Binding and Stabilization of Collagen Mrnasᰔ Azariyas A
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RNA-Dependent RNA Polymerase Consensus Sequence of the L-A Double-Stranded RNA Virus: Definition of Essential Domains
Proc. Nati. Acad. Sci. USA Vol. 89, pp. 2185-2189, March 1992 Biochemistry RNA-dependent RNA polymerase consensus sequence of the L-A double-stranded RNA virus: Definition of essential domains JUAN CARLOS RIBAS AND REED B. WICKNER Section on the Genetics of Simple Eukaryotes, Laboratory of Biochemical Pharmacology, National Institute of Diabetes and Digestive and Kidney Diseases, Building 8, Room 207, National Institutes of Health, Bethesda, MD 20892 Communicated by Herbert Tabor, November 27, 1991 (received for review October 2, 1991) ABSTRACT The L-A double-stranded RNA virus of Sac- lacking M1 (reviewed in refs. 10 and 18). M1 depends on L-A charomyces cerevisiac makes a gag-pol fusion protein by a -1 for its coat and replication proteins (19). MAK10 is one of ribosomal frameshift. The pol amino acid sequence includes three chromosomal genes needed for L-A virus propagation consensus patterns typical of the RNA-dependent RNA poly- within yeast cells (20). In a maklO host, L-A proteins merases (EC 2.7.7.48) of (+) strand and double-stranded RNA expressed from a cDNA clone of L-A support the replication viruses of animals and plants. We have carried out "alanine- of the M1 satellite virus but (for unknown reasons) do not scanning mutagenesis" of the region of L-A including the two support propagation of the L-A virus itself (21). Thus, while most conserved polymerase motifs, SG...T...NT..N (. = any L-A requires the MAK10 product itself, M1 requires MAK10 amino acid) and GDD. By constructing and analyzing 46 only because it requires the L-A-encoded proteins. -
Transiently Structured Head Domains Control Intermediate Filament Assembly
Transiently structured head domains control intermediate filament assembly Xiaoming Zhoua, Yi Lina,1, Masato Katoa,b,c, Eiichiro Morid, Glen Liszczaka, Lillian Sutherlanda, Vasiliy O. Sysoeva, Dylan T. Murraye, Robert Tyckoc, and Steven L. McKnighta,2 aDepartment of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390; bInstitute for Quantum Life Science, National Institutes for Quantum and Radiological Science and Technology, 263-8555 Chiba, Japan; cLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520; dDepartment of Future Basic Medicine, Nara Medical University, 840 Shijo-cho, Kashihara, Nara, Japan; and eDepartment of Chemistry, University of California, Davis, CA 95616 Contributed by Steven L. McKnight, January 2, 2021 (sent for review October 30, 2020; reviewed by Lynette Cegelski, Tatyana Polenova, and Natasha Snider) Low complexity (LC) head domains 92 and 108 residues in length are, IF head domains might facilitate filament assembly in a manner respectively, required for assembly of neurofilament light (NFL) and analogous to LC domain function by RNA-binding proteins in the desmin intermediate filaments (IFs). As studied in isolation, these IF assembly of RNA granules. head domains interconvert between states of conformational disor- IFs are defined by centrally located α-helical segments 300 to der and labile, β-strand–enriched polymers. Solid-state NMR (ss-NMR) 350 residues in length. These central, α-helical segments are spectroscopic studies of NFL and desmin head domain polymers re- flanked on either end by head and tail domains thought to be veal spectral patterns consistent with structural order. -
Microtubule-Associated Protein Tau (Molecular Pathology/Neurodegenerative Disease/Neurofibriliary Tangles) M
Proc. Nati. Acad. Sci. USA Vol. 85, pp. 4051-4055, June 1988 Medical Sciences Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: Identification as the microtubule-associated protein tau (molecular pathology/neurodegenerative disease/neurofibriliary tangles) M. GOEDERT*, C. M. WISCHIK*t, R. A. CROWTHER*, J. E. WALKER*, AND A. KLUG* *Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, United Kingdom; and tDepartment of Psychiatry, University of Cambridge Clinical School, Hills Road, Cambridge CB2 2QQ, United Kingdom Contributed by A. Klug, March 1, 1988 ABSTRACT Screening of cDNA libraries prepared from (21). This task is made all the more difficult because there is the frontal cortex ofan zheimer disease patient and from fetal no functional or physiological assay for the protein(s) of the human brain has led to isolation of