Literature DB >> 11704852

SUMO: of branched proteins and nuclear bodies.

J S Seeler1, A Dejean.   

Abstract

SUMO belongs to a growing number of ubiquitin-like proteins that covalently modify their target proteins. Although some evidence supports a role of SUMO modification in regulating protein stability, most studied examples support a model by which SUMO alters the interaction properties of its targets, often affecting their subcellular localization behavior. Examination of the PML nuclear bodies, whose principal components are SUMO-modified, has revealed this modification to be essential for their structural and functional integrity. This and other examples thus support the view that SUMO regulates the stability not of individual proteins, but rather that of entire multiprotein complexes.

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Year:  2001        PMID: 11704852     DOI: 10.1038/sj.onc.1204758

Source DB:  PubMed          Journal:  Oncogene        ISSN: 0950-9232            Impact factor:   9.867


  49 in total

Review 1.  Modification with SUMO. A role in transcriptional regulation.

Authors:  Alexis Verger; José Perdomo; Merlin Crossley
Journal:  EMBO Rep       Date:  2003-02       Impact factor: 8.807

Review 2.  Role of ICP0 in the strategy of conquest of the host cell by herpes simplex virus 1.

Authors:  Ryan Hagglund; Bernard Roizman
Journal:  J Virol       Date:  2004-03       Impact factor: 5.103

3.  SIRT1 stabilizes PML promoting its sumoylation.

Authors:  M Campagna; D Herranz; M A Garcia; L Marcos-Villar; J González-Santamaría; P Gallego; S Gutierrez; M Collado; M Serrano; M Esteban; C Rivas
Journal:  Cell Death Differ       Date:  2010-06-25       Impact factor: 15.828

Review 4.  The role of post-translational modifications in fine-tuning BLM helicase function during DNA repair.

Authors:  Stefanie Böhm; Kara Anne Bernstein
Journal:  DNA Repair (Amst)       Date:  2014-08-24

5.  A universal strategy for proteomic studies of SUMO and other ubiquitin-like modifiers.

Authors:  Germán Rosas-Acosta; William K Russell; Adeline Deyrieux; David H Russell; Van G Wilson
Journal:  Mol Cell Proteomics       Date:  2004-11-30       Impact factor: 5.911

6.  Ikaros SUMOylation: switching out of repression.

Authors:  Pablo Gómez-del Arco; Joseph Koipally; Katia Georgopoulos
Journal:  Mol Cell Biol       Date:  2005-04       Impact factor: 4.272

7.  Down-regulation of c-Fos/c-Jun AP-1 dimer activity by sumoylation.

Authors:  Guillaume Bossis; Cécile E Malnou; Rosa Farras; Elisabetta Andermarcher; Robert Hipskind; Manuel Rodriguez; Darja Schmidt; Stefan Muller; Isabelle Jariel-Encontre; Marc Piechaczyk
Journal:  Mol Cell Biol       Date:  2005-08       Impact factor: 4.272

8.  G2E3 is a nucleo-cytoplasmic shuttling protein with DNA damage responsive localization.

Authors:  William S Brooks; Sami Banerjee; David F Crawford
Journal:  Exp Cell Res       Date:  2006-12-14       Impact factor: 3.905

9.  Effect of SUMO-SIM Interaction on the ICP0-Mediated Degradation of PML Isoform II and Its Associated Proteins in Herpes Simplex Virus 1 Infection.

Authors:  Behdokht Jan Fada; Elie Kaadi; Subodh Kumar Samrat; Yi Zheng; Haidong Gu
Journal:  J Virol       Date:  2020-06-01       Impact factor: 5.103

10.  A novel plant cysteine protease has a dual function as a regulator of 1-aminocyclopropane-1-carboxylic Acid synthase gene expression.

Authors:  Noa Matarasso; Silvia Schuster; Adi Avni
Journal:  Plant Cell       Date:  2005-03-04       Impact factor: 11.277

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