Product Datasheet: ARP55720 P050

Total Page:16

File Type:pdf, Size:1020Kb

Product Datasheet: ARP55720 P050 Aviva Systems Biology C6orf182 antibody - middle region (ARP55720_P050) Product Number ARP55720_P050 Product Page http://www.avivasysbio.com/c6orf182-antibody-middle-region-arp55720-p050.html Product Name C6orf182 antibody - middle region (ARP55720_P050) Size 100 ul Gene Symbol CEP57L1 Alias Symbols MGC21731, MGC70837, bA487F23.2, cep57R, C6orf182 Protein Size (# AA) 460 amino acids Molecular Weight 54kDa Product Format Liquid. Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose. NCBI Gene Id 285753 Host Rabbit Clonality Polyclonal Concentration Batch dependent within range: 100 ul at 0.5 - 1 mg/ml Official Gene Full Centrosomal protein 57kDa-like 1 Name Description This is a rabbit polyclonal antibody against C6orf182. It was validated on Western Blot by Aviva Systems Biology. At Aviva Systems Biology we manufacture rabbit polyclonal antibodies on a large scale (200-1000 products/month) of high throughput manner. Our antibodies are peptide based and protein family oriented. We usually provide antibodies covering each member of a whole protein family of your interest. We also use our best efforts to provide you antibodies recognize various epitopes of a target protein. For availability of antibody needed for your experiment, please inquire ([email protected]). Peptide Sequence Synthetic peptide located within the following region: LNVEREKNMILEQQAQLQREKEQDQMKLYAKLEKLDVLEKECFRLTTTQK Description of The exact functions of C6orf182 remain unknown. Target Protein Interactions KLC4; LZTS2; FAM161A; KATNAL1; CEP44; TSGA10; CEP70; CEP63; MYO15B; CCDC102B; LENG1; CCDC136; CARD9; RINT1; TRIM54; LMO3; CEP55; ROPN1; TRAPPC2L; TFIP11; NUP62; MTUS2; MID2; MORF4L1; GADD45G; IKZF1; CALCOCO2; HGS; AP1M1; KRT38; TRIP6; TRAF2; TCEB3; SNAPC3 Reconstitution and For short term use, store at 2-8C up to 1 week. For long term storage, store at -20C in Storage small aliquots to prevent freeze-thaw cycles. Lead Time Domestic: within 6-8 weeks delivery International: 6-8 weeks *** Required Wet/Dry Ice Surcharge will automatically be applied upon checkout for the shipment. See Surcharges Blocking Peptide For anti-CEP57L1 (ARP55720_P050) antibody is Catalog # AAP55720 (Previous Catalog # AAPP36427) Immunogen The immunogen is a synthetic peptide directed towards the middle region of human C6orf182 5754 Pacific Center Blvd., Suite 201 San Diego, CA 92121 USA | Tel: (858)552-6979 | [email protected] 1 Complete Anti-C6orf182 (ARP55720_P050) computational species homology data Tissue Tool Find tissues and cell lines supported by DNA array analysis to express C6orf182. Swissprot Id Q8IYX8 Protein Name Centrosomal protein CEP57L1 Protein Accession NP_776191 # Purification Affinity Purified RNA Seq Find tissues and cell lines supported by RNA-seq analysis to express C6orf182. Nucleotide NM_173830 Accession # Conjugation ARP55720_P050-FITC Conjugated Options ARP55720_P050-HRP Conjugated ARP55720_P050-Biotin Conjugated Species Reactivity Cow, Dog, Guinea Pig, Horse, Human, Mouse, Rabbit, Rat, Yeast Application WB Predicted Cow: 93%; Dog: 93%; Guinea Pig: 93%; Horse: 93%; Human: 100%; Mouse: 100%; Homology Based Rabbit: 93%; Rat: 100%; Yeast: 83% on Immunogen Sequence Image 1: Human Jurkat WB Suggested Anti-C6orf182 Antibody Titration: 0.2-1 ug/ml ELISA Titer: 1:312500 Positive Control: Jurkat cell lysate AVIVA SYSTEMS BIOLOGY manufactures and sells quality antibody products covering genome wide proteins. This product is for Research Use Only. Not for diagnostic, human, or veterinary use. Optimal conditions of its use should be determined by end users. 5754 Pacific Center Blvd., Suite 201 San Diego, CA 92121 USA | Tel: (858)552-6979 | [email protected] 2.
