen6, RC Petersen7, RC Green8, CR Jack7, MW Weiner9,10, CT Baldwin11, K Lunetta12, LA Farrer11,13, SJ Furney14,15,16, S Lovestone14,15,16, A Simmons14,15,16, P Mecocci17, B Vellas18, M Tsolaki19, I Kloszewska20, H Soininen21, BC McDonald1,22, MR Farlow22, B Ghetti23, MJ Huentelman2, and AJ Saykin1,3,4,22 for the Multi-Institutional Research on Alzheimer Genetic Epidemiology (MIRAGE) Study; for the AddNeuroMed Consortium; for the Indiana Memory and Aging Study; for the Alzheimer’s Disease Neuroimaging Initiative (ADNI)24 1Department of Radiology and Imaging Sciences, Center for Neuroimaging, Indiana University School of Medicine, Indianapolis, IN, USA 2Neurogenomics Division, The Translational Genomics Research Institute (TGen), Phoenix, AZ, USA 3Center for Computational Biology and Bioinformatics, Indiana University School of Medicine, Indianapolis, IN, USA 4Department of Medical and Molecular Genetics, Indiana University School of Medicine, Indianapolis, IN, -
Defining the Relevant Combinatorial Space of the PKC/CARD-CC Signal Transduction Nodes
bioRxiv preprint doi: https://doi.org/10.1101/228767; this version posted May 2, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-ND 4.0 International license. Defining the relevant combinatorial space of the PKC/CARD-CC signal transduction nodes Jens Staal1,2,*, Yasmine Driege1,2, Mira Haegman1,2, Styliani Iliaki1,2, Domien Vanneste1,2, Inna Affonina1,2, Harald Braun1,2, Rudi Beyaert1,2 1 Department of Biomedical Molecular Biology, Ghent University, Ghent, Belgium, 2 VIB-UGent Center for Inflammation Research, Unit of Molecular Signal Transduction in Inflammation, VIB, Ghent, Belgium. * corresponding author: [email protected] Running title: PKC/CARD-CC signaling Abbreviations: Bcl10 = B Cell CLL/Lymphoma 10 CARD = Caspase activation and recruitment domain CC = Coiled-coil domain MALT1 = Mucosa-associated lymphoid tissue lymphoma translocation protein 1 PKC = protein kinase C Keywords: Inflammation, cancer, NF-kappaB, paracaspase Conflict of interests: The authors declare no conflict of interest. bioRxiv preprint doi: https://doi.org/10.1101/228767; this version posted May 2, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-ND 4.0 International license. Abstract Biological signal transduction typically display a so-called bow-tie or hour glass topology: Multiple receptors lead to multiple cellular responses but the signals all pass through a narrow waist of central signaling nodes. -
Structural Determinants of MALT1 Protease Activity
doi:10.1016/j.jmb.2012.02.018 J. Mol. Biol. (2012) 419,4–21 Contents lists available at www.sciencedirect.com Journal of Molecular Biology journal homepage: http://ees.elsevier.com.jmb Structural Determinants of MALT1 Protease Activity Christian Wiesmann 1, Lukas Leder 1, Jutta Blank 1, Anna Bernardi 1, Samu Melkko 1, Arnaud Decock 1, Allan D'Arcy 1, Frederic Villard 1, Paulus Erbel 1, Nicola Hughes 1, Felix Freuler 1, Rainer Nikolay 1, Juliano Alves 2, Frederic Bornancin 1 and Martin Renatus 1⁎ 1Novartis Institutes for BioMedical Research, Forum 1, Novartis Campus, CH-4002 Basel, Switzerland 2Genomics Institute of the Novartis Research Foundation, 10675 John Jay Hopkins Drive, San Diego, CA 92121, USA Received 19 December 2011; The formation of the CBM (CARD11–BCL10–MALT1) complex is pivotal received in revised form for antigen-receptor-mediated activation of the transcription factor NF-κB. 13 February 2012; Signaling is dependent on MALT1 (mucosa-associated lymphoid tissue accepted 15 February 2012 lymphoma translocation protein 1), which not only acts as a scaffolding Available online protein but also possesses proteolytic activity mediated by its caspase-like 23 February 2012 domain. It remained unclear how the CBM activates MALT1. Here, we provide biochemical and structural evidence that MALT1 activation is Edited by M. Guss dependent on its dimerization and show that mutations at the dimer interface abrogate activity in cells. The unliganded protease presents itself in Keywords: a dimeric yet inactive state and undergoes substantial conformational protease; changes upon substrate binding. These structural changes also affect the caspase; conformation of the C-terminal Ig-like domain, a domain that is required for structure; MALT1 activity. -
