Compositionally Distinct Nuclear Pore Complexes of Functionally Distinct Dimorphic Nuclei in the Ciliate Tetrahymena
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Aneuploidy: Using Genetic Instability to Preserve a Haploid Genome?
Health Science Campus FINAL APPROVAL OF DISSERTATION Doctor of Philosophy in Biomedical Science (Cancer Biology) Aneuploidy: Using genetic instability to preserve a haploid genome? Submitted by: Ramona Ramdath In partial fulfillment of the requirements for the degree of Doctor of Philosophy in Biomedical Science Examination Committee Signature/Date Major Advisor: David Allison, M.D., Ph.D. Academic James Trempe, Ph.D. Advisory Committee: David Giovanucci, Ph.D. Randall Ruch, Ph.D. Ronald Mellgren, Ph.D. Senior Associate Dean College of Graduate Studies Michael S. Bisesi, Ph.D. Date of Defense: April 10, 2009 Aneuploidy: Using genetic instability to preserve a haploid genome? Ramona Ramdath University of Toledo, Health Science Campus 2009 Dedication I dedicate this dissertation to my grandfather who died of lung cancer two years ago, but who always instilled in us the value and importance of education. And to my mom and sister, both of whom have been pillars of support and stimulating conversations. To my sister, Rehanna, especially- I hope this inspires you to achieve all that you want to in life, academically and otherwise. ii Acknowledgements As we go through these academic journeys, there are so many along the way that make an impact not only on our work, but on our lives as well, and I would like to say a heartfelt thank you to all of those people: My Committee members- Dr. James Trempe, Dr. David Giovanucchi, Dr. Ronald Mellgren and Dr. Randall Ruch for their guidance, suggestions, support and confidence in me. My major advisor- Dr. David Allison, for his constructive criticism and positive reinforcement. -
NLS-Mediated NPC Functions of the Nucleoporin Pom121
FEBS Letters 584 (2010) 3292–3298 journal homepage: www.FEBSLetters.org NLS-mediated NPC functions of the nucleoporin Pom121 Sevil Yavuz, Rachel Santarella-Mellwig, Birgit Koch, Andreas Jaedicke, Iain W. Mattaj *,1, Wolfram Antonin **,1 European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany article info abstract Article history: RanGTP mediates nuclear import and mitotic spindle assembly by dissociating import receptors Received 23 February 2010 from nuclear localization signal (NLS) bearing proteins. We investigated the interplay between Revised 31 May 2010 import receptors and the transmembrane nucleoporin Pom121. We found that Pom121 interacts Accepted 2 July 2010 with importin a/b and a group of nucleoporins in an NLS-dependent manner. In vivo, replacement Available online 14 July 2010 of Pom121 with an NLS mutant version resulted in defective nuclear transport, induction of aber- Edited by Ulrike Kuttay rant cytoplasmic membrane stacks and decreased cell viability. We propose that the NLS sites of Pom121 affect its function in NPC assembly both by influencing nucleoporin interactions and pore membrane structure. Keywords: Pom121 Nucleoporin Structured summary: Importin MINT-7951230: pom121 (uniprotkb:Q5EWX9) physically interacts (MI:0914) with nup155 (uni- protkb:O75694), Nup133 (uniprotkb:Q8WUM0) and Importin beta (uniprotkb:Q14974) by pull down (MI:0096) MINT-7951210: pom121 (uniprotkb:Q5EWX9) physically interacts (MI:0915) with Importin alpha (uni- protkb:P52170) and Importin beta (uniprotkb:P52297) -
TMEM33 (A-17): Sc-244421
