Structural and Functional Dissection of Reovirus Capsid Folding and Assembly by the Prefoldin-Tric/CCT Chaperone Network
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CCT3 Rabbit Pab
Leader in Biomolecular Solutions for Life Science CCT3 Rabbit pAb Catalog No.: A6547 3 Publications Basic Information Background Catalog No. The protein encoded by this gene is a molecular chaperone that is a member of the A6547 chaperonin containing TCP1 complex (CCT), also known as the TCP1 ring complex (TRiC). This complex consists of two identical stacked rings, each containing eight different Observed MW proteins. Unfolded polypeptides enter the central cavity of the complex and are folded 60kDa in an ATP-dependent manner. The complex folds various proteins, including actin and tubulin. Alternate transcriptional splice variants have been characterized for this gene. Calculated MW In addition, a pseudogene of this gene has been found on chromosome 8. 56kDa/60kDa Category Primary antibody Applications WB,IHC,IF Cross-Reactivity Human, Mouse, Rat Recommended Dilutions Immunogen Information WB 1:500 - 1:2000 Gene ID Swiss Prot 7203 P49368 IHC 1:50 - 1:200 Immunogen 1:50 - 1:200 IF Recombinant fusion protein containing a sequence corresponding to amino acids 1-300 of human CCT3 (NP_005989.3). Synonyms CCT3;CCT-gamma;CCTG;PIG48;TCP-1-gamma;TRIC5 Contact Product Information www.abclonal.com Source Isotype Purification Rabbit IgG Affinity purification Storage Store at -20℃. Avoid freeze / thaw cycles. Buffer: PBS with 0.02% sodium azide,50% glycerol,pH7.3. Validation Data Western blot analysis of extracts of various cell lines, using CCT3 antibody (A6547) at 1:1000 dilution. Secondary antibody: HRP Goat Anti-Rabbit IgG (H+L) (AS014) at 1:10000 dilution. Lysates/proteins: 25ug per lane. Blocking buffer: 3% nonfat dry milk in TBST. -
A Computational Approach for Defining a Signature of Β-Cell Golgi Stress in Diabetes Mellitus
Page 1 of 781 Diabetes A Computational Approach for Defining a Signature of β-Cell Golgi Stress in Diabetes Mellitus Robert N. Bone1,6,7, Olufunmilola Oyebamiji2, Sayali Talware2, Sharmila Selvaraj2, Preethi Krishnan3,6, Farooq Syed1,6,7, Huanmei Wu2, Carmella Evans-Molina 1,3,4,5,6,7,8* Departments of 1Pediatrics, 3Medicine, 4Anatomy, Cell Biology & Physiology, 5Biochemistry & Molecular Biology, the 6Center for Diabetes & Metabolic Diseases, and the 7Herman B. Wells Center for Pediatric Research, Indiana University School of Medicine, Indianapolis, IN 46202; 2Department of BioHealth Informatics, Indiana University-Purdue University Indianapolis, Indianapolis, IN, 46202; 8Roudebush VA Medical Center, Indianapolis, IN 46202. *Corresponding Author(s): Carmella Evans-Molina, MD, PhD ([email protected]) Indiana University School of Medicine, 635 Barnhill Drive, MS 2031A, Indianapolis, IN 46202, Telephone: (317) 274-4145, Fax (317) 274-4107 Running Title: Golgi Stress Response in Diabetes Word Count: 4358 Number of Figures: 6 Keywords: Golgi apparatus stress, Islets, β cell, Type 1 diabetes, Type 2 diabetes 1 Diabetes Publish Ahead of Print, published online August 20, 2020 Diabetes Page 2 of 781 ABSTRACT The Golgi apparatus (GA) is an important site of insulin processing and granule maturation, but whether GA organelle dysfunction and GA stress are present in the diabetic β-cell has not been tested. We utilized an informatics-based approach to develop a transcriptional signature of β-cell GA stress using existing RNA sequencing and microarray datasets generated using human islets from donors with diabetes and islets where type 1(T1D) and type 2 diabetes (T2D) had been modeled ex vivo. To narrow our results to GA-specific genes, we applied a filter set of 1,030 genes accepted as GA associated. -
Structure of the Molecular Chaperone Prefoldin