Molecular Architecture and Regulation of BCL10-MALT1 Filaments
ARTICLE DOI: 10.1038/s41467-018-06573-8 OPEN Molecular architecture and regulation of BCL10-MALT1 filaments Florian Schlauderer1, Thomas Seeholzer2, Ambroise Desfosses3, Torben Gehring2, Mike Strauss 4, Karl-Peter Hopfner 1, Irina Gutsche3, Daniel Krappmann2 & Katja Lammens1 The CARD11-BCL10-MALT1 (CBM) complex triggers the adaptive immune response in lymphocytes and lymphoma cells. CARD11/CARMA1 acts as a molecular seed inducing 1234567890():,; BCL10 filaments, but the integration of MALT1 and the assembly of a functional CBM complex has remained elusive. Using cryo-EM we solved the helical structure of the BCL10- MALT1 filament. The structural model of the filament core solved at 4.9 Å resolution iden- tified the interface between the N-terminal MALT1 DD and the BCL10 caspase recruitment domain. The C-terminal MALT1 Ig and paracaspase domains protrude from this core to orchestrate binding of mediators and substrates at the filament periphery. Mutagenesis studies support the importance of the identified BCL10-MALT1 interface for CBM complex assembly, MALT1 protease activation and NF-κB signaling in Jurkat and primary CD4 T-cells. Collectively, we present a model for the assembly and architecture of the CBM signaling complex and how it functions as a signaling hub in T-lymphocytes. 1 Gene Center, Ludwig-Maximilians University, Feodor-Lynen-Str. 25, 81377 München, Germany. 2 Research Unit Cellular Signal Integration, Institute of Molecular Toxicology and Pharmacology, Helmholtz-Zentrum München - German Research Center for Environmental Health, Ingolstaedter Landstrasse 1, 85764 Neuherberg, Germany. 3 University Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale IBS, F-38044 Grenoble, France. 4 Department of Anatomy and Cell Biology, McGill University, Montreal, Canada H3A 0C7. -
Copy Number Variation at Chromosome 5Q21.2 Is Associated with Intraocular Pressure
Genetics Copy Number Variation at Chromosome 5q21.2 Is Associated With Intraocular Pressure Abhishek Nag,1 Cristina Venturini,2 Pirro G. Hysi,1 Matthew Arno,3 Estibaliz Aldecoa-Otalora Astarloa,3 Stuart MacGregor,4 Alex W. Hewitt,5,6 Terri L. Young,7 Paul Mitchell,8 Ananth C. Viswanathan,9 David A. Mackey,6 and Christopher J. Hammond1 1Department of Twin Research and Genetic Epidemiology, King’s College London, St. Thomas’ Hospital, London, United Kingdom 2UCL Institute of Ophthalmology, London, United Kingdom 3King’s Genomics Facilities, King’s College London, London, United Kingdom 4Queensland Institute of Medical Research, Statistical Genetics, Herston, Brisbane, Australia 5Centre for Eye Research Australia, University of Melbourne, Royal Victorian Eye and Ear Hospital, Melbourne, Australia 6University of Western Australia, Centre for Ophthalmology and Visual Science, Lions Eye Institute, Perth, Australia 7Center for Human Genetics, Duke University Medical Center, Durham, North Carolina 8Centre for Vision Research, Westmead Millennium Institute, University of Sydney, Sydney, Australia 9NIHR Biomedical Research Centre at Moorfields Eye Hospital NHS Foundation Trust and UCL Institute of Ophthalmology, London, United Kingdom Correspondence: Chris Hammond, PURPOSE. Glaucoma is a major cause of blindness in the world. Recent genome-wide Department of Twin Research and association studies (GWAS) have identified common genetic variants for glaucoma, but still a Genetic Epidemiology, St. Thomas’ significant heritability gap remains. We hypothesized -