the cDNA for a core protein PHF. The only identification so far possible is the morphol- of the paired helical fiament of Alzheimer disease. The partial ogy of the PHFs at the electron microscope level, and here amino acid sequence of this core protein was used to design we would accept only experiments on isolated individual synthetic oligonucleotide probes. The cDNA encodes a protein of filaments, not on neurofibrillary tangles (in which other 352 amino acids that contains a characteristic amino acid repeat material might be occluded). One thus needs a label or marker in its carboxyl-terminal half. This protein is highly homologous for the PHF itself, which can at the same time be used to to the sequence ofthe mouse microtubule-assoiated protein tau follow the steps of the biochemical purification. -
Neurofilaments: Neurobiological Foundations for Biomarker Applications
Neurofilaments: neurobiological foundations for biomarker applications Arie R. Gafson1, Nicolas R. Barthelmy2*, Pascale Bomont3*, Roxana O. Carare4*, Heather D. Durham5*, Jean-Pierre Julien6,7*, Jens Kuhle8*, David Leppert8*, Ralph A. Nixon9,10,11,12*, Roy Weller4*, Henrik Zetterberg13,14,15,16*, Paul M. Matthews1,17 1 Department of Brain Sciences, Imperial College, London, UK 2 Department of Neurology, Washington University School of Medicine, St Louis, MO, USA 3 a ATIP-Avenir team, INM, INSERM , Montpellier university , Montpellier , France. 4 Clinical Neurosciences, Faculty of Medicine, University of Southampton, Southampton General Hospital, Southampton, United Kingdom 5 Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, Québec, Canada 6 Department of Psychiatry and Neuroscience, Laval University, Quebec, Canada. 7 CERVO Brain Research Center, 2601 Chemin de la Canardière, Québec, QC, G1J 2G3, Canada 8 Neurologic Clinic and Policlinic, Departments of Medicine, Biomedicine and Clinical Research, University Hospital Basel, University of Basel, Basel, Switzerland. 9 Center for Dementia Research, Nathan Kline Institute, Orangeburg, NY, 10962, USA. 10Departments of Psychiatry, New York University School of Medicine, New York, NY, 10016, 11 Neuroscience Institute, New York University School of Medicine, New York, NY, 10016, USA. 12Department of Cell Biology, New York University School of Medicine, New York, NY, 10016, USA 13 University College London Queen Square Institute of Neurology, London, UK 14 UK Dementia Research Institute at University College London 15 Department of Psychiatry and Neurochemistry, Institute of Neuroscience and Physiology, the Sahlgrenska Academy at the University of Gothenburg, Mölndal, Sweden 16 Clinical Neurochemistry Laboratory, Sahlgrenska University Hospital, Mölndal, Sweden 17 UK Dementia Research Institute at Imperial College, London * Co-authors ordered alphabetically Address for correspondence: Prof. -
INITIAL EXPRESSION of NEUROFILAMENTS and VIMENTIN in the CENTRAL and PERIPHERAL NERVOUS SYSTEM of the MOUSE EMBRYO in Vivol
0270-6474/84/0408-2080$02.00/O The Journal of Neuroscience Copyright 0 Society for Neuroscience Vol. 4, No. 8, pp. 2080-2094 Printed in U.S.A. August 1984 INITIAL EXPRESSION OF NEUROFILAMENTS AND VIMENTIN IN THE CENTRAL AND PERIPHERAL NERVOUS SYSTEM OF THE MOUSE EMBRYO IN VIVOl PHILIPPE COCHARD’ AND DENISE PAULIN* Institut d%mbryologie du Centre National de la Recherche Scientifique et du Collkge de France, 94130 Nogent-sur-Marne, France and *Laboratoire de Gdn&ique Cellulaire, Institut Pasteur, 75015 Paris, France Received December 9,1983; Accepted February 9, 1984 Abstract The appearance of neurofilaments (NFs) and vimentin (Vim) in the nervous system of the mouse embryo was documented using immunohistochemical techniques. The three NF protein subunits appear early and simultaneously in central and peripheral neurons at 9 to 10 days of gestation. The onset of NF expression is concomitant with axon elongation and correlates extremely well with neurofibrillar differentiation and, in the case of autonomic ganglia, with the expression of adrenergic neurotransmitter properties. In the central and peripheral nervous system, NF expression is preceded by that of Vim, and both types of intermediate filaments coexist within the same cell for a short period of time. Specific markers of neuronal and glial cell types are powerful cases, they have revealed common epitopes shared by the tools for studying the mechanisms generating cellular diversi- various classes of IF (Pruss et al., 1981; Dellagi et al., 1982; fication in the nervous system. In recent years, intermediate Gown and Vogel, 1982 and, in the NF class, by the various NF filaments (IFS), a particular class of cytoskeletal proteins, have subunits (Willard and Simon, 1981; Lee et al., 1982; Goldstein attracted much interest, largely because of their polymorphism; et al., 1983). -