Recommended publications
  • Title a New Centrosomal Protein Regulates Neurogenesis By
    Title A new centrosomal protein regulates neurogenesis by microtubule organization Authors: Germán Camargo Ortega1-3†, Sven Falk1,2†, Pia A. Johansson1,2†, Elise Peyre4, Sanjeeb Kumar Sahu5, Loïc Broic4, Camino De Juan Romero6, Kalina Draganova1,2, Stanislav Vinopal7, Kaviya Chinnappa1‡, Anna Gavranovic1, Tugay Karakaya1, Juliane Merl-Pham8, Arie Geerlof9, Regina Feederle10,11, Wei Shao12,13, Song-Hai Shi12,13, Stefanie M. Hauck8, Frank Bradke7, Victor Borrell6, Vijay K. Tiwari§, Wieland B. Huttner14, Michaela Wilsch- Bräuninger14, Laurent Nguyen4 and Magdalena Götz1,2,11* Affiliations: 1. Institute of Stem Cell Research, Helmholtz Center Munich, German Research Center for Environmental Health, Munich, Germany. 2. Physiological Genomics, Biomedical Center, Ludwig-Maximilian University Munich, Germany. 3. Graduate School of Systemic Neurosciences, Biocenter, Ludwig-Maximilian University Munich, Germany. 4. GIGA-Neurosciences, Molecular regulation of neurogenesis, University of Liège, Belgium 5. Institute of Molecular Biology (IMB), Mainz, Germany. 6. Instituto de Neurociencias, Consejo Superior de Investigaciones Científicas and Universidad Miguel Hernández, Sant Joan d’Alacant, Spain. 7. Laboratory for Axon Growth and Regeneration, German Center for Neurodegenerative Diseases (DZNE), Bonn, Germany. 8. Research Unit Protein Science, Helmholtz Centre Munich, German Research Center for Environmental Health, Munich, Germany. 9. Protein Expression and Purification Facility, Institute of Structural Biology, Helmholtz Center Munich, German Research Center for Environmental Health, Munich, Germany. 10. Institute for Diabetes and Obesity, Monoclonal Antibody Core Facility, Helmholtz Center Munich, German Research Center for Environmental Health, Munich, Germany. 11. SYNERGY, Excellence Cluster of Systems Neurology, Biomedical Center, Ludwig- Maximilian University Munich, Germany. 12. Developmental Biology Program, Sloan Kettering Institute, Memorial Sloan Kettering Cancer Center, New York, USA 13.
    [Show full text]
  • 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.
