Literature DB >> 20610547

Orphan nuclear bodies.

Maria Carmo-Fonseca1, Maria T Berciano, Miguel Lafarga.   

Abstract

Orphan nuclear bodies are defined as nonchromatin nuclear compartments that have been less well studied compared with other well-characterized structures in the nucleus. Nuclear bodies have traditionally been thought of as uniform distinct entities depending on the protein "markers" they contain. However, it is becoming increasingly apparent that nuclear bodies enriched in different sets of transcriptional regulators share a link to the ubiquitin-proteasome and SUMO-conjugation pathways. An emerging concept is that some orphan nuclear bodies might act as sites of protein modification by SUMO and/or proteasomal degradation of ubiquitin-tagged proteins. By defining a specialized environment for protein modification and degradation, orphan nuclear bodies may increase the capacity of cells to survive under varying environmental conditions.

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Year:  2010        PMID: 20610547      PMCID: PMC2926751          DOI: 10.1101/cshperspect.a000703

Source DB:  PubMed          Journal:  Cold Spring Harb Perspect Biol        ISSN: 1943-0264            Impact factor:   10.005


  45 in total

1.  The CTCF insulator protein is posttranslationally modified by SUMO.

Authors:  Melissa J MacPherson; Linda G Beatty; Wenjing Zhou; Minjie Du; Paul D Sadowski
Journal:  Mol Cell Biol       Date:  2008-11-24       Impact factor: 4.272

2.  KRAB zinc-finger proteins localise to novel KAP1-containing foci that are adjacent to PML nuclear bodies.

Authors:  Stephanie Briers; Catherine Crawford; Wendy A Bickmore; Heidi G Sutherland
Journal:  J Cell Sci       Date:  2009-03-03       Impact factor: 5.285

Review 3.  Molecular mechanisms of proteasome assembly.

Authors:  Shigeo Murata; Hideki Yashiroda; Keiji Tanaka
Journal:  Nat Rev Mol Cell Biol       Date:  2009-02       Impact factor: 94.444

Review 4.  Ubiquitin, the proteasome and protein degradation in neuronal function and dysfunction.

Authors:  Hwan-Ching Tai; Erin M Schuman
Journal:  Nat Rev Neurosci       Date:  2008-11       Impact factor: 34.870

Review 5.  Diversity of degradation signals in the ubiquitin-proteasome system.

Authors:  Tommer Ravid; Mark Hochstrasser
Journal:  Nat Rev Mol Cell Biol       Date:  2008-09       Impact factor: 94.444

6.  RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation.

Authors:  Michael H Tatham; Marie-Claude Geoffroy; Linnan Shen; Anna Plechanovova; Neil Hattersley; Ellis G Jaffray; Jorma J Palvimo; Ronald T Hay
Journal:  Nat Cell Biol       Date:  2008-04-13       Impact factor: 28.824

7.  Specific interaction between Sam68 and neuronal mRNAs: implication for the activity-dependent biosynthesis of elongation factor eEF1A.

Authors:  Julien Grange; Agnès Belly; Stéphane Dupas; Alain Trembleau; Rémy Sadoul; Yves Goldberg
Journal:  J Neurosci Res       Date:  2009-01       Impact factor: 4.164

8.  LPS-induced down-regulation of NO-sensitive guanylyl cyclase in astrocytes occurs by proteasomal degradation in clastosomes.

Authors:  María Antonia Baltrons; Paula Pifarré; María Teresa Berciano; Miguel Lafarga; Agustina García
Journal:  Mol Cell Neurosci       Date:  2007-11-17       Impact factor: 4.314

9.  Role of promyelocytic leukemia (PML) sumolation in nuclear body formation, 11S proteasome recruitment, and As2O3-induced PML or PML/retinoic acid receptor alpha degradation.

Authors:  V Lallemand-Breitenbach; J Zhu; F Puvion; M Koken; N Honoré; A Doubeikovsky; E Duprez; P P Pandolfi; E Puvion; P Freemont; H de Thé
Journal:  J Exp Med       Date:  2001-06-18       Impact factor: 14.307

10.  Sam68 regulates translation of target mRNAs in male germ cells, necessary for mouse spermatogenesis.

Authors:  Maria Paola Paronetto; Valeria Messina; Enrica Bianchi; Marco Barchi; Gillian Vogel; Costanzo Moretti; Fioretta Palombi; Mario Stefanini; Raffaele Geremia; Stéphane Richard; Claudio Sette
Journal:  J Cell Biol       Date:  2009-04-20       Impact factor: 10.539

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  9 in total

1.  Fine structure of the "PcG body" in human U-2 OS cells established by correlative light-electron microscopy.

Authors:  Jana Smigová; Pavel Juda; Dušan Cmarko; Ivan Raška
Journal:  Nucleus       Date:  2011 May-Jun       Impact factor: 4.197

Review 2.  Specific genomic cues regulate Cajal body assembly.

Authors:  Iain A Sawyer; Gordon L Hager; Miroslav Dundr
Journal:  RNA Biol       Date:  2016-10-07       Impact factor: 4.652

Review 3.  Expanding the roles of chromatin insulators in nuclear architecture, chromatin organization and genome function.

Authors:  Todd Schoborg; Mariano Labrador
Journal:  Cell Mol Life Sci       Date:  2014-07-11       Impact factor: 9.261

4.  Spectral imaging to visualize higher-order genomic organization.

Authors:  Iain A Sawyer; Sergei P Shevtsov; Miroslav Dundr
Journal:  Nucleus       Date:  2016-05-11       Impact factor: 4.197

Review 5.  A Crowdsourced nucleus: understanding nuclear organization in terms of dynamically networked protein function.

Authors:  Ashley M Wood; Arturo G Garza-Gongora; Steven T Kosak
Journal:  Biochim Biophys Acta       Date:  2014-01-09

Review 6.  ArcRNAs and the formation of nuclear bodies.

Authors:  Shinichi Nakagawa; Tomohiro Yamazaki; Taro Mannen; Tetsuro Hirose
Journal:  Mamm Genome       Date:  2021-06-03       Impact factor: 2.957

7.  The role of nuclear bodies in gene expression and disease.

Authors:  Marie Morimoto; Cornelius F Boerkoel
Journal:  Biology (Basel)       Date:  2013-07-09

8.  Stress induced nuclear granules form in response to accumulation of misfolded proteins in Caenorhabditis elegans.

Authors:  Katherine M Sampuda; Mason Riley; Lynn Boyd
Journal:  BMC Cell Biol       Date:  2017-04-19       Impact factor: 4.241

9.  Accumulation of poly(A) RNA in nuclear granules enriched in Sam68 in motor neurons from the SMNΔ7 mouse model of SMA.

Authors:  J Oriol Narcís; Olga Tapia; Olga Tarabal; Lídia Piedrafita; Jordi Calderó; Maria T Berciano; Miguel Lafarga
Journal:  Sci Rep       Date:  2018-06-25       Impact factor: 4.379

  9 in total

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