Differential Organization of Desmin and Vimentin in Muscle Is Due to Differences in Their Head Domains Robert B
Differential Organization of Desmin and Vimentin in Muscle Is Due to Differences in Their Head Domains Robert B. Cary and Michael W. Klymkowsky Molecular, Cellular and Developmental Biology, University of Colorado, Boulder, Colorado 80309-0347 Abstract. In most myogenic systems, synthesis of the aggregates. In embryonic epithelial cells, both vimen- intermediate filament (IF) protein vimentin precedes tin and desmin formed extended IF networks. Vimen- the synthesis of the muscle-specific IF protein desmin. tin and desmin differ most dramatically in their NH:- In the dorsal myotome of the Xenopus embryo, how- terminal "head" regions. To determine whether the ever, there is no preexisting vimentin filament system head region was responsible for the differences in the and desmin's initial organization is quite different from behavior of these two proteins, we constructed plas- that seen in vimentin-containing myocytes (Cary and mids encoding chimeric proteins in which the head of Klymkowsky, 1994. Differentiation. In press.). To de- one was attached to the body of the other. In muscle, termine whether the organization of IFs in the Xeno- the vimentin head-desmin body (VDD) polypeptide pus myotome reflects features unique to Xenopus or is formed longitudinal IFs and massive IF bundles like due to specific properties of desmin, we used the in- vimentin. The desmin head-vimentin body (DVV) jection of plasmid DNA to drive the synthesis of polypeptide, on the other hand, formed IF meshworks vimentin or desmin in myotomal cells. At low levels and non-filamentous structures like desmin. In em- of accumulation, exogenous vimentin and desmin both bryonic epithelial cells DVV formed a discrete fila- enter into the endogenous desmin system of the myo- ment network while VDD did not. -
Vimentin, Carcinoembryonic Antigen and Keratin in the Diagnosis of Mesothelioma, Adenocarcinoma and Reactive Pleural Lesions
Eur Respir J 1990, 3, 997-1001 Vimentin, carcinoembryonic antigen and keratin in the diagnosis of mesothelioma, adenocarcinoma and reactive pleural lesions N. AI-Saffar, P .S. Hasleton Vimentin, carcinoembryonic antigen and keratin in the diagnosis of Dept of Pathology, Regional CardiO!horacic Centre, mesothelioma, adenocarcinoma and reactive pleural lesions. N. Al-Saffar, P .S. Wythenshawe Hospital, Manchester, UK. Hasleton. ABSTRACT: An immunohistochemical study of reactive pleural lesions, Correspondence: P.S. Hasleton, Dept of Pathology, Wythensbawe Hospital, Southmoor Road, adenocarcinomas and mesothellomas using carclnoembyronic antigen Wythenshawe, Manchester M23 9LT, UK. (CEA), cytokeratln and vlmentln was carried out. All the specimens were obtained at surgery except for 11 mesotheliomas found at necropsy. Keywords: Adenocarcinoma (lung); carcinoembryonic Vlmentln was positive In 23 or 27 mesotheliomas and negative In all the antigen (CEA); keratin; mesothelioma (pleural); adenocarcinomas and 4 of 17 reactive mesothelial lesions. Conversely, vimentin. CEA was positive In all the adenocarcinomas but negative 1n all mesothe liomas. Immunoreactivity for vlmentln was seen In only 3 of 11 post Received: February 1990; accepted after revision May mortem mesotheliomas. Vlmentln Is a useful adjunct to the tissue diagnosis 2, 1990. of mesothelioma especially when CEA Is negative and cytokeratln positive. Its use appears largely confirmed to well fixed surgically derived tissues. Eur Respir J., 1990, 3, 997- 1001. The diagnosis of malignant pleural mesothelioma is 38 mesothelioma cases were necropsy specimens often difficult. It may be confused histologically with a coming mainly from the Medical Boarding Panel (M.B.P.) reactive pleurisy or adenocarcinoma. Separation from (Respiratory Diseases). Seven were epithelial, three benign lesions is obviously important. -
Myosin II Isoform Switching Mediates Invasiveness After TGF-Β–Induced Epithelial–Mesenchymal Transition
