Literature DB >> 12181345

Clastosome: a subtype of nuclear body enriched in 19S and 20S proteasomes, ubiquitin, and protein substrates of proteasome.

Miguel Lafarga1, Maria Teresa Berciano, Emma Pena, Isabel Mayo, Jose G Castaño, Dirk Bohmann, João Pedro Rodrigues, João Paulo Tavanez, Maria Carmo-Fonseca.   

Abstract

Nuclear bodies represent a heterogeneous class of nuclear structures. Herein, we describe that a subset of nuclear bodies is highly enriched in components of the ubiquitin-proteasome pathway of proteolysis. We coined the term clastosome (from the Greek klastos, broken and soma, body) to refer to this type of nuclear body. Clastosomes contain a high concentration of 1) ubiquitin conjugates, 2) the proteolytically active 20S core and the 19S regulatory complexes of the 26S proteasome, and 3) protein substrates of the proteasome. Although detected in a variety of cell types, clastosomes are scarce under normal conditions; however, they become more abundant when proteasomal activity is stimulated. In contrast, clastosomes disappear when cells are treated with proteasome inhibitors. Protein substrates of the proteasome that are found concentrated in clastosomes include the short-lived transcription factors c-Fos and c-Jun, adenovirus E1A proteins, and the PML protein. We propose that clastosomes are sites where proteolysis of a variety of protein substrates is taking place.

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Year:  2002        PMID: 12181345      PMCID: PMC117941          DOI: 10.1091/mbc.e02-03-0122

Source DB:  PubMed          Journal:  Mol Biol Cell        ISSN: 1059-1524            Impact factor:   4.138


  67 in total

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Journal:  Brain Res       Date:  1996-05-06       Impact factor: 3.252

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Authors:  T K Kim; T Maniatis
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Authors:  R Bravo; J Burckhardt; T Curran; R Müller
Journal:  EMBO J       Date:  1986-04       Impact factor: 11.598

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  56 in total

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Authors:  Valérie Lallemand-Breitenbach; Hugues de Thé
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5.  N4BP1 is a newly identified nucleolar protein that undergoes SUMO-regulated polyubiquitylation and proteasomal turnover at promyelocytic leukemia nuclear bodies.

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Review 6.  Orphan nuclear bodies.

Authors:  Maria Carmo-Fonseca; Maria T Berciano; Miguel Lafarga
Journal:  Cold Spring Harb Perspect Biol       Date:  2010-07-07       Impact factor: 10.005

7.  Reorganization of Cajal bodies and nucleolar targeting of coilin in motor neurons of type I spinal muscular atrophy.

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8.  Dynamic Behavior of the RNA Polymerase II and the Ubiquitin Proteasome System During the Neuronal DNA Damage Response to Ionizing Radiation.

Authors:  Iñigo Casafont; Ana Palanca; Vanesa Lafarga; Jorge Mata-Garrido; Maria T Berciano; Miguel Lafarga
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9.  Nucleocytoplasmic shuttling of p62/SQSTM1 and its role in recruitment of nuclear polyubiquitinated proteins to promyelocytic leukemia bodies.

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Journal:  J Biol Chem       Date:  2009-12-15       Impact factor: 5.157

10.  Nontelomeric TRF2-REST interaction modulates neuronal gene silencing and fate of tumor and stem cells.

Authors:  Peisu Zhang; Michael J Pazin; Catherine M Schwartz; Kevin G Becker; Robert P Wersto; Caroline M Dilley; Mark P Mattson
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