SAN TA C RUZ BI OTEC HNOL OG Y, INC . TMEM33 (A-17): sc-244421 BACKGROUND PRODUCT TMEM33 (transmembrane protein 33), also known as protein DB83, is a 247 Each vial contains 200 µg IgG in 1.0 ml of PBS with < 0.1% sodium azide amino acid protein encoded by a gene mapping to human chromosome 4. and 0.1% gelatin. Representing approximately 6% of the human genome, chromosome 4 con - Blocking peptide available for competition studies, sc-244421 P, (100 µg tains nearly 900 genes. Notably, the Huntingtin gene, which is found to en- peptide in 0.5 ml PBS containing < 0.1% sodium azide and 0.2% BSA). code an expanded glutamine tract in cases of Huntington’s disease, is on chromosome 4. FGFR-3 is also encoded on chromosome 4 and has been asso - APPLICATIONS ciated with thanatophoric dwarfism, achondroplasia, Muenke syndrome and bladder cancer. Chromosome 4 is also tied to Ellis-van Creveld syndrome, TMEM33 (A-17) is recommended for detection of TMEM33 of mouse, rat methylmalonic acidemia and polycystic kidney disease. Chromosome 4 report - and human origin by Western Blotting (starting dilution 1:200, dilution range edly contains the largest gene deserts (regions of the genome with no protein 1:100-1:1000), immunofluorescence (starting dilution 1:50, dilution range encoding genes) and has one of the two lowest recombination frequencies 1:50-1:500) and solid phase ELISA (starting dilution 1:30, dilution range of the human chromosomes. 1:30-1:3000); non cross-reactive with other TMEM family members. TMEM33 (A-17) is also recommended for detection of TMEM33 in additional REFERENCES species, including equine, canine, bovine, porcine and avian. -
Macrophage Activation JUNB Is a Key Transcriptional Modulator Of
JUNB Is a Key Transcriptional Modulator of Macrophage Activation Mary F. Fontana, Alyssa Baccarella, Nidhi Pancholi, Miles A. Pufall, De'Broski R. Herbert and Charles C. Kim This information is current as of October 2, 2021. J Immunol 2015; 194:177-186; Prepublished online 3 December 2014; doi: 10.4049/jimmunol.1401595 http://www.jimmunol.org/content/194/1/177 Downloaded from Supplementary http://www.jimmunol.org/content/suppl/2014/12/03/jimmunol.140159 Material 5.DCSupplemental References This article cites 40 articles, 7 of which you can access for free at: http://www.jimmunol.org/content/194/1/177.full#ref-list-1 http://www.jimmunol.org/ Why The JI? Submit online. • Rapid Reviews! 30 days* from submission to initial decision • No Triage! Every submission reviewed by practicing scientists by guest on October 2, 2021 • Fast Publication! 4 weeks from acceptance to publication *average Subscription Information about subscribing to The Journal of Immunology is online at: http://jimmunol.org/subscription Permissions Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html Email Alerts Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts The Journal of Immunology is published twice each month by The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2014 by The American Association of Immunologists, Inc. All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. The Journal of Immunology JUNB Is a Key Transcriptional Modulator of Macrophage Activation Mary F. Fontana,* Alyssa Baccarella,* Nidhi Pancholi,* Miles A. -
Nuclear Pore Complexes Cluster in Dysmorphic Nuclei of Normal and Progeria Cells During Replicative Senescence
