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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

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
Authors
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/
Citation
Blood, 2004, v. 103 n. 4, p. 1445-1453 How to Cite?
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.
Persistent Identifierhttp://hdl.handle.net/10722/48499
ISSN
2014 Impact Factor: 10.452
2014 SCImago Journal Rankings: 5.246
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorYam, JWPen_HK
dc.contributor.authorJin, DYen_HK
dc.contributor.authorSo, CWen_HK
dc.contributor.authorChan, LCen_HK
dc.date.accessioned2008-05-22T04:15:24Z-
dc.date.available2008-05-22T04:15:24Z-
dc.date.issued2004en_HK
dc.identifier.citationBlood, 2004, v. 103 n. 4, p. 1445-1453en_HK
dc.identifier.issn0006-4971en_HK
dc.identifier.urihttp://hdl.handle.net/10722/48499-
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.en_HK
dc.format.extent146861 bytes-
dc.format.extent3021 bytes-
dc.format.mimetypeapplication/pdf-
dc.format.mimetypetext/plain-
dc.languageengen_HK
dc.publisherAmerican Society of Hematology. The Journal's web site is located at http://bloodjournal.hematologylibrary.org/en_HK
dc.relation.ispartofBlooden_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.subjectCarrier Proteins - chemistry - genetics - metabolismen_HK
dc.subjectDNA-Binding Proteins - genetics - metabolismen_HK
dc.subjectNucleocytoplasmic Transport Proteinsen_HK
dc.subjectProto-Oncogenesen_HK
dc.subjectSteroid Isomerasesen_HK
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 proteinen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0006-4971&volume=103&issue=4&spage=1445&epage=1453&date=2004&atitle=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+proteinen_HK
dc.identifier.emailYam, JWP:judyyam@pathology.hku.hken_HK
dc.identifier.emailJin, DY:dyjin@hkucc.hku.hken_HK
dc.identifier.emailChan, LC:chanlc@hkucc.hku.hken_HK
dc.identifier.authorityYam, JWP=rp00468en_HK
dc.identifier.authorityJin, DY=rp00452en_HK
dc.identifier.authorityChan, LC=rp00373en_HK
dc.description.naturepostprinten_HK
dc.identifier.doi10.1182/blood-2003-07-2452en_HK
dc.identifier.pmid14551139en_HK
dc.identifier.scopuseid_2-s2.0-0842307321en_HK
dc.identifier.hkuros86076-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0842307321&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume103en_HK
dc.identifier.issue4en_HK
dc.identifier.spage1445en_HK
dc.identifier.epage1453en_HK
dc.identifier.isiWOS:000188828200046-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridYam, JWP=6603711123en_HK
dc.identifier.scopusauthoridJin, DY=7201973614en_HK
dc.identifier.scopusauthoridSo, CW=7102919928en_HK
dc.identifier.scopusauthoridChan, LC=7403540707en_HK

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