Myosin II isoform switching mediates invasiveness after TGF-β–induced epithelial–mesenchymal transition Jordan R. Beacha,b, George S. Husseyc, Tyler E. Millera, Arindam Chaudhuryd, Purvi Patele, James Monslowa, Qiao Zhenga, Ruth A. Kerif, Ofer Reizesa, Anne R. Bresnicke, Philip H. Howec, and Thomas T. Egelhoffa,1 aDepartment of Cell Biology, Cleveland Clinic, Cleveland, OH 44195; Departments of bPhysiology and Biophysics and fPharmacology, Case Western Reserve University, Cleveland, OH 44106; cHollings Cancer Center, Medical University of South Carolina, Charleston, SC 29425; dDepartment of Molecular Physiology and Biophysics, Baylor College of Medicine, Houston, TX 77030; and eDepartment of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461 Edited by Robert Adelstein, National Institutes of Health, Bethesda, MD, and accepted by the Editorial Board September 27, 2011 (received for review April 22, 2011) Despite functional significance of nonmuscle myosin II in cell gratory modes have been suggested, including amoeboid and migration and invasion, its role in epithelial–mesenchymal transition mesenchymal, and some studies have suggested that cells can (EMT) or TGF-β signaling is unknown. Analysis of normal mammary switch between migration modes depending on the extracellular gland expression revealed that myosin IIC is expressed in luminal environment (9). Recent work indicates that nuclear translocation cells, whereas myosin IIB expression is up-regulated in myoepithelial can be a rate-limiting step during amoeboid 3D migration (10, 11). cells that have more mesenchymal characteristics. Furthermore, TGF- Others studies have shown that contraction of the cell rear is ab- β induction of EMT in nontransformed murine mammary gland ep- solutely necessary for cancer cell invasion (12). -
Tau Inhibits Vesicle and Organelle Transport
Journal of Cell Science 112, 2355-2367 (1999) 2355 Printed in Great Britain © The Company of Biologists Limited 1999 JCS9926 Tau regulates the attachment/detachment but not the speed of motors in microtubule-dependent transport of single vesicles and organelles B. Trinczek*, A. Ebneth‡, E.-M. Mandelkow and E. Mandelkow* Max-Planck Unit for Structural Molecular Biology, Notkestrasse 85, D-22607 Hamburg, Germany *Authors for correspondence (e-mail: [email protected]; [email protected]) ‡Present address: GENION Forschungsgesellschaft mbH, Abteistrasse 57, 20149 Hamburg, Germany Accepted 30 April; published on WWW 24 June 1999 SUMMARY We have performed a real time analysis of fluorescence- even with that of vimentin intermediate filaments. The net tagged vesicle and mitochondria movement in living CHO effect is a directional bias in the minus-end direction of cells transfected with microtubule-associated protein tau or microtubules which leads to the retraction of mitochondria its microtubule-binding domain. Tau does not alter the or vimentin IFs towards the cell center. The data suggest speed of moving vesicles, but it affects the frequencies of that tau can control intracellular trafficking by affecting attachment and detachment to the microtubule tracks. the attachment and detachment cycle of the motors, in Thus, tau decreases the run lengths both for plus-end and particular by reducing the attachment of kinesin to minus-end directed motion to an equal extent. Reversals microtubules, whereas the movement itself is unaffected. from minus-end to plus-end directed movement of single vesicles are strongly reduced by tau, but reversals in the opposite direction (plus to minus) are not. -
UC Berkeley UC Berkeley Electronic Theses and Dissertations
UC Berkeley UC Berkeley Electronic Theses and Dissertations Title Mechanistic insights into the roles of P-TEFb and its novel cofactors in tumorigenesis and HIV transcription Permalink https://escholarship.org/uc/item/54n5v31q Author He, Nanhai Publication Date 2012 Peer reviewed|Thesis/dissertation eScholarship.org Powered by the California Digital Library University of California Mechanistic insights into the roles of P-TEFb and its novel cofactors in tumorigenesis and HIV transcription By Nanhai He A dissertation submitted in partial satisfaction of the requirements for the degree of Doctor of Philosophy in Molecular and Cell Biology in the Graduate Division of the University of California, Berkeley Committee in charge: Professor Qiang Zhou, Chair Professor Mike Botchan Professor Tom Abler Professor Fenyong Liu Spring 2012 1 Abstract Mechanistic insights into the roles of P-TEFb and its novel cofactors in tumorigenesis and HIV transcription