Nuclear Pore Complexes Cluster in Dysmorphic Nuclei of Normal and Progeria Cells during Replicative Senescence Jennifer M. Röhrl, Rouven Arnold and Karima Djabali * Epigenetics of Aging, Department of Dermatology and Allergy, TUM School of Medicine, Technical University of Munich (TUM), 85748 Garching, Germany; [email protected] (J.M.R.); [email protected] (R.A.) * Correspondence: [email protected] Supplementary Figures Figure S1: Seeding of NPCs, by ELYS on anaphase chromosomes was not affected in HGPS. Immunocytochemistry of (a) control (GMO1652c) and (b) HGPS (HGADFN003) fibroblasts using α‐ELYS and α‐LA antibody, counterstained with DAPI. NPCs cluster in interphase HGPS cells (b), unlike the evenly distributed punctate pattern in interphase control cells (a). Recruitment of ELYS to anaphase chromosomes is not affected in HGPS cells, compared to control. No defect in ELYS localization can be observed in HGPS from prophase to cytokinesis. NPC, nuclear pore complex; HGPS, Hutchinson‐Gilford progeria. n ≥3. Figure S2: Recruitment of basket nucleoporin NUP153 and scaffold nucleoporin NUP107 were not affected in HGPS. Immunocytochemistry of (a) control (GMO1652c) and (b) HGPS (HGADFN003) fibroblasts using α‐ NUP107 and α‐NUP153 antibodies, counterstained with DAPI. NPCs cluster in interphase HGPS cells (b), unlike the evenly spread out punctate pattern in control interphase (a). Recruitment of NUP153 to anaphase chromosomes is not affected in HGPS cells, compared to the control. No defect in NUP153 or NUP107 localization can be observed in HGPS from prophase to cytokinesis. n ≥3. Figure S3: SUN1 aggregates did not colocalize with mAb414. Immunocytochemistry of (a) control (GMO1652c) and (b) HGPS (HGADFN003) fibroblasts using mAb414 and α‐SUN1 antibodies, counterstained with DAPI. -
Snapshot: the Nuclear Envelope II Andrea Rothballer and Ulrike Kutay Institute of Biochemistry, ETH Zurich, 8093 Zurich, Switzerland
SnapShot: The Nuclear Envelope II Andrea Rothballer and Ulrike Kutay Institute of Biochemistry, ETH Zurich, 8093 Zurich, Switzerland H. sapiens D. melanogaster C. elegans S. pombe S. cerevisiae Cytoplasmic filaments RanBP2 (Nup358) Nup358 CG11856 NPP-9 – – – Nup214 (CAN) DNup214 CG3820 NPP-14 Nup146 SPAC23D3.06c Nup159 Cytoplasmic ring and Nup88 Nup88 (Mbo) CG6819 – Nup82 SPBC13A2.02 Nup82 associated factors GLE1 GLE1 CG14749 – Gle1 SPBC31E1.05 Gle1 hCG1 (NUP2L1, NLP-1) tbd CG18789 – Amo1 SPBC15D4.10c Nup42 (Rip1) Nup98 Nup98 CG10198 Npp-10N Nup189N SPAC1486.05 Nup145N, Nup100, Nup116 Nup 98 complex RAE1 (GLE2) Rae1 CG9862 NPP-17 Rae1 SPBC16A3.05 Gle2 (Nup40) Nup160 Nup160 CG4738 NPP-6 Nup120 SPBC3B9.16c Nup120 Nup133 Nup133 CG6958 NPP-15 Nup132, Nup131 SPAC1805.04, Nup133 SPBP35G2.06c Nup107 Nup107 CG6743 NPP-5 Nup107 SPBC428.01c Nup84 Nup96 Nup96 CG10198 NPP-10C Nup189C SPAC1486.05 Nup145C Outer NPC scaffold Nup85 (PCNT1) Nup75 CG5733 NPP-2 Nup-85 SPBC17G9.04c Nup85 (Nup107-160 complex) Seh1 Nup44A CG8722 NPP-18 Seh1 SPAC15F9.02 Seh1 Sec13 Sec13 CG6773 Npp-20 Sec13 SPBC215.15 Sec13 Nup37 tbd CG11875 – tbd SPAC4F10.18 – Nup43 Nup43 CG7671 C09G9.2 – – – Centrin-21 tbd CG174931, CG318021 R08D7.51 Cdc311 SPCC1682.04 Cdc311 Nup205 tbd CG11943 NPP-3 Nup186 SPCC290.03c Nup192 Nup188 tbd CG8771 – Nup184 SPAP27G11.10c Nup188 Central NPC scaffold Nup155 Nup154 CG4579 NPP-8 tbd SPAC890.06 Nup170, Nup157 (Nup53-93 complex) Nup93 tbd CG7262 NPP-13 Nup97, Npp106 SPCC1620.11, Nic96 SPCC1739.14 Nup53(Nup35, MP44) tbd CG6540 NPP-19 Nup40 SPAC19E9.01c -
Identification and Characterization of TMEM33 As a Reticulon-Binding Protein