    [Show full text]
  • Supplemental Information Proximity Interactions Among Centrosome
    Current Biology, Volume 24 Supplemental Information Proximity Interactions among Centrosome Components Identify Regulators of Centriole Duplication Elif Nur Firat-Karalar, Navin Rauniyar, John R. Yates III, and Tim Stearns Figure S1 A Myc Streptavidin -tubulin Merge Myc Streptavidin -tubulin Merge BirA*-PLK4 BirA*-CEP63 BirA*- CEP192 BirA*- CEP152 - BirA*-CCDC67 BirA* CEP152 CPAP BirA*- B C Streptavidin PCM1 Merge Myc-BirA* -CEP63 PCM1 -tubulin Merge BirA*- CEP63 DMSO - BirA* CEP63 nocodazole BirA*- CCDC67 Figure S2 A GFP – + – + GFP-CEP152 + – + – Myc-CDK5RAP2 + + + + (225 kDa) Myc-CDK5RAP2 (216 kDa) GFP-CEP152 (27 kDa) GFP Input (5%) IP: GFP B GFP-CEP152 truncation proteins Inputs (5%) IP: GFP kDa 1-7481-10441-1290218-1654749-16541045-16541-7481-10441-1290218-1654749-16541045-1654 250- Myc-CDK5RAP2 150- 150- 100- 75- GFP-CEP152 Figure S3 A B CEP63 – – + – – + GFP CCDC14 KIAA0753 Centrosome + – – + – – GFP-CCDC14 CEP152 binding binding binding targeting – + – – + – GFP-KIAA0753 GFP-KIAA0753 (140 kDa) 1-496 N M C 150- 100- GFP-CCDC14 (115 kDa) 1-424 N M – 136-496 M C – 50- CEP63 (63 kDa) 1-135 N – 37- GFP (27 kDa) 136-424 M – kDa 425-496 C – – Inputs (2%) IP: GFP C GFP-CEP63 truncation proteins D GFP-CEP63 truncation proteins Inputs (5%) IP: GFP Inputs (5%) IP: GFP kDa kDa 1-135136-424425-4961-424136-496FL Ctl 1-135136-424425-4961-424136-496FL Ctl 1-135136-424425-4961-424136-496FL Ctl 1-135136-424425-4961-424136-496FL Ctl Myc- 150- Myc- 100- CCDC14 KIAA0753 100- 100- 75- 75- GFP- GFP- 50- CEP63 50- CEP63 37- 37- Figure S4 A siCtl
    [Show full text]
  • Supplemental Information
    Supplemental information Dissection of the genomic structure of the miR-183/96/182 gene. Previously, we showed that the miR-183/96/182 cluster is an intergenic miRNA cluster, located in a ~60-kb interval between the genes encoding nuclear respiratory factor-1 (Nrf1) and ubiquitin-conjugating enzyme E2H (Ube2h) on mouse chr6qA3.3 (1). To start to uncover the genomic structure of the miR- 183/96/182 gene, we first studied genomic features around miR-183/96/182 in the UCSC genome browser (http://genome.UCSC.edu/), and identified two CpG islands 3.4-6.5 kb 5’ of pre-miR-183, the most 5’ miRNA of the cluster (Fig. 1A; Fig. S1 and Seq. S1). A cDNA clone, AK044220, located at 3.2-4.6 kb 5’ to pre-miR-183, encompasses the second CpG island (Fig. 1A; Fig. S1). We hypothesized that this cDNA clone was derived from 5’ exon(s) of the primary transcript of the miR-183/96/182 gene, as CpG islands are often associated with promoters (2). Supporting this hypothesis, multiple expressed sequences detected by gene-trap clones, including clone D016D06 (3, 4), were co-localized with the cDNA clone AK044220 (Fig. 1A; Fig. S1). Clone D016D06, deposited by the German GeneTrap Consortium (GGTC) (http://tikus.gsf.de) (3, 4), was derived from insertion of a retroviral construct, rFlpROSAβgeo in 129S2 ES cells (Fig. 1A and C). The rFlpROSAβgeo construct carries a promoterless reporter gene, the β−geo cassette - an in-frame fusion of the β-galactosidase and neomycin resistance (Neor) gene (5), with a splicing acceptor (SA) immediately upstream, and a polyA signal downstream of the β−geo cassette (Fig.
