File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Ebp1 sumoylation, regulated by TLS/FUS E3 ligase, is required for its anti-proliferative activity

TitleEbp1 sumoylation, regulated by TLS/FUS E3 ligase, is required for its anti-proliferative activity
Authors
KeywordsEbp1
Cell proliferation
TLS/FUS
Sumoylation
Issue Date2010
Citation
Oncogene, 2010, v. 29, n. 7, p. 1017-1030 How to Cite?
AbstractEbp1, an ErbB3 receptor-binding protein, inhibits cell proliferation and acts as a putative tumor suppressor. Ebp1 translocates into the nucleus and functions as a transcription co-repressor for E2F-1. Here, we show that Ebp1 p42 isoform can be sumoylated on both K93 and K298 residues, which mediate its nuclear translocation and are required for its anti-proliferative activity. We find that translocation in liposarcoma (TLS)/FUS, an RNA-binding nuclear protein that is involved in pre-mRNA processing and nucleocytoplasmic shuttling, has Sumo1 E3 ligase activity for Ebp1 p42. Ebp1 directly binds TLS/FUS, which is regulated by genotoxic stress-triggered phosphorylation on Ebp1. Ebp1 sumoylation facilitates its nucleolar distribution and protein stability. Overexpression of TLS enhances Ebp1 sumoylation, whereas depletion of TLS abolishes Ebp1 sumoylation. Moreover, unsumoylated Ebp1 mutants fail to suppress E2F-1-regulated transcription, resulting in loss of its anti-proliferation activity. Hence, TLS-mediated sumoylation is required for Ebp1 transcriptional repressive activity. © 2010 Macmillan Publishers Limited All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/225080
ISSN
2015 Impact Factor: 7.932
2015 SCImago Journal Rankings: 4.047

 

DC FieldValueLanguage
dc.contributor.authorOh, S. M.-
dc.contributor.authorLiu, Z.-
dc.contributor.authorOkada, M.-
dc.contributor.authorJang, S. W.-
dc.contributor.authorLiu, X.-
dc.contributor.authorChan, C. B.-
dc.contributor.authorLuo, H.-
dc.contributor.authorYe, K.-
dc.date.accessioned2016-04-18T11:16:43Z-
dc.date.available2016-04-18T11:16:43Z-
dc.date.issued2010-
dc.identifier.citationOncogene, 2010, v. 29, n. 7, p. 1017-1030-
dc.identifier.issn0950-9232-
dc.identifier.urihttp://hdl.handle.net/10722/225080-
dc.description.abstractEbp1, an ErbB3 receptor-binding protein, inhibits cell proliferation and acts as a putative tumor suppressor. Ebp1 translocates into the nucleus and functions as a transcription co-repressor for E2F-1. Here, we show that Ebp1 p42 isoform can be sumoylated on both K93 and K298 residues, which mediate its nuclear translocation and are required for its anti-proliferative activity. We find that translocation in liposarcoma (TLS)/FUS, an RNA-binding nuclear protein that is involved in pre-mRNA processing and nucleocytoplasmic shuttling, has Sumo1 E3 ligase activity for Ebp1 p42. Ebp1 directly binds TLS/FUS, which is regulated by genotoxic stress-triggered phosphorylation on Ebp1. Ebp1 sumoylation facilitates its nucleolar distribution and protein stability. Overexpression of TLS enhances Ebp1 sumoylation, whereas depletion of TLS abolishes Ebp1 sumoylation. Moreover, unsumoylated Ebp1 mutants fail to suppress E2F-1-regulated transcription, resulting in loss of its anti-proliferation activity. Hence, TLS-mediated sumoylation is required for Ebp1 transcriptional repressive activity. © 2010 Macmillan Publishers Limited All rights reserved.-
dc.languageeng-
dc.relation.ispartofOncogene-
dc.subjectEbp1-
dc.subjectCell proliferation-
dc.subjectTLS/FUS-
dc.subjectSumoylation-
dc.titleEbp1 sumoylation, regulated by TLS/FUS E3 ligase, is required for its anti-proliferative activity-
dc.typeArticle-
dc.description.natureLink_to_subscribed_fulltext-
dc.identifier.doi10.1038/onc.2009.411-
dc.identifier.pmid19946338-
dc.identifier.scopuseid_2-s2.0-77149134314-
dc.identifier.volume29-
dc.identifier.issue7-
dc.identifier.spage1017-
dc.identifier.epage1030-
dc.identifier.eissn1476-5594-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats