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Article: The phosphatase-transcription activator EYA1 is targeted by anaphase-promoting complex/Cdh1 for degradation at M-to-G1 transition

TitleThe phosphatase-transcription activator EYA1 is targeted by anaphase-promoting complex/Cdh1 for degradation at M-to-G1 transition
Authors
Issue Date2013
PublisherAmerican Society for Microbiology.
Citation
Molecular and Cellular Biology, 2013, v. 33 n. 5, p. 927-936 How to Cite?
AbstractThe phosphatase and transactivator EYA family proteins are overexpressed in many cancer cell lines and are abundantly distributed in undifferentiated cells during development. Loss-of-function studies have shown that EYA1 is required for cell proliferation and survival during mammalian organogenesis. However, how EYA1 is regulated during development is unknown. Here, we report that EYA1 is regulated throughout the cell cycle via ubiquitin-mediated proteolysis. The level of EYA1 protein fluctuates in the cell cycle, peaking during mitosis and dropping drastically as cells exit into G(1). We found that EYA1 is efficiently degraded during mitotic exit in a Cdh1-dependent manner and that these two proteins physically interact. Overexpression of Cdh1 reduces the protein levels of ectopically expressed or endogenous EYA1, whereas depletion of Cdh1 by RNA interference stabilizes the EYA1 protein. Together, our results indicate that anaphase-promoting complex/cyclosome (APC/C)-Cdh1 specifically targets EYA1 for degradation during M-to-G(1) transition, failure of which may compromise cell proliferation and survival.
Persistent Identifierhttp://hdl.handle.net/10722/195098
ISSN
2015 Impact Factor: 4.427
2015 SCImago Journal Rankings: 3.806
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorSun, J-
dc.contributor.authorKaroulia, Z-
dc.contributor.authorWong, EYM-
dc.contributor.authorAhmed, M-
dc.contributor.authorItoh, K-
dc.contributor.authorXu, PX-
dc.date.accessioned2014-02-21T08:52:03Z-
dc.date.available2014-02-21T08:52:03Z-
dc.date.issued2013-
dc.identifier.citationMolecular and Cellular Biology, 2013, v. 33 n. 5, p. 927-936-
dc.identifier.issn0270-7306-
dc.identifier.urihttp://hdl.handle.net/10722/195098-
dc.description.abstractThe phosphatase and transactivator EYA family proteins are overexpressed in many cancer cell lines and are abundantly distributed in undifferentiated cells during development. Loss-of-function studies have shown that EYA1 is required for cell proliferation and survival during mammalian organogenesis. However, how EYA1 is regulated during development is unknown. Here, we report that EYA1 is regulated throughout the cell cycle via ubiquitin-mediated proteolysis. The level of EYA1 protein fluctuates in the cell cycle, peaking during mitosis and dropping drastically as cells exit into G(1). We found that EYA1 is efficiently degraded during mitotic exit in a Cdh1-dependent manner and that these two proteins physically interact. Overexpression of Cdh1 reduces the protein levels of ectopically expressed or endogenous EYA1, whereas depletion of Cdh1 by RNA interference stabilizes the EYA1 protein. Together, our results indicate that anaphase-promoting complex/cyclosome (APC/C)-Cdh1 specifically targets EYA1 for degradation during M-to-G(1) transition, failure of which may compromise cell proliferation and survival.-
dc.languageeng-
dc.publisherAmerican Society for Microbiology.-
dc.relation.ispartofMolecular and Cellular Biology-
dc.rightsMolecular and Cellular Biology. Copyright © American Society for Microbiology.-
dc.rightsCopyright © American Society for Microbiology, Molecular and Cellular Biology, 2013, v. 33 n. 5, p. 927-936-
dc.subject.meshG1 Phase-
dc.subject.meshIntracellular Signaling Peptides and Proteins - genetics - metabolism-
dc.subject.meshNuclear Proteins - genetics - metabolism-
dc.subject.meshProtein Tyrosine Phosphatases - genetics - metabolism-
dc.subject.meshUbiquitin-Protein Ligase Complexes - genetics - metabolism-
dc.titleThe phosphatase-transcription activator EYA1 is targeted by anaphase-promoting complex/Cdh1 for degradation at M-to-G1 transitionen_US
dc.typeArticleen_US
dc.identifier.emailWong, EYM: eymwongb@HKUCC.hku.hk-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1128/MCB.01516-12-
dc.identifier.pmid23263983-
dc.identifier.pmcidPMC3623089-
dc.identifier.scopuseid_2-s2.0-84874729909-
dc.identifier.hkuros270311-
dc.identifier.volume33-
dc.identifier.issue5-
dc.identifier.spage927-
dc.identifier.epage936-
dc.identifier.isiWOS:000317267800005-
dc.publisher.placeUnited States-

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