CORE Metadata, citation and similar papers at core.ac.uk Provided by Elsevier - Publisher Connector Cell, Vol. 103, 621±632, November 10, 2000, Copyright 2000 by Cell Press Structure of the Molecular Chaperone Prefoldin: Unique Interaction of Multiple Coiled Coil Tentacles with Unfolded Proteins of newly synthesized bacterial %10ف ,Ralf Siegert,² Michel R. Leroux,²³ 1999). In addition Clemens Scheufler, F. Ulrich Hartl,* proteins complete their folding in the sequestered envi- and Ismail Moarefi* ronment provided by GroEL/GroES (Horwich et al., 1993; Max-Planck Institut fuÈ r Biochemie Ewalt et al., 1997; Houry et al., 1999). The eukaryotic Am Klopferspitz 18a Hsp70 chaperone machine also binds nascent chains D82152 Martinsried (Beckmann et al., 1990; Nelson et al., 1992; Eggers et Germany al., 1997; Thulasiraman et al., 1999), and some proteins, including actins and tubulins, depend on the Group II cytosolic chaperonin TRiC (TCP-1 ring Complex; also Summary termed CCT) for folding (Frydman et al., 1992; Gao et al., 1992; Yaffe et al., 1992; Kubota et al., 1995; Siegers Prefoldin (GimC) is a hexameric molecular chaperone et al., 1999). complex built from two related classes of subunits The archaeal Group II chaperonin (thermosome) is and present in all eukaryotes and archaea. Prefoldin closely related to its eukaryotic homologue TRiC (Gutsche et al., 1999). In contrast, Hsp70 proteins and interacts with nascent polypeptide chains and, in vitro, TF are generally missing from the archaeal kingdom can functionally substitute for the Hsp70 chaperone though some archaea have acquired Hsp70, presumably system in stabilizing non-native proteins for subse- by lateral gene transfer (Gribaldo et al., 1999). -
1 Supporting Information for a Microrna Network Regulates
Supporting Information for A microRNA Network Regulates Expression and Biosynthesis of CFTR and CFTR-ΔF508 Shyam Ramachandrana,b, Philip H. Karpc, Peng Jiangc, Lynda S. Ostedgaardc, Amy E. Walza, John T. Fishere, Shaf Keshavjeeh, Kim A. Lennoxi, Ashley M. Jacobii, Scott D. Rosei, Mark A. Behlkei, Michael J. Welshb,c,d,g, Yi Xingb,c,f, Paul B. McCray Jr.a,b,c Author Affiliations: Department of Pediatricsa, Interdisciplinary Program in Geneticsb, Departments of Internal Medicinec, Molecular Physiology and Biophysicsd, Anatomy and Cell Biologye, Biomedical Engineeringf, Howard Hughes Medical Instituteg, Carver College of Medicine, University of Iowa, Iowa City, IA-52242 Division of Thoracic Surgeryh, Toronto General Hospital, University Health Network, University of Toronto, Toronto, Canada-M5G 2C4 Integrated DNA Technologiesi, Coralville, IA-52241 To whom correspondence should be addressed: Email: [email protected] (M.J.W.); yi- [email protected] (Y.X.); Email: [email protected] (P.B.M.) This PDF file includes: Materials and Methods References Fig. S1. miR-138 regulates SIN3A in a dose-dependent and site-specific manner. Fig. S2. miR-138 regulates endogenous SIN3A protein expression. Fig. S3. miR-138 regulates endogenous CFTR protein expression in Calu-3 cells. Fig. S4. miR-138 regulates endogenous CFTR protein expression in primary human airway epithelia. Fig. S5. miR-138 regulates CFTR expression in HeLa cells. Fig. S6. miR-138 regulates CFTR expression in HEK293T cells. Fig. S7. HeLa cells exhibit CFTR channel activity. Fig. S8. miR-138 improves CFTR processing. Fig. S9. miR-138 improves CFTR-ΔF508 processing. Fig. S10. SIN3A inhibition yields partial rescue of Cl- transport in CF epithelia. -
2020 Program Book
PROGRAM BOOK Note that TAGC was cancelled and held online with a different schedule and program. This document serves as a record of the original program designed for the in-person meeting. April 22–26, 2020 Gaylord National Resort & Convention Center Metro Washington, DC TABLE OF CONTENTS About the GSA ........................................................................................................................................................ 