    [Show full text]
  • Cytoplasmic E2f4 Forms Organizing Centres for Initiation of Centriole Amplification During Multiciliogenesis
    ARTICLE Received 13 Feb 2017 | Accepted 8 May 2017 | Published 4 Jul 2017 DOI: 10.1038/ncomms15857 OPEN Cytoplasmic E2f4 forms organizing centres for initiation of centriole amplification during multiciliogenesis Munemasa Mori1, Renin Hazan2, Paul S. Danielian2, John E. Mahoney1,w, Huijun Li1, Jining Lu1, Emily S. Miller2, Xueliang Zhu3, Jacqueline A. Lees2 & Wellington V. Cardoso1 Abnormal development of multiciliated cells is a hallmark of a variety of human conditions associated with chronic airway diseases, hydrocephalus and infertility. Multiciliogenesis requires both activation of a specialized transcriptional program and assembly of cytoplasmic structures for large-scale centriole amplification that generates basal bodies. It remains unclear, however, what mechanism initiates formation of these multiprotein complexes in epithelial progenitors. Here we show that this is triggered by nucleocytoplasmic translocation of the transcription factor E2f4. After inducing a transcriptional program of centriole biogenesis, E2f4 forms apical cytoplasmic organizing centres for assembly and nucleation of deuterosomes. Using genetically altered mice and E2F4 mutant proteins we demonstrate that centriole amplification is crucially dependent on these organizing centres and that, without cytoplasmic E2f4, deuterosomes are not assembled, halting multiciliogenesis. Thus, E2f4 integrates nuclear and previously unsuspected cytoplasmic events of centriole amplification, providing new perspectives for the understanding of normal ciliogenesis, ciliopathies and cancer. 1 Columbia Center for Human Development, Department of Medicine, Pulmonary Allergy Critical Care, Columbia University Medical Center, New York City, New York 10032, USA. 2 David H. Koch Institute for Integrative Cancer Research, MIT, Cambridge, Massachusetts 02139, USA. 3 State Key Laboratory of Cell Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, 320 Yueyang Road, Shanghai 200031, China.
    [Show full text]
  • CEP63 Deficiency Promotes P53-Dependent Microcephaly and Reveals a Role for the Centrosome in Meiotic Recombination
    ARTICLE Received 25 Mar 2015 | Accepted 30 May 2015 | Published 9 Jul 2015 DOI: 10.1038/ncomms8676 CEP63 deficiency promotes p53-dependent microcephaly and reveals a role for the centrosome in meiotic recombination Marko Marjanovic´1,2, Carlos Sa´nchez-Huertas1,*, Berta Terre´1,*, Rocı´oGo´mez3, Jan Frederik Scheel4,w, Sarai Pacheco5,6, Philip A. Knobel1, Ana Martı´nez-Marchal5,6, Suvi Aivio1, Lluı´s Palenzuela1, Uwe Wolfrum4, Peter J. McKinnon7, Jose´ A. Suja3, Ignasi Roig5,6, Vincenzo Costanzo8, Jens Lu¨ders1 & Travis H. Stracker1 CEP63 is a centrosomal protein that facilitates centriole duplication and is regulated by the DNA damage response. Mutations in CEP63 cause Seckel syndrome, a human disease characterized by microcephaly and dwarfism. Here we demonstrate that Cep63-deficient mice recapitulate Seckel syndrome pathology. The attrition of neural progenitor cells involves p53-dependent cell death, and brain size is rescued by the deletion of p53. Cell death is not the result of an aberrant DNA damage response but is triggered by centrosome-based mitotic errors. In addition, Cep63 loss severely impairs meiotic recombination, leading to profound male infertility. Cep63-deficient spermatocytes display numerical and structural centrosome aberrations, chromosome entanglements and defective telomere clustering, suggesting that a reduction in centrosome-mediated chromosome movements underlies recombination failure. Our results provide novel insight into the molecular pathology of microcephaly and establish a role for the centrosome in meiotic recombination. 1 Institute for Research in Biomedicine (IRB Barcelona), Barcelona 08028, Spain. 2 Division of Molecular Medicine, Rud–er Bosˇkovic´ Institute, Zagreb 10000, Croatia. 3 Departamento de Biologı´a, Edificio de Biolo´gicas, Universidad Auto´noma de Madrid, Madrid 28049, Spain.