Kobe J. Med. Sci., Vol. 60, No. 3, pp. E57-E65, 2014 Identification and Characterization of TMEM33 as a Reticulon-binding Protein TAKESHI URADE1,2, YASUNORI YAMAMOTO1, XIA ZHANG1, YONSON KU2, and TOSHIAKI SAKISAKA*1 1Division of Membrane Dynamics, Department of Physiology and Cell Biology, 2Division of Hepato-biliary-pancreatic surgery, Department of Surgery, Kobe University Graduate School of Medicine, Kobe 650-0017 Japan Received 16 July, 2014/ Accepted 31 July, 2014 Key words: TMEM33, Reticulon, ER tubules ABSTRACT Endoplasmic reticulum (ER) is an organelle that has an elaborate and continuous membrane system composed of sheet-like cisternae and a network of interconnected tubules. The ER tubules are shaped by reticulons, a conserved ER membrane protein family. However, how the membrane-shaping activity is regulated remains to be elucidated. To understand the mode of action of reticulons, we isolated TMEM33, a conserved protein harboring three transmembrane domains, as a reticulon 4C-binding protein by affinity chromatography. In addition to reticulon 4C, TMEM33 binds to reticulon 1A, -2B, -3C and a reticulon homology domain-containing protein Arl6IP1. Exogenously expressed TMEM33 localizes at both the ER membrane and the nuclear envelope. Exogenously expressed TMEM33 co-localizes with exogenously expressed reticulon 4C well at the ER sheets and partially at the ER tubules. Exogenously expressed TMEM33 suppresses the exogenously expressed reticulon 4C-induced tubulation of ER. These results suggest that TMEM33 has a potency to suppress the membrane-shaping activity of reticulons, thereby regulating the tubular structure of ER. INTRODUCTION The ER (endoplasmic reticulum) is a continuous membrane system extended from nuclear envelope and composed of interconnected sheets and tubules [11,20,21,25,28]. -
The RNA-Protein Interactome of Differentiated Kidney Tubular Epithelial Cells
BASIC RESEARCH www.jasn.org The RNA-Protein Interactome of Differentiated Kidney Tubular Epithelial Cells Michael Ignarski,1 Constantin Rill,1 Rainer W.J. Kaiser,1 Madlen Kaldirim,1 René Neuhaus,1 Reza Esmaillie,1 Xinping Li,2 Corinna Klein,3 Katrin Bohl,1 Maike Petersen,1 Christian K. Frese,3 Martin Höhne ,1 Ilian Atanassov,2 Markus M. Rinschen,1 Katja Höpker,1 Bernhard Schermer,1,4,5 Thomas Benzing,1,4,5 Christoph Dieterich,6,7 Francesca Fabretti,1 and Roman-Ulrich Müller 1,4,5 1Department II of Internal Medicine and Center for Molecular Medicine Cologne, University of Cologne, Faculty of Medicine and University Hospital of Cologne, Cologne, Germany; 2Proteomics Core Facility, Max Planck Institute for Biology of Ageing, Cologne, Germany; 3Proteomics Facility, Cologne Excellence Cluster on Cellular Stress Responses in Aging-associated Diseases, 4Nephrolab, Cologne Excellence Cluster on Cellular Stress Responses in Aging- associated Diseases, Faculty of Medicine and University Hospital Cologne, and 5Systems Biology of Ageing Cologne, University of Cologne, Cologne, Germany; 6Department of Internal Medicine III, Klaus Tschira Institute for Integrative Computational Cardiology, University Hospital Heidelberg, Heidelberg, Germany; and 7German Center for Cardiovascular Research (DZHK)–Partner site, Heidelberg/Mannheim, Germany ABSTRACT Background RNA-binding proteins (RBPs) are fundamental regulators of cellular biology that affect all steps in the generation and processing of RNA molecules. Recent evidence suggests that regulation of RBPs that modulate both RNA stability and translation may have a profound effect on the proteome. However, regulation of RBPs in clinically relevant experimental conditions has not been studied systematically. Methods We used RNA interactome capture, a method for the global identification of RBPs to characterize the global RNA‐binding proteome (RBPome) associated with polyA-tailed RNA species in murine ciliated epithelial cells of the inner medullary collecting duct. -