3 Conference Organizers ...........................................................................................................................................4 General Information ...............................................................................................................................................7 Mobile App ....................................................................................................................................................7 Registration, Badges, and Pre-ordered T-shirts .............................................................................................7 Oral Presenters: Speaker Ready Room - Camellia 4.......................................................................................7 Poster Sessions and Exhibits - Prince George’s Exhibition Hall ......................................................................7 GSA Central - Booth 520 ................................................................................................................................8 Internet Access ..............................................................................................................................................8 -
Genetics of Tuberous Sclerosis Complex: Implications for Clinical Practice
Journal name: The Application of Clinical Genetics Article Designation: REVIEW Year: 2017 Volume: 10 The Application of Clinical Genetics Dovepress Running head verso: Caban et al Running head recto: Genetics of TSC open access to scientific and medical research DOI: http://dx.doi.org/10.2147/TACG.S90262 Open Access Full Text Article REVIEW Genetics of tuberous sclerosis complex: implications for clinical practice Carolina Caban1,2 Abstract: Tuberous sclerosis complex (TSC) is a multisystem disorder that results from hetero- Nubaira Khan1,2 zygous mutations in either TSC1 or TSC2. The primary organ systems that are affected include Daphne M Hasbani3 the brain, skin, lung, kidney, and heart, all with variable frequency, penetrance, and severity. Peter B Crino1,2 Neurological features include epilepsy, autism, and intellectual disability. There are more than 1,500 known pathogenic variants for TSC1 and TSC2, including deletion, nonsense, and missense 1Department of Neurology, 2Shriners Hospitals Pediatric Research mutations, and all pathogenic mutations are inactivating, leading to loss of function effects on Center, Temple University School of the encoded proteins TSC1 and TSC2. These proteins form a complex to constitutively inhibit 3 Medicine, Department of Neurology, mechanistic target of rapamycin (mTOR) signaling cascade, and as a consequence, mTOR signal- St. Christopher’s Hospital for Children, Drexel University College ing is constitutively active within all TSC-associated lesions. The mTOR inhibitors rapamycin For personal use only. of Medicine, Philadelphia, PA, USA (sirolimus) and everolimus have been shown to reduce the size of renal and brain lesions and improve pulmonary function in TSC, and these compounds may also decrease seizure frequency. -
PTEN, and KCTD13 and RAF1) That Significantly Enhanced Or Suppressed Cell Proliferation Phenotypes
bioRxiv preprint doi: https://doi.org/10.1101/185355; this version posted September 20, 2017. 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-NC-ND 4.0 International license. Pervasive epistasis modulates neurodevelopmental defects of the autism-associated 16p11.2 deletion Janani Iyer1,9, Mayanglambam Dhruba Singh1,9, Matthew Jensen1,2,9, Payal Patel1,9, Lucilla Pizzo1, Emily Huber1, Haley Koerselman3, Alexis T. Weiner1, Paola Lepanto4, Komal Vadodaria1, Alexis Kubina1, Qingyu Wang1,2, Abigail Talbert1, Sneha Yennawar1, Jose Badano4, J. Robert Manak3,5, Melissa M. Rolls1, Arjun Krishnan6,7, and Santhosh Girirajan1,2,8* 1. Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802 2. Bioinformatics and Genomics Program, Huck Institute of Life Sciences, The Pennsylvania State University, University Park, PA 16802 3. Departments of Biology, University of Iowa, Iowa City, IA 52242 4. Human Molecular Genetics Laboratory, Institut Pasteur de Montevideo, Montevideo, Uruguay 5. Department of Pediatrics, University of Iowa, Iowa City, IA 52242 6. Department of Computational Mathematics, Science and Engineering, Michigan State University, East Lansing, MI 48824 7. Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824 8. Department of Anthropology, The Pennsylvania State University, University Park, PA 16802 9. These authors contributed equally to this work. Correspondence to: Santhosh Girirajan 205A Life Sciences Building The Pennsylvania State University University Park, PA 16802 E-mail: [email protected] Phone: 814-865-0674 1 bioRxiv preprint doi: https://doi.org/10.1101/185355; this version posted September 20, 2017. -