    [Show full text]
  • The Evolutionary Conserved FOXJ1 Target Gene Fam183b Is Essential for Motile Cilia in Xenopus but Dispensable for Ciliary Functi
    www.nature.com/scientificreports OPEN The evolutionary conserved FOXJ1 target gene Fam183b is essential for motile cilia in Xenopus but Received: 16 April 2018 Accepted: 20 September 2018 dispensable for ciliary function in Published: xx xx xxxx mice Anja Beckers1, Tim Ott2, Karin Schuster-Gossler1, Karsten Boldt3, Leonie Alten1, Marius Uefng3, Martin Blum2 & Achim Gossler 1 The transcription factor FOXJ1 is essential for the formation of motile cilia throughout the animal kingdom. Target genes therefore likely constitute an important part of the motile cilia program. Here, we report on the analysis of one of these targets, Fam183b, in Xenopus and mice. Fam183b encodes a protein with unknown function which is conserved from the green algae Chlamydomonas to humans. Fam183b is expressed in tissues harbouring motile cilia in both mouse and frog embryos. FAM183b protein localises to basal bodies of cilia in mIMCD3 cells and of multiciliated cells of the frog larval epidermis. In addition, FAM183b interacts with NUP93, which also localises to basal bodies. During frog embryogenesis, Fam183b was dispensable for laterality specifcation and brain development, but required for ciliogenesis and motility of epidermal multiciliated cells and nephrostomes, i.e. the embryonic kidney. Surprisingly, mice homozygous for a null allele did not display any defects indicative of disrupted motile ciliary function. The lack of a cilia phenotype in mouse and the limited requirements in frog contrast with high sequence conservation and the correlation of gene expression with the presence of motile cilia. This fnding may be explained through compensatory mechanisms at sites where no defects were observed in our FAM183b-loss-of-function studies.
    [Show full text]
  • In Vivo ERK1/2 Reporter Predictively Models Response and Resistance to Combined
    Author Manuscript Published OnlineFirst on July 3, 2019; DOI: 10.1158/1535-7163.MCT-18-1056 Author manuscripts have been peer reviewed and accepted for publication but have not yet been edited. In vivo ERK1/2 reporter predictively models response and resistance to combined BRAF and MEK inhibitors in melanoma Ileine M. Sanchez1, Timothy J. Purwin1, Inna Chervoneva2, Dan A. Erkes1, Mai Q. Nguyen1, Michael A. Davies4, Katherine L. Nathanson5, Kristel Kemper6, Daniel S. Peeper6, and Andrew E. Aplin1,3 1 Department of Cancer Biology, Thomas Jefferson University, Philadelphia, PA 19107, USA 2 Division of Biostatistics, 3 Department of Pharmacology and Experimental Therapeutics Sidney Kimmel Cancer Center at Jefferson, Philadelphia, PA 19107, USA 4 Department of Melanoma Medical Oncology, Division of Cancer Medicine, University of Texas MD Anderson Cancer Center, Houston TX 77030, USA 5 Translational Medicine and Human Genetics, Department of Medicine, Perelman School of Medicine at the University of Pennsylvania, Abramson Cancer Center, Perelman School of Medicine at the University of Pennsylvania, Philadelphia PA 19104, USA 6 Division of Molecular Oncology & Immunology, Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, Netherlands Corresponding author: Andrew E. Aplin, Department of Cancer Biology, Thomas Jefferson University, 233 South 10th Street, Philadelphia, PA 19107. Tel: (215) 503- 7296. Fax: (215) 923-9248; E-mail: [email protected] Running title: In vivo pathway reporting on combination targeted therapy Keywords: melanoma, MEK, vemurafenib, resistance, BRAF 1 Downloaded from mct.aacrjournals.org on September 29, 2021. © 2019 American Association for Cancer Research. Author Manuscript Published OnlineFirst on July 3, 2019; DOI: 10.1158/1535-7163.MCT-18-1056 Author manuscripts have been peer reviewed and accepted for publication but have not yet been edited.
