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Article: Identification and characterization of EBP, a novel EEN binding protein that inhibits Ras signaling and is recruited into the nucleus by the MLL-EEN fusion protein
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TitleIdentification and characterization of EBP, a novel EEN binding protein that inhibits Ras signaling and is recruited into the nucleus by the MLL-EEN fusion protein
 
AuthorsYam, JWP
Jin, DY
So, CW
Chan, LC1
 
KeywordsCarrier Proteins - chemistry - genetics - metabolism
DNA-Binding Proteins - genetics - metabolism
Nucleocytoplasmic Transport Proteins
Proto-Oncogenes
Steroid Isomerases
 
Issue Date2004
 
PublisherAmerican Society of Hematology. The Journal's web site is located at http://bloodjournal.hematologylibrary.org/
 
CitationBlood, 2004, v. 103 n. 4, p. 1445-1453 [How to Cite?]
DOI: http://dx.doi.org/10.1182/blood-2003-07-2452
 
AbstractThe chimeric MLL-EEN fusion protein is created as a result of chromosomal translocation t(11;19)(q23;p13). EEN, an Src homology 3 (SH3) domain-containing protein in the endophilin family, has been implicated in endocytosis, although little is known about its role in leukemogenesis mediated by the MLL-EEN fusion protein. In this study, we have identified and characterized EBP, a novel EEN binding protein that interacts with the SH3 domain of EEN through a proline-rich motif PPERP. EBP is a ubiquitous protein that is normally expressed in the cytoplasm but is recruited to the nucleus by MLL-EEN with a punctate localization pattern characteristic of the MLL chimeric proteins. EBP interacts simultaneously with EEN and Sos, a guanine-nucleotide exchange factor for Ras. Coexpressoin of EBP with EEN leads to suppression of Ras-induced cellular transformation and Ras-mediated activation of Elk-1. Taken together, our findings suggest a new mechanism for MLL-EEN-mediated leukemogenesis in which MLL-EEN interferes with the Ras-suppressing activities of EBP through direct interaction. © 2004 by The American Society of Hematology.
 
ISSN0006-4971
2013 Impact Factor: 9.775
 
DOIhttp://dx.doi.org/10.1182/blood-2003-07-2452
 
ISI Accession Number IDWOS:000188828200046
 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorYam, JWP
 
dc.contributor.authorJin, DY
 
dc.contributor.authorSo, CW
 
dc.contributor.authorChan, LC
 
dc.date.accessioned2008-05-22T04:15:24Z
 
dc.date.available2008-05-22T04:15:24Z
 
dc.date.issued2004
 
dc.description.abstractThe chimeric MLL-EEN fusion protein is created as a result of chromosomal translocation t(11;19)(q23;p13). EEN, an Src homology 3 (SH3) domain-containing protein in the endophilin family, has been implicated in endocytosis, although little is known about its role in leukemogenesis mediated by the MLL-EEN fusion protein. In this study, we have identified and characterized EBP, a novel EEN binding protein that interacts with the SH3 domain of EEN through a proline-rich motif PPERP. EBP is a ubiquitous protein that is normally expressed in the cytoplasm but is recruited to the nucleus by MLL-EEN with a punctate localization pattern characteristic of the MLL chimeric proteins. EBP interacts simultaneously with EEN and Sos, a guanine-nucleotide exchange factor for Ras. Coexpressoin of EBP with EEN leads to suppression of Ras-induced cellular transformation and Ras-mediated activation of Elk-1. Taken together, our findings suggest a new mechanism for MLL-EEN-mediated leukemogenesis in which MLL-EEN interferes with the Ras-suppressing activities of EBP through direct interaction. © 2004 by The American Society of Hematology.
 
dc.description.naturepostprint
 
dc.format.extent146861 bytes
 
dc.format.extent3021 bytes
 
dc.format.mimetypeapplication/pdf
 
dc.format.mimetypetext/plain
 
dc.identifier.citationBlood, 2004, v. 103 n. 4, p. 1445-1453 [How to Cite?]
DOI: http://dx.doi.org/10.1182/blood-2003-07-2452
 
dc.identifier.doihttp://dx.doi.org/10.1182/blood-2003-07-2452
 
dc.identifier.epage1453
 
dc.identifier.hkuros86076
 
dc.identifier.isiWOS:000188828200046
 
dc.identifier.issn0006-4971
2013 Impact Factor: 9.775
 
dc.identifier.issue4
 
dc.identifier.openurl
 
dc.identifier.pmid14551139
 
dc.identifier.scopuseid_2-s2.0-0842307321
 
dc.identifier.spage1445
 
dc.identifier.urihttp://hdl.handle.net/10722/48499
 
dc.identifier.volume103
 
dc.languageeng
 
dc.publisherAmerican Society of Hematology. The Journal's web site is located at http://bloodjournal.hematologylibrary.org/
 
dc.publisher.placeUnited States
 
dc.relation.ispartofBlood
 
dc.relation.referencesReferences in Scopus
 
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License
 
dc.subjectCarrier Proteins - chemistry - genetics - metabolism
 
dc.subjectDNA-Binding Proteins - genetics - metabolism
 
dc.subjectNucleocytoplasmic Transport Proteins
 
dc.subjectProto-Oncogenes
 
dc.subjectSteroid Isomerases
 
dc.titleIdentification and characterization of EBP, a novel EEN binding protein that inhibits Ras signaling and is recruited into the nucleus by the MLL-EEN fusion protein
 
dc.typeArticle
 
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Author Affiliations
  1. Queen Mary Hospital Hong Kong