Downloaded from the Xena Public Data Hubs (
www.nature.com/scientificreports OPEN Investigating Chaperonin- Containing TCP-1 subunit 2 as an essential component of the chaperonin complex for tumorigenesis Anne E. Showalter1,6, Ana C. Martini1,6, Daniel Nierenberg1, Kristen Hosang1, Naima Ahmed Fahmi2,3, Priya Gopalan4, Amr S. Khaled5, Wei Zhang 2,3 & Annette R. Khaled1* Chaperonin-containing TCP-1 (CCT or TRiC) is a multi-subunit complex that folds many of the proteins essential for cancer development. CCT is expressed in diverse cancers and could be an ideal therapeutic target if not for the fact that the complex is encoded by eight distinct genes, complicating the development of inhibitors. Few defnitive studies addressed the role of specifc subunits in promoting the chaperonin’s function in cancer. To this end, we investigated the activity of CCT2 (CCTβ) by overexpressing or depleting the subunit in breast epithelial and breast cancer cells. We found that increasing total CCT2 in cells by 1.3-1.8-fold using a lentiviral system, also caused CCT3, CCT4, and CCT5 levels to increase. Likewise, silencing cct2 gene expression by ~50% caused other CCT subunits to decrease. Cells expressing CCT2 were more invasive and had a higher proliferative index. CCT2 depletion in a syngeneic murine model of triple negative breast cancer (TNBC) prevented tumor growth. These results indicate that the CCT2 subunit is integral to the activity of the chaperonin and is needed for tumorigenesis. Hence CCT2 could be a viable target for therapeutic development in breast and other cancers. Te hallmarks of cancer (uncontrolled proliferation, genomic instability, metastasis, etc.) reveal the complex nature of this disease and the challenges faced developing efective therapeutics1,2. -
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. -
Analysis of the Indacaterol-Regulated Transcriptome in Human Airway
Supplemental material to this article can be found at: http://jpet.aspetjournals.org/content/suppl/2018/04/13/jpet.118.249292.DC1 1521-0103/366/1/220–236$35.00 https://doi.org/10.1124/jpet.118.249292 THE JOURNAL OF PHARMACOLOGY AND EXPERIMENTAL THERAPEUTICS J Pharmacol Exp Ther 366:220–236, July 2018 Copyright ª 2018 by The American Society for Pharmacology and Experimental Therapeutics Analysis of the Indacaterol-Regulated Transcriptome in Human Airway Epithelial Cells Implicates Gene Expression Changes in the s Adverse and Therapeutic Effects of b2-Adrenoceptor Agonists Dong Yan, Omar Hamed, Taruna Joshi,1 Mahmoud M. Mostafa, Kyla C. Jamieson, Radhika Joshi, Robert Newton, and Mark A. Giembycz Departments of Physiology and Pharmacology (D.Y., O.H., T.J., K.C.J., R.J., M.A.G.) and Cell Biology and Anatomy (M.M.M., R.N.), Snyder Institute for Chronic Diseases, Cumming School of Medicine, University of Calgary, Calgary, Alberta, Canada Received March 22, 2018; accepted April 11, 2018 Downloaded from ABSTRACT The contribution of gene expression changes to the adverse and activity, and positive regulation of neutrophil chemotaxis. The therapeutic effects of b2-adrenoceptor agonists in asthma was general enriched GO term extracellular space was also associ- investigated using human airway epithelial cells as a therapeu- ated with indacaterol-induced genes, and many of those, in- tically relevant target. Operational model-fitting established that cluding CRISPLD2, DMBT1, GAS1, and SOCS3, have putative jpet.aspetjournals.org the long-acting b2-adrenoceptor agonists (LABA) indacaterol, anti-inflammatory, antibacterial, and/or antiviral activity. Numer- salmeterol, formoterol, and picumeterol were full agonists on ous indacaterol-regulated genes were also induced or repressed BEAS-2B cells transfected with a cAMP-response element in BEAS-2B cells and human primary bronchial epithelial cells by reporter but differed in efficacy (indacaterol $ formoterol . -
