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Article: Stabilization of PML nuclear localization by conjugation and oligomerization of SUMO-3

TitleStabilization of PML nuclear localization by conjugation and oligomerization of SUMO-3
Authors
KeywordsAcute promyelocytic leukemia
Nuclear body
Promyelocytic leukemia protein
Issue Date2005
PublisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/onc
Citation
Oncogene, 2005, v. 24 n. 35, p. 5401-5413 How to Cite?
AbstractThe PML gene of acute promyelocytic leukemia (APL) encodes a cell-growth and tumor suppressor. PML localizes to discrete nuclear bodies (NBs) that are disrupted in APL cells, resulting from a reciprocal chromosome translocation t (15;17). Here we show that the nuclear localization of PML is also regulated by SUMO-3, one of the three recently identified SUMO isoforms in human cells. SUMO-3 bears similar subcellular distribution to those of SUMO-1 and -2 in the interphase nuclear body, which is colocalized with PML protein. However, both SUMO-2 and -3 are also localized to nucleoli, a region lacking SUMO-1. Immunoprecipitated PML protein bears SUMO-3 moiety in a covalently modified form, supporting the notion that PML is conjugated by SUMO-3. To determine the functional relevance of SUMO-3 conjugation on PML molecular dynamics, we suppressed SUMO-3 protein expression using a siRNA-mediated approach. Depletion of SUMO-3 markedly reduced the number of PML-containing NBa and their integrity, which is rescued by exogenous expression of SUMO-3 but not SUMO-1 or SUMO-2. The specific requirement of SUMO-3 for PML nuclear localization is validated by expression of SUMO-3 conjugation defective mutant. Moreover, we demonstrate that oligomerization of SUMO-3 is required for PML retention in the nucleus. Taken together, our studies provide first line of evidence showing that SUMO-3 is essential for PML localization and offer novel insight into the pathobiochemistry of APL. © 2005 Nature Publishing Group All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/136783
ISSN
2023 Impact Factor: 6.9
2023 SCImago Journal Rankings: 2.334
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorFu, Cen_HK
dc.contributor.authorAhmed, Ken_HK
dc.contributor.authorDing, Hen_HK
dc.contributor.authorDing, Xen_HK
dc.contributor.authorLan, Jen_HK
dc.contributor.authorYang, Zen_HK
dc.contributor.authorMiao, Yen_HK
dc.contributor.authorZhu, Yen_HK
dc.contributor.authorShi, Yen_HK
dc.contributor.authorZhu, Jen_HK
dc.contributor.authorHuang, Hen_HK
dc.contributor.authorYao, Xen_HK
dc.date.accessioned2011-07-29T02:12:10Z-
dc.date.available2011-07-29T02:12:10Z-
dc.date.issued2005en_HK
dc.identifier.citationOncogene, 2005, v. 24 n. 35, p. 5401-5413en_HK
dc.identifier.issn0950-9232en_HK
dc.identifier.urihttp://hdl.handle.net/10722/136783-
dc.description.abstractThe PML gene of acute promyelocytic leukemia (APL) encodes a cell-growth and tumor suppressor. PML localizes to discrete nuclear bodies (NBs) that are disrupted in APL cells, resulting from a reciprocal chromosome translocation t (15;17). Here we show that the nuclear localization of PML is also regulated by SUMO-3, one of the three recently identified SUMO isoforms in human cells. SUMO-3 bears similar subcellular distribution to those of SUMO-1 and -2 in the interphase nuclear body, which is colocalized with PML protein. However, both SUMO-2 and -3 are also localized to nucleoli, a region lacking SUMO-1. Immunoprecipitated PML protein bears SUMO-3 moiety in a covalently modified form, supporting the notion that PML is conjugated by SUMO-3. To determine the functional relevance of SUMO-3 conjugation on PML molecular dynamics, we suppressed SUMO-3 protein expression using a siRNA-mediated approach. Depletion of SUMO-3 markedly reduced the number of PML-containing NBa and their integrity, which is rescued by exogenous expression of SUMO-3 but not SUMO-1 or SUMO-2. The specific requirement of SUMO-3 for PML nuclear localization is validated by expression of SUMO-3 conjugation defective mutant. Moreover, we demonstrate that oligomerization of SUMO-3 is required for PML retention in the nucleus. Taken together, our studies provide first line of evidence showing that SUMO-3 is essential for PML localization and offer novel insight into the pathobiochemistry of APL. © 2005 Nature Publishing Group All rights reserved.en_HK
dc.languageengen_US
dc.publisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/oncen_HK
dc.relation.ispartofOncogeneen_HK
dc.subjectAcute promyelocytic leukemia-
dc.subjectNuclear body-
dc.subjectPromyelocytic leukemia protein-
dc.subject.meshBlotting, Westernen_HK
dc.subject.meshCell Nucleus - metabolismen_HK
dc.subject.meshFluorescent Antibody Techniqueen_HK
dc.subject.meshHeLa Cellsen_HK
dc.subject.meshHumansen_HK
dc.subject.meshImmunoprecipitationen_HK
dc.subject.meshIntranuclear Inclusion Bodies - chemistry - metabolismen_HK
dc.subject.meshLeukemia, Promyelocytic, Acute - metabolismen_HK
dc.subject.meshMicroscopy, Confocalen_HK
dc.subject.meshMutagenesis, Site-Directeden_HK
dc.subject.meshNeoplasm Proteins - chemistry - metabolismen_HK
dc.subject.meshNuclear Proteins - chemistry - metabolismen_HK
dc.subject.meshProtein Isoforms - chemistry - metabolismen_HK
dc.subject.meshRNA, Small Interferingen_HK
dc.subject.meshSUMO-1 Protein - chemistry - metabolismen_HK
dc.subject.meshSmall Ubiquitin-Related Modifier Proteins - chemistry - metabolismen_HK
dc.subject.meshTranscription Factors - chemistry - metabolismen_HK
dc.subject.meshTumor Suppressor Proteins - chemistry - metabolismen_HK
dc.titleStabilization of PML nuclear localization by conjugation and oligomerization of SUMO-3en_HK
dc.typeArticleen_HK
dc.identifier.emailFu, C:chuanhai@hku.hken_HK
dc.identifier.authorityFu, C=rp01515en_HK
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1038/sj.onc.1208714en_HK
dc.identifier.pmid15940266en_HK
dc.identifier.scopuseid_2-s2.0-24644522876en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-24644522876&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume24en_HK
dc.identifier.issue35en_HK
dc.identifier.spage5401en_HK
dc.identifier.epage5413en_HK
dc.identifier.eissn1476-5594-
dc.identifier.isiWOS:000231222300001-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridFu, C=8583808400en_HK
dc.identifier.scopusauthoridAhmed, K=7202086800en_HK
dc.identifier.scopusauthoridDing, H=8726266600en_HK
dc.identifier.scopusauthoridDing, X=12140021800en_HK
dc.identifier.scopusauthoridLan, J=9744914000en_HK
dc.identifier.scopusauthoridYang, Z=13008800900en_HK
dc.identifier.scopusauthoridMiao, Y=8726267000en_HK
dc.identifier.scopusauthoridZhu, Y=7406072614en_HK
dc.identifier.scopusauthoridShi, Y=7404964663en_HK
dc.identifier.scopusauthoridZhu, J=8787884900en_HK
dc.identifier.scopusauthoridHuang, H=9744720200en_HK
dc.identifier.scopusauthoridYao, X=7402530401en_HK
dc.identifier.citeulike221071-
dc.identifier.issnl0950-9232-

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