    [Show full text]
  • Cep57 and Cep57l1 Function Redundantly to Recruit the Cep63
    © 2020. Published by The Company of Biologists Ltd | Journal of Cell Science (2020) 133, jcs241836. doi:10.1242/jcs.241836 SHORT REPORT Cep57 and Cep57l1 function redundantly to recruit the Cep63–Cep152 complex for centriole biogenesis Huijie Zhao1,*, Sen Yang1,2,*, Qingxia Chen1,2,3, Xiaomeng Duan1, Guoqing Li1, Qiongping Huang1, Xueliang Zhu1,2,3,‡ and Xiumin Yan1,‡ ABSTRACT SAS-5 in Caenorhabditis elegans) to load Sas-6 for cartwheel The Cep63–Cep152 complex located at the mother centriole recruits formation (Arquint et al., 2015, 2012; Cizmecioglu et al., 2010; Plk4 to initiate centriole biogenesis. How the complex is targeted to Dzhindzhev et al., 2010; Moyer et al., 2015; Ohta et al., 2014, 2018). mother centrioles, however, is unclear. In this study, we show that Several proteins, including Cep135, Cpap (also known as CENPJ), Cep57 and its paralog, Cep57l1, colocalize with Cep63 and Cep152 Cp110 (CCP110) and Cep120, contribute to building the centriolar at the proximal end of mother centrioles in both cycling cells and microtubule (MT) wall and mediate centriole elongation (Azimzadeh multiciliated cells undergoing centriole amplification. Both Cep57 and and Marshall, 2010; Brito et al., 2012; Carvalho-Santos et al., 2012; Cep57l1 bind to the centrosomal targeting region of Cep63. The Comartin et al., 2013; Hung et al., 2004; Kohlmaier et al., 2009; Lin depletion of both proteins, but not either one, blocks loading of the et al., 2013a,b; Loncarek and Bettencourt-Dias, 2018; Schmidt et al., Cep63–Cep152 complex to mother centrioles and consequently 2009). It is known that Cep152 is recruited by Cep63 to act as the cradle prevents centriole duplication.
    [Show full text]
  • Modifier Genes in Microcephaly: a Report on WDR62, CEP63, RAD50
    G C A T T A C G G C A T genes Article Modifier Genes in Microcephaly: A Report on WDR62, CEP63, RAD50 and PCNT Variants Exacerbating Disease Caused by Biallelic Mutations of ASPM and CENPJ Ehtisham Ul Haq Makhdoom 1,2,3,†, Syeda Seema Waseem 1,4,†, Maria Iqbal 1,2,4, Uzma Abdullah 5 , Ghulam Hussain 3, Maria Asif 1,4, Birgit Budde 1 , Wolfgang Höhne 1, Sigrid Tinschert 6, Saadia Maryam Saadi 2 , Hammad Yousaf 2, Zafar Ali 7, Ambrin Fatima 8, Emrah Kaygusuz 9 , Ayaz Khan 2 , Muhammad Jameel 2, Sheraz Khan 2 , Muhammad Tariq 2 , Iram Anjum 10 , Janine Altmüller 1, Holger Thiele 1, Stefan Höning 4, Shahid Mahmood Baig 2,8,11, Peter Nürnberg 1,12 and Muhammad Sajid Hussain 1,4,12,* 1 Cologne Center for Genomics (CCG), Faculty of Medicine and University Hospital Cologne, University of Cologne, 50931 Cologne, Germany; [email protected] (E.U.H.M.); [email protected] (S.S.W.); [email protected] (M.I.); [email protected] (M.A.); [email protected] (B.B.); [email protected] (W.H.); [email protected] (J.A.); [email protected] (H.T.); [email protected] (P.N.) 2 Human Molecular Genetics Laboratory, Health Biotechnology Division, National Institute for Biotechnology and Genetic Engineering (NIBGE) College, PIEAS, Faisalabad 38000, Pakistan; [email protected] (S.M.S.); [email protected] (H.Y.); [email protected] (A.K.); [email protected] (M.J.); [email protected] (S.K.); [email protected] (M.T.); [email protected] (S.M.B.) 3 Citation: Makhdoom, E.U.H.; Neurochemicalbiology and Genetics Laboratory (NGL), Department of Physiology, Faculty of Life Sciences, Waseem, S.S.; Iqbal, M.; Abdullah, U.; Government College University, Faisalabad 38000, Pakistan; [email protected] 4 Hussain, G.; Asif, M.; Budde, B.; Institute of Biochemistry I, Medical Faculty, University of Cologne, 50931 Cologne, Germany; [email protected] Höhne, W.; Tinschert, S.; Saadi, 5 University Institute of Biochemistry and Biotechnology (UIBB), PMAS-Arid Agriculture University, S.M.; et al.