Gene Section Short Communication
Atlas of Genetics and Cytogenetics in Oncology and Haematology OPEN ACCESS JOURNAL INIST-CNRS Gene Section Short Communication CARD10 (caspase recruitment domain family, member 10) Gamze Ayaz, Mesut Muyan Department of Biological Sciences, Middle East Technical University, Ankara, Turkey (GA, MM) Published in Atlas Database: August 2014 Online updated version : http://AtlasGeneticsOncology.org/Genes/CARD10ID43187ch22q13.html Printable original version : http://documents.irevues.inist.fr/bitstream/handle/2042/62142/08-2014-CARD10ID43187ch22q13.pdf DOI: 10.4267/2042/62142 This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 2.0 France Licence. © 2015 Atlas of Genetics and Cytogenetics in Oncology and Haematology Abstract Pseudogene Caspase recruitment domain family, member 10, No reported pseudogene. CARD10 (also known as CARMA3 or Bimp1), is a member of the membrane-associated guanylate Protein kinase (MAGUK) superfamily proteins that act to Description organize signaling at the plasma membrane. This family of proteins contains Src-homology 3 (SH3), CARD10 (NP_055365) is a 1032 amino-acid long PDZ, GuK domains and caspase recruitment domain protein with a molecular mass of 116 kDa. (CARD). The amino-terminally located CARD of This protein consists of antiparallel alpha helices. CARD10 functions as an activator of BCL10 and CARD10 contains an N-terminal CARD domain, NF-kappaB (NF-kB) signaling critical for the followed by a central coiled-coil (CC) domain and a regulation of cellular survival and proliferation. C-terminal region encompassing a PDZ domain, a CARD10 (CARMA3) is reported to be over- SH3 domain and a GUK domain (Wang et al., 2001). expressed in various cancer types that include breast, The CARD domain has a hydrophobic core and a glioma, colon and non-small-cell lung cancers. -
Rare Copy Number Variants in the Genome of Chinese Female Children and Adolescents with Turner Syndrome
Bioscience Reports (2019) 39 BSR20181305 https://doi.org/10.1042/BSR20181305 Research Article Rare copy number variants in the genome of Chinese female children and adolescents with Turner syndrome Li Li1,*, Qingfeng Li1,*, Qiong Wang2,LiLiu3,RuLi4,HuishuLiu1, Yaojuan He1 and Gendie E. Lash2 1Department of Obstetrics and Gynecology, Guangzhou Women and Children’s Medical Center, Guangzhou Medical University, 9 Jinsui Road, Guangzhou, Guangdong 510160, China; 2Guangzhou Institute of Pediatrics, Guangzhou Women and Children’s Medical Center, Guangzhou Medical University, 9 Jinsui Road, Guangzhou, Guangdong 510160, China; 3Department of Pediatrics Endocrinology, Guangzhou Women and Children’s Medical Center, Guangzhou Medical University, 9 Jinsui Road, Guangzhou, Guangdong 510160, China; 4Prenatal Diagnostic Center, Guangzhou Women and Children’s Medical Center, Guangzhou Medical University, 9 Jinsui Road, Guangzhou, Guangdong 510160, China Correspondence: Li Li ([email protected]) or Gendie E. Lash ([email protected]) Turner syndrome (TS) is a congenital disease caused by complete or partial loss of one X chromosome. Low bone mineral status is a major phenotypic characteristic of TS that can not be fully explained by X chromosome loss, suggesting other autosomal-linked mutations may also exist. Therefore, the present study aimed to detect potential genetic mutations in TS through examination of copy number variation (CNV). Seventeen patients with TS and 15 healthy volunteer girls were recruited. Array-based comparative genomic hybridization (a-CGH) was performed on whole blood genomic DNA (gDMA) from the 17 TS patients and 15 healthy volunteer girls to identify potential CNVs. The abnormal CNV of one identified gene (CARD11) was verified by quantitative PCR. -