Two Distinct Human POM121 Genes: Requirement for the Formation of Nuclear Pore Complexes
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector FEBS Letters 581 (2007) 4910–4916 Two distinct human POM121 genes: Requirement for the formation of nuclear pore complexes Tomoko Funakoshia, Kazuhiro Maeshimaa, Kazuhide Yahatab, Sumio Suganoc, Fumio Imamotob, Naoko Imamotoa,* a Cellular Dynamics Laboratory, Discovery Research Institute, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan b Department of Molecular Biology, BIKEN, Osaka University, Osaka, Japan c The Institute of Medical Science, The University of Tokyo, Tokyo, Japan Received 30 March 2007; revised 12 September 2007; accepted 12 September 2007 Available online 21 September 2007 Edited by Ulrike Kutay essential in somatic cells, as this protein is not ubiquitously ex- Abstract Pom121 is one of the integral membrane components of the nuclear pore complex (NPC) in vertebrate cells. Unlike ro- pressed in mammalian cells [6]. Pom121 is recruited at an early dent cells carrying a single POM121 gene, human cells possess stage of post-mitotic nuclear reassembly in vertebrate cells, multiple POM121 gene loci on chromosome 7q11.23, as a conse- and its turnover on the interphase NPC is very slow [7]. These quence of complex segmental-duplications in this region during findings make Pom121 a strong candidate that could possess human evolution. In HeLa cells, two ‘‘full-length’’ Pom121 are essential roles in anchoring the NPC to the NE. Indeed, transcribed and translated by two distinct genetic loci. RNAi Pom121 was shown to be essential for NPC formation, but experiments showed that efficient depletion of both Pom121 pro- not gp210 in the Xenopus egg extracts [8]. -
Nuclear Pore Density Controls Heterochromatin Reorganization During 2 Senescence 3 4 Charlene Boumendil1, Priya Hari2, Karl C
bioRxiv preprint doi: https://doi.org/10.1101/374033; this version posted July 21, 2018. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. 1 Nuclear pore density controls heterochromatin reorganization during 2 senescence 3 4 Charlene Boumendil1, Priya Hari2, Karl C. F. Olsen1, Juan Carlos Acosta2, Wendy A. 5 Bickmore1* 6 7 1MRC Human Genetics Unit, Institute oF Genetics and Molecular Medicine, University 8 of Edinburgh, Crewe Road South, Edinburgh EH4 2XU 9 10 2Cancer Research UK Edinburgh Centre, Institute oF Genetics and Molecular Medicine, 11 University oF Edinburgh, Crewe Road South, Edinburgh EH4 2XR 12 13 *correspondence to WAB, MRC Human Genetics Unit, Institute oF Genetics and Molecular 14 Medicine, University oF Edinburgh, Crewe Road South, Edinburgh EH4 2XU. 15 [email protected] 16 17 18 19 Abstract 20 Oncogene induced senescence (OIS) is a cell cycle arrest program triggered by oncogenic signalling. 21 An important characteristic oF OIS is activation oF the senescence associated secretory phenotype 22 (SASP)1 which can reinForce cell cycle arrest, lead to paracrine senescence but also promote tumour 23 progression2–4. Concomitant with cell cycle arrest and the SASP activation, OIS cells undergo a striking 24 nuclear chromatin reorganization, with loss oF heterochromatin From the nuclear periphery and the 25 appearance oF internal senescence-associated heterochromatin Foci (SAHF)5. The mechanisms by 26 which SAHF are Formed, and their role in cell cycle arrest and expression oF the SASP, remain poorly 27 understood. -