    [Show full text]
  • Multicilin Drives Centriole Biogenesis Via E2f Proteins
    Downloaded from genesdev.cshlp.org on September 26, 2021 - Published by Cold Spring Harbor Laboratory Press Multicilin drives centriole biogenesis via E2f proteins Lina Ma,1 Ian Quigley,1 Heymut Omran,2 and Chris Kintner1,3 1The Salk Institute for Biological Studies, La Jolla 92037, California, USA; 2Department of Pediatrics, University Hospital Muenster, 48149 Muenster; Germany Multiciliate cells employ hundreds of motile cilia to produce fluid flow, which they nucleate and extend by first assembling hundreds of centrioles. In most cells, entry into the cell cycle allows centrioles to undergo a single round of duplication, but in differentiating multiciliate cells, massive centriole assembly occurs in G0 by a process initiated by a small coiled-coil protein, Multicilin. Here we show that Multicilin acts by forming a ternary complex with E2f4 or E2f5 and Dp1 that binds and activates most of the genes required for centriole biogenesis, while other cell cycle genes remain off. This complex also promotes the deuterosome pathway of centriole biogenesis by activating the expression of deup1 but not its paralog, cep63. Finally, we show that this complex is disabled by mutations in human Multicilin that cause a severe congenital mucociliary clearance disorder due to reduced generation of multiple cilia. By coopting the E2f regulation of cell cycle genes, Multicilin drives massive centriole assembly in epithelial progenitors in a manner required for multiciliate cell differentiation. [Keywords: centrioles; e2f4; multiciliate cells] Supplemental material is available for this article. Received April 17, 2014; revised version accepted May 27, 2014. The centriole, a cylindrical organelle made up of triplet cently have come into focus molecularly (Tang 2013).
    [Show full text]
  • Cep63 Knockout Inhibits the Malignant Phenotypes of Papillary Thyroid Cancer Cell Line TPC‑1
    ONCOLOGY REPORTS 46: 199, 2021 Cep63 knockout inhibits the malignant phenotypes of papillary thyroid cancer cell line TPC‑1 CHENGUANG LIU1,2*, FANGQIN YU1,2*, RUNSHENG MA1,2, LELE ZHANG1,2, GONGBO DU1,2, DONGPENG NIU1,2 and DETAO YIN1,2 1Department of Thyroid Surgery, The First Affiliated Hospital of Zhengzhou University; 2Key Discipline Laboratory of Clinical Medicine of Henan, Zhengzhou, Henan 450052, P.R. China Received November 8, 2020; Accepted June 30, 2021 DOI: 10.3892/or.2021.8150 Abstract. The present study was designed to observe the Papillary thyroid cancer (PTC) is the most common patholog‑ expression of the centrosomal protein 63 in papillary thyroid ical type and accounts for approximately 70‑80% of all thyroid cancer (PTC) tissues and cells and to explore the clinical cancers (2‑5). Most PTCs can be treated with thyroid surgery significance of Cep63 expression in PTC. Primary PTC alone or combined with radioactive iodine therapy. Although tissues and matched normal thyroid tissues were collected, numerous genetic changes have been revealed in thyroid and the Cep63 expression level was determined by reverse cancer, the molecular mechanism of PTC progression has not transcription‑quantitative PCR and western blotting. A stable been fully studied. Therefore, further study of the mechanism Cep63‑knockout cell line was constructed to assess the prolif‑ by which PTC occurs and develops is urgently needed. eration, invasion, migration and apoptosis abilities in vitro. A Centrosomes are the microtubule‑organizing centers subcutaneous tumorigenesis model was established in nude of animal cells that ensure normal behavior of chromo‑ mice to evaluate the effect of Cep63 on tumor growth and somes during mitosis, so their number must be precisely proliferation in vivo.
    [Show full text]