Intrinsic Plasma Cell Differentiation Defects in B Cell Expansion with Nf-Κb and T Cell Anergy Patient B Cells
ORIGINAL RESEARCH published: 02 August 2017 doi: 10.3389/fimmu.2017.00913 Intrinsic Plasma Cell Differentiation Defects in B Cell Expansion with NF-κB and T Cell Anergy Patient B Cells Swadhinya Arjunaraja 1, Brent D. Nosé 1, Gauthaman Sukumar 2,3, Nathaniel M. Lott 2,3, Clifton L. Dalgard 2,3 and Andrew L. Snow 1* 1 Department of Pharmacology and Molecular Therapeutics, Uniformed Services University of the Health Sciences, Bethesda, MD, United States, 2 Department of Anatomy, Physiology and Genetics, Uniformed Services University of the Health Sciences, Bethesda, MD, United States, 3 The American Genome Center, Uniformed Services University of the Health Sciences, Bethesda, MD, United States B cell Expansion with NF-κB and T cell Anergy (BENTA) disease is a novel B cell lymph- oproliferative disorder caused by germline, gain-of-function mutations in the lymphocyte Edited by: scaffolding protein CARD11, which drives constitutive NF- B signaling. Despite dramatic Elissa Deenick, κ Garvan Institute of Medical polyclonal expansion of naive and immature B cells, BENTA patients also present with Research, Australia signs of primary immunodeficiency, including markedly reduced percentages of class- Reviewed by: switched/memory B cells and poor humoral responses to certain vaccines. Using purified Vanessa L. Bryant, Walter and Eliza Hall Institute for naive B cells from our BENTA patient cohort, here we show that BENTA B cells exhibit Medical Research, Australia intrinsic defects in B cell differentiation. Despite a profound in vitro survival advantage David Andrew Fulcher, relative to normal donor B cells, BENTA patient B cells were severely impaired in their Australian National University, lo hi Australia ability to differentiate into short-lived IgD CD38 plasmablasts or CD138+ long-lived Julia Ellyard, plasma cells in response to various stimuli. -
An Evolutionary View
bioRxiv preprint doi: https://doi.org/10.1101/317719; this version posted May 9, 2018. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY 4.0 International license. How Much Information is Provided by Human Epigenomic Data? An Evolutionary View Brad Gulko1,2 and Adam Siepel2 1Graduate Field of Computer Science, Cornell University, Ithaca, NY, USA 2Simons Center for Quantitative Biology, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY, USA ABSTRACT Here, we ask the question, “How much information do available epigenomic data sets provide about human genomic function, individually or in combination?” We measure genomic function by using signatures of natural selection as a proxy, and we measure information in terms of reductions in entropy derived from a probabilistic evolutionary model. Our analysis of the human genome considers measures of chromatin accessibility (DNase-seq), chromatin states (ChromHMM), RNA expression (RNA-seq), small RNAs, and DNA methylation across 115 cell types from the Roadmap Epigenomics project, together with gene annotations, splice sites, predicted transcription factor binding sites, and predicted DNA melting temperatures. Selective pressure is measured using patterns of genetic variation across ~50 modern humans and several nonhuman primates. We find that protein-coding gene annotations are most informative about genomic function, followed in decreasing order by RNA-seq, ChromHMM, splice sites, melting temperature, and DNase-seq. Several features exhibit clear synergy, meaning that they yield more information in combination than they do individually.