Identification of a molecular recognition feature in the E1A oncoprotein that binds the SUMO conjugase UBC9 and likely interferes with polySUMOylation. (Q44410005)

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scientific article published on 14 June 2010

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English	Identification of a molecular recognition feature in the E1A oncoprotein that binds the SUMO conjugase UBC9 and likely interferes with polySUMOylation.	scientific article published on 14 June 2010

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5 February 2020

Identification of a molecular recognition feature in the E1A oncoprotein that binds the SUMO conjugase UBC9 and likely interferes with polySUMOylation (English)

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5 February 2020

Ahmed F. Yousef

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G J Fonseca

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P Pelka

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J N G Ablack

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C Walsh

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F A Dick

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D P Bazett-Jones

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G S Shaw

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J S Mymryk

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Interaction of the E1A oncoprotein with Yak1p, a novel regulator of yeast pseudohyphal differentiation, and related mammalian kinases

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The conserved Mynd domain of BS69 binds cellular and oncoviral proteins through a common PXLXP motif

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Comparative sequence analysis of the largest E1A proteins of human and simian adenoviruses

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The SUMO isopeptidase Ulp2 prevents accumulation of SUMO chains in yeast

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Structure and Analysis of a Complex between SUMO and Ubc9 Illustrates Features of a Conserved E2-Ubl Interaction

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CtBP, an unconventional transcriptional corepressor in development and oncogenesis

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PML nuclear bodies: dynamic sensors of DNA damage and cellular stress

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Common variants in the UBC9 gene encoding the SUMO-conjugating enzyme are associated with breast tumor grade

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Size, position and dynamic behavior of PML nuclear bodies following cell stress as a paradigm for supramolecular trafficking and assembly

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Epigenetic reprogramming by adenovirus e1a.

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Evolutionary rate in the protein interaction network

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Adenovirus-5 E1A: paradox and paradigm

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Mammalian SUMO E3-ligases PIAS1 and PIAS4 promote responses to DNA double-strand breaks

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Analysis of the human protein interactome and comparison with yeast, worm and fly interaction datasets

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Concepts in sumoylation: a decade on

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Evidence for dynamically organized modularity in the yeast protein-protein interaction network

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mUBC9, a novel adenovirus E1A-interacting protein that complements a yeast cell cycle defect

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Lethality and centrality in protein networks

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Modification of proteins by ubiquitin and ubiquitin-like proteins

1 reference

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Ubc9 sumoylation regulates SUMO target discrimination

1 reference

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Noncovalent interaction between Ubc9 and SUMO promotes SUMO chain formation

1 reference

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Arsenic degrades PML or PML-RARalpha through a SUMO-triggered RNF4/ubiquitin-mediated pathway

1 reference

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31 March 2020

Identification of a substrate recognition site on Ubc9.

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Abrogation of oncogene-associated apoptosis allows transformation of p53-deficient cells

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Specificity and stability in topology of protein networks

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Targeting Ubc9 for cancer therapy

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Overexpression of a dominant-negative mutant Ubc9 is associated with increased sensitivity to anticancer drugs.

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Retinoblastoma protein partners

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The SUMO modification pathway is involved in the BRCA1 response to genotoxic stress.

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Activation of the Slx5-Slx8 ubiquitin ligase by poly-small ubiquitin-like modifier conjugates

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Intrinsic structural disorder in adenovirus E1A: a viral molecular hub linking multiple diverse processes.

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SUMO-targeted ubiquitin ligases in genome stability.

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Molecular mimicry of SUMO promotes DNA repair

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Towards a proteome-scale map of the human protein–protein interaction network

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MAP kinase and cAMP filamentation signaling pathways converge on the unusually large promoter of the yeast FLO11 gene

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Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3

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The small ubiquitin-like modifier-1 (SUMO-1) consensus sequence mediates Ubc9 binding and is essential for SUMO-1 modification

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Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity

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SUMO conjugation and deconjugation

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Identification of a SUMO-binding motif that recognizes SUMO-modified proteins

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Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding motif: a reversal of the bound orientation

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Conserved function of RNF4 family proteins in eukaryotes: targeting a ubiquitin ligase to SUMOylated proteins

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

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The quest for human cancer viruses.

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Ubiquitin-dependent proteolytic control of SUMO conjugates

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The Intrinsic Affinity between E2 and the Cys Domain of E1 in Ubiquitin-like Modifications

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Arsenic trioxide stimulates SUMO-2/3 modification leading to RNF4-dependent proteolytic targeting of PML.

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The yeast Hex3.Slx8 heterodimer is a ubiquitin ligase stimulated by substrate sumoylation

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Coactivator requirements for p53-dependent transcription in the yeast Saccharomyces cerevisiae.

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Ubc9 promotes breast cell invasion and metastasis in a sumoylation-independent manner

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Identifiers

10.1038/ONC.2010.226

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20543865 AND SRC:MED&resulttype=core&format=json

5 February 2020

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20543865 AND SRC:MED&resulttype=core&format=json

5 February 2020

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