by Nanhai He Doctor of Philosophy in Molecular and Cell Biology University of California, Berkeley Professor Qiang Zhou, Chair Ongoing research in the field of transcription has given rise to the unappreciated role of elongation control as a rate limiting step for transcription, and the general transcription elongation factor P-TEFb therefore has taken the central stages. P-TEFb is composed of cyclin T1 and the cyclin-dependent kinase Cdk9. It stimulates transcription elongation by releasing the paused RNA Polymerase II (Pol II) through phosphorylating Pol II at Ser2 and antagonizing the effects of negative elongation factors. P-TEFb is not only essential for the transcription of the vast majority of cellular genes, but also critical for the expression of HIV genome. -
Neurofilaments and Neurofilament Proteins in Health and Disease
Downloaded from http://cshperspectives.cshlp.org/ on October 5, 2021 - Published by Cold Spring Harbor Laboratory Press Neurofilaments and Neurofilament Proteins in Health and Disease Aidong Yuan,1,2 Mala V. Rao,1,2 Veeranna,1,2 and Ralph A. Nixon1,2,3 1Center for Dementia Research, Nathan Kline Institute, Orangeburg, New York 10962 2Department of Psychiatry, New York University School of Medicine, New York, New York 10016 3Cell Biology, New York University School of Medicine, New York, New York 10016 Correspondence: [email protected], [email protected] SUMMARY Neurofilaments (NFs) are unique among tissue-specific classes of intermediate filaments (IFs) in being heteropolymers composed of four subunits (NF-L [neurofilament light]; NF-M [neuro- filament middle]; NF-H [neurofilament heavy]; and a-internexin or peripherin), each having different domain structures and functions. Here, we review how NFs provide structural support for the highly asymmetric geometries of neurons and, especially, for the marked radial expan- sion of myelinated axons crucial for effective nerve conduction velocity. NFs in axons exten- sively cross-bridge and interconnect with other non-IF components of the cytoskeleton, including microtubules, actin filaments, and other fibrous cytoskeletal elements, to establish a regionallyspecialized networkthat undergoes exceptionallyslow local turnoverand serves as a docking platform to organize other organelles and proteins. We also discuss how a small pool of oligomeric and short filamentous precursors in the slow phase of axonal transport maintains this network. A complex pattern of phosphorylation and dephosphorylation events on each subunit modulates filament assembly, turnover, and organization within the axonal cytoskel- eton. Multiple factors, and especially turnover rate, determine the size of the network, which can vary substantially along the axon. -
Myosin Heavy Chain 10 (MYH10) Gene Silencing Reduces Cell
LAB/IN VITRO RESEARCH e-ISSN 1643-3750 © Med Sci Monit, 2018; 24: 9110-9119 DOI: 10.12659/MSM.911523 Received: 2018.06.04 Accepted: 2018.08.06 Myosin Heavy Chain 10 (MYH10) Gene Silencing Published: 2018.12.15 Reduces Cell Migration and Invasion in the Glioma Cell Lines U251, T98G, and SHG44 by Inhibiting the Wnt/b-Catenin Pathway Authors’ Contribution: AB 1 Yang Wang* 1 Department of Neurosurgery, 2nd Ward, Taihe Hospital, Shiyan, Hubei, P.R. China rd Study Design A AB 2 Qi Yang* 2 Department of Orthopedic Surgery, 3 Ward, Taihe Hospital, Shiyan, Hubei, Data Collection B P.R. China Statistical Analysis C CD 3 Yanli Cheng 3 Skin Department, Taihe Hospital, Shiyan, Hubei, P.R. China Data Interpretation D DE 4 Meng Gao 4 Department of Ophthalmology and Otolaryngology, Weifang Maternal and Child Manuscript Preparation E CE 5 Lei Kuang Health Care Hospital, Weifang, Shandong, P.R. China Literature Search F 5 Department of Neurosurgery, 3rd Ward, Taihe Hospital, Shiyan, Hubei, P.R. China Funds Collection G EF 6 Chun Wang 6 Department of Neurosurgery, Suizhou Central Hospital, Suizhou, Hubei, P.R. China * These authors contributed equally to this work Corresponding Author: Chun Wang, e-mail: [email protected] Source of support: Departmental sources Background: The myosin heavy chain 10 or MYH10 gene encodes non-muscle myosin II B (NM IIB), and is involved in tumor cell migration, invasion, extracellular matrix (ECM) production, and epithelial-mesenchymal transition (EMT). This study aimed to investigate the effects of the MYH10 gene on normal human glial cells and glioma cell lines in vitro, by gene silencing, and to determine the signaling pathways involved.