Chaperonin-Assisted Protein Folding: a Chronologue
Quarterly Reviews of Chaperonin-assisted protein folding: Biophysics a chronologue cambridge.org/qrb Arthur L. Horwich1,2 and Wayne A. Fenton2 1Howard Hughes Medical Institute, Yale School of Medicine, Boyer Center, 295 Congress Avenue, New Haven, CT 06510, USA and 2Department of Genetics, Yale School of Medicine, Boyer Center, 295 Congress Avenue, New Invited Review Haven, CT 06510, USA Cite this article: Horwich AL, Fenton WA (2020). Chaperonin-assisted protein folding: a Abstract chronologue. Quarterly Reviews of Biophysics This chronologue seeks to document the discovery and development of an understanding of – 53, e4, 1 127. https://doi.org/10.1017/ oligomeric ring protein assemblies known as chaperonins that assist protein folding in the cell. S0033583519000143 It provides detail regarding genetic, physiologic, biochemical, and biophysical studies of these Received: 16 August 2019 ATP-utilizing machines from both in vivo and in vitro observations. The chronologue is orga- Revised: 21 November 2019 nized into various topics of physiology and mechanism, for each of which a chronologic order Accepted: 26 November 2019 is generally followed. The text is liberally illustrated to provide firsthand inspection of the key Key words: pieces of experimental data that propelled this field. Because of the length and depth of this Chaperonin; GroEL; GroES; Hsp60; protein piece, the use of the outline as a guide for selected reading is encouraged, but it should also be folding of help in pursuing the text in direct order. Author for correspondence: Arthur L. Horwich, E-mail: [email protected] Table of contents I. Foundational discovery of Anfinsen and coworkers – the amino acid sequence of a polypeptide contains all of the information required for folding to the native state 7 II. -
Anti-NUDC Antibody (Aa282-331) Rabbit Anti Human Polyclonal Antibody Catalog # ALS17941
10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 Anti-NUDC Antibody (aa282-331) Rabbit Anti Human Polyclonal Antibody Catalog # ALS17941 Specification Anti-NUDC Antibody (aa282-331) - Product Information Application WB, IHC-P, E Primary Accession Q9Y266 Predicted Human, Mouse, Rat Host Rabbit Clonality Polyclonal Isotype IgG Calculated MW 38243 Anti-NUDC Antibody (aa282-331) - Additional Information Gene ID 10726 Alias Symbol NUDC Other Names NUDC, HNUDC, MNUDC, NPD011, Nuclear migration protein nudC Target/Specificity NudC Antibody detects endogenous levels of total NudC protein. Reconstitution & Storage Immunoaffinity purified Precautions Anti-NUDC Antibody (aa282-331) is for research use only and not for use in diagnostic or therapeutic procedures. Anti-NUDC Antibody (aa282-331) - Protein Information Name NUDC Function Plays a role in neurogenesis and neuronal migration (By similarity). Necessary for correct formation of mitotic spindles and chromosome separation during mitosis (PubMed:<a href="http://www.uniprot.org/c itations/12852857" Page 1/2 10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 target="_blank">12852857</a>, PubMed:<a href="http://www.uniprot.org/ci tations/12679384" target="_blank">12679384</a>, PubMed:<a href="http://www.uniprot.org/ci tations/25789526" target="_blank">25789526</a>). Necessary for cytokinesis and cell proliferation (PubMed:<a href="http://www. uniprot.org/citations/12852857" target="_blank">12852857</a>, PubMed:<a href="http://www.uniprot.org/ci tations/12679384" target="_blank">12679384</a>). Cellular Location Cytoplasm, cytoskeleton. Nucleus. Cytoplasm, cytoskeleton, spindle. Midbody Note=In a filamentous pattern adjacent to the nucleus of migrating cerebellar granule cells.