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Conference Paper: Identification of novel nuclear export domains of transcription factor OREBP/TonEBP/NFAT5

TitleIdentification of novel nuclear export domains of transcription factor OREBP/TonEBP/NFAT5
Authors
Issue Date2006
PublisherFederation of American Societies for Experimental Biology
Citation
Experimental Biology 2006, San Francisco, CA, 1-5 April 2006. In The FASEB Journal, 2006, v, 20 n. 5, p. A823-A824 How to Cite?
AbstractThe Osmotic Response Element-Binding Protein (OREBP), also known as the Tonicity Enhancer-Binding Protein (TonEBP) or NFAT5, regulates the hypertonicity-induced expression of a battery of genes crucial for the adaptation of mammalian cells to extracellular hypertonic stress. The activity of OREBP/TonEBP is regulated at multiple levels including nucleocytoplasmic trafficking. Specifically, OREBP/TonEBP undergoes nuclear translocation and export under hypertonic and hypotonic condition respectively. Here we show that, by immunocytochemistry and GFP fusion, the transactivation domain of OREBP/TonEBP is dispensable for proper subcellular localization of OREBP/TonEBP in response to change in osmolality. Under isotonicity, OREBP/TonEBP undergoes nucleocytoplasmic shuttling which can be blocked by leptomycin B (LMB) treatment. Unexpectedly, two leucine-rich motifs that exhibit significant sequence similarity to canonical nuclear export signal (NES) located in the N-terminal of OREBP/TonEBP are not responsible for the export. Nevertheless, we identified a CRM1 responsive protein domain (designated NES-A) responsible for the nucleocytoplasmic shuttling of OREBP