Table 4. 391 Probe Sets Still Rhythmic After Sleep Deprivation
Table 4. 391 probe sets still rhythmic after sleep deprivation Affymetrix ID Gene Symbol Description Accession time_sin time_cos adj.P.Val 1438211_s_at Dbp D site albumin promoter binding protein BB550183 -0.013 -0.877 1.44E-13 1418174_at Dbp D site albumin promoter binding protein BC018323 -0.036 -0.880 1.74E-13 1425099_a_at Arntl aryl hydrocarbon receptor nuclear translocator-like BC011080 0.135 0.418 1.02E-11 1416958_at Nr1d2 nuclear receptor subfamily 1, group D, member 2 NM_011584 -0.035 -0.397 7.53E-11 1421087_at Per3 period homolog 3 (Drosophila) NM_011067 -0.119 -0.477 3.46E-10 1450779_at Fabp7 fatty acid binding protein 7, brain NM_021272 0.433 0.404 3.82E-10 1424175_at Tef thyrotroph embryonic factor BC017689 -0.113 -0.279 1.39E-09 1435188_at Gm129 gene model 129, (NCBI) BB407125 -0.097 -0.667 4.17E-09 1417602_at Per2 period homolog 2 (Drosophila) AF035830 -0.460 -0.408 5.97E-09 1425560_a_at S100a16 S100 calcium binding protein A16 BC020031 0.228 0.194 5.97E-09 1435459_at Fmo2 flavin containing monooxygenase 2 BM936480 -0.255 -0.426 6.23E-09 1457350_at Per2 period homolog 2 (Drosophila) BG298986 -0.312 -0.485 7.81E-09 1445892_at Per2 Period homolog 2 (Drosophila) BM238318 -0.300 -0.432 1.50E-08 1448383_at Mmp14 matrix metallopeptidase 14 (membrane-inserted) NM_008608 0.082 0.474 3.74E-08 1456046_at Cd93 CD93 antigen AV319144 0.357 0.320 4.89E-08 1429286_at 1190003M12Rik RIKEN cDNA 1190003M12 gene AK004474 -0.511 -0.245 5.08E-08 similar to Putative RNA-binding protein 3 (RNA- 1422660_at LOC671237 AY052560 -0.269 -0.318 5.40E-08 -
Mutations in NUP160 Are Implicated in Steroid-Resistant Nephrotic Syndrome
BASIC RESEARCH www.jasn.org Mutations in NUP160 Are Implicated in Steroid-Resistant Nephrotic Syndrome Feng Zhao,1,2,3,4 Jun-yi Zhu ,2 Adam Richman,2 Yulong Fu,2 Wen Huang,2 Nan Chen,5 Xiaoxia Pan,5 Cuili Yi,1 Xiaohua Ding,1 Si Wang,1 Ping Wang,1 Xiaojing Nie,1,3,4 Jun Huang,1,3,4 Yonghui Yang,1,3,4 Zihua Yu ,1,3,4 and Zhe Han2,6 1Department of Pediatrics, Fuzhou Dongfang Hospital, Fujian, People’s Republic of China; 2Center for Genetic Medicine Research, Children’s National Health System, Washington, DC; 3Department of Pediatrics, Affiliated Dongfang Hospital, Xiamen University, Fujian, People’s Republic of China; 4Department of Pediatrics, Fuzhou Clinical Medical College, Fujian Medical University, Fujian, People’s Republic of China; 5Department of Nephrology, Ruijin Hospital, Shanghai Jiaotong University School of Medicine, Shanghai, People’s Republic of China; and 6Department of Genomics and Precision Medicine, The George Washington University School of Medicine and Health Sciences, Washington, DC ABSTRACT Background Studies have identified mutations in .50 genes that can lead to monogenic steroid-resistant nephrotic syndrome (SRNS). The NUP160 gene, which encodes one of the protein components of the nuclear pore complex nucleoporin 160 kD (Nup160), is expressed in both human and mouse kidney cells. Knockdown of NUP160 impairs mouse podocytes in cell culture. Recently, siblings with SRNS and pro- teinuria in a nonconsanguineous family were found to carry compound-heterozygous mutations in NUP160. Methods We identified NUP160 mutations by whole-exome and Sanger sequencing of genomic DNA from a young girl with familial SRNS and FSGS who did not carry mutations in other genes known to be associated with SRNS.