Literature DB >> 21892772

Emerging roles of the SUMO pathway in development.

Hilda Lomelí1, Martha Vázquez.   

Abstract

Sumoylation is a reversible post-translational modification that targets a variety of proteins mainly within the nucleus, but also in the plasma membrane and cytoplasm of the cell. It controls diverse cellular mechanisms such as subcellular localization, protein-protein interactions, or transcription factor activity. In recent years, the use of several developmental model systems has unraveled many critical functions for the sumoylation system in the early life of diverse species. In particular, detailed analyses of mutant organisms in both the components of the SUMO pathway and their targets have established the importance of the SUMO system in early developmental processes, such as cell division, cell lineage commitment, specification, and/or differentiation. In addition, an increasing number of developmental proteins, including transcription factors and epigenetic regulators, have been identified as sumoylation substrates. Sumoylation acts on these targets through various mechanisms. For example, this modification has been involved in converting a transcription factor from an activator to a repressor or in regulating the localization and/or stability of numerous transcription factors. This review will summarize current information on the function of sumoylation in embryonic development in different species from yeast to mammals.

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Year:  2011        PMID: 21892772     DOI: 10.1007/s00018-011-0792-5

Source DB:  PubMed          Journal:  Cell Mol Life Sci        ISSN: 1420-682X            Impact factor:   9.261


  142 in total

1.  Global analysis of protein sumoylation in Saccharomyces cerevisiae.

Authors:  James A Wohlschlegel; Erica S Johnson; Steven I Reed; John R Yates
Journal:  J Biol Chem       Date:  2004-08-23       Impact factor: 5.157

2.  SoxE factors function equivalently during neural crest and inner ear development and their activity is regulated by SUMOylation.

Authors:  Kimberly M Taylor; Carole Labonne
Journal:  Dev Cell       Date:  2005-11       Impact factor: 12.270

Review 3.  Wrestling with SUMO in a new arena.

Authors:  Van G Wilson; Germán Rosas-Acosta
Journal:  Sci STKE       Date:  2005-06-28

4.  Melanotic mutants in Drosophila: pathways and phenotypes.

Authors:  Svetlana Minakhina; Ruth Steward
Journal:  Genetics       Date:  2006-07-02       Impact factor: 4.562

Review 5.  Transcriptional control of erythropoiesis: emerging mechanisms and principles.

Authors:  S-I Kim; E H Bresnick
Journal:  Oncogene       Date:  2007-10-15       Impact factor: 9.867

6.  Molecular cloning and characterization of human AOS1 and UBA2, components of the sentrin-activating enzyme complex.

Authors:  L Gong; B Li; S Millas; E T Yeh
Journal:  FEBS Lett       Date:  1999-04-01       Impact factor: 4.124

7.  Molecular characterization of embryonic gonads by gene expression profiling in Drosophila melanogaster.

Authors:  Shuji Shigenobu; Yu Kitadate; Chiyo Noda; Satoru Kobayashi
Journal:  Proc Natl Acad Sci U S A       Date:  2006-09-01       Impact factor: 11.205

8.  The small ubiquitin-like modifier (SUMO) is required for gonadal and uterine-vulval morphogenesis in Caenorhabditis elegans.

Authors:  Limor Broday; Irina Kolotuev; Christine Didier; Anindita Bhoumik; Bhagwati P Gupta; Paul W Sternberg; Benjamin Podbilewicz; Ze'ev Ronai
Journal:  Genes Dev       Date:  2004-10-01       Impact factor: 11.361

9.  A proteomic strategy for gaining insights into protein sumoylation in yeast.

Authors:  Carilee Denison; Adam D Rudner; Scott A Gerber; Corey E Bakalarski; Danesh Moazed; Steven P Gygi
Journal:  Mol Cell Proteomics       Date:  2004-11-12       Impact factor: 5.911

10.  Yeast axial-element protein, Red1, binds SUMO chains to promote meiotic interhomologue recombination and chromosome synapsis.

Authors:  Feng-Ming Lin; Yi-Ju Lai; Hui-Ju Shen; Yun-Hsin Cheng; Ting-Fang Wang
Journal:  EMBO J       Date:  2009-12-03       Impact factor: 11.598

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  36 in total

1.  RpL22e, but not RpL22e-like-PA, is SUMOylated and localizes to the nucleoplasm of Drosophila meiotic spermatocytes.

Authors:  Michael G Kearse; Jill A Ireland; Smrithi M Prem; Alex S Chen; Vassie C Ware
Journal:  Nucleus       Date:  2013-06-06       Impact factor: 4.197

2.  SUMOylation is essential for sex-specific assembly and function of the Caenorhabditis elegans dosage compensation complex on X chromosomes.

Authors:  Rebecca R Pferdehirt; Barbara J Meyer
Journal:  Proc Natl Acad Sci U S A       Date:  2013-09-16       Impact factor: 11.205

3.  Inflammatory factor-specific sumoylation regulates NF-κB signalling in glomerular cells from diabetic rats.

Authors:  Sijiao Chen; Tao Yang; Furong Liu; Hongyan Li; Yinghua Guo; Hongyan Yang; Jinchun Xu; Jindan Song; Zhiming Zhu; Daoyan Liu
Journal:  Inflamm Res       Date:  2013-10-31       Impact factor: 4.575

4.  In vivo analysis of a fluorescent SUMO fusion in transgenic Drosophila.

Authors:  Marion Bocksberger; François Karch; Jean-Michel Gibert
Journal:  Fly (Austin)       Date:  2014       Impact factor: 2.160

Review 5.  SUMO, a heavyweight player in plant abiotic stress responses.

Authors:  Pedro Humberto Castro; Rui Manuel Tavares; Eduardo R Bejarano; Herlânder Azevedo
Journal:  Cell Mol Life Sci       Date:  2012-08-19       Impact factor: 9.261

6.  Multiple crosstalks between mRNA biogenesis and SUMO.

Authors:  Jérôme O Rouvière; Marie-Claude Geoffroy; Benoit Palancade
Journal:  Chromosoma       Date:  2013-04-14       Impact factor: 4.316

Review 7.  Control of Meiotic Crossovers: From Double-Strand Break Formation to Designation.

Authors:  Stephen Gray; Paula E Cohen
Journal:  Annu Rev Genet       Date:  2016-09-14       Impact factor: 16.830

Review 8.  Caenorhabditis elegans Dosage Compensation: Insights into Condensin-Mediated Gene Regulation.

Authors:  Sarah Elizabeth Albritton; Sevinç Ercan
Journal:  Trends Genet       Date:  2017-10-13       Impact factor: 11.639

9.  SUMOylation is developmentally regulated and required for cell pairing during conjugation in Tetrahymena thermophila.

Authors:  Amjad M Nasir; Qianyi Yang; Douglas L Chalker; James D Forney
Journal:  Eukaryot Cell       Date:  2014-12-19

10.  Senp1 is essential for desumoylating Sumo1-modified proteins but dispensable for Sumo2 and Sumo3 deconjugation in the mouse embryo.

Authors:  Prashant Sharma; Satoru Yamada; Margaret Lualdi; Mary Dasso; Michael R Kuehn
Journal:  Cell Rep       Date:  2013-05-16       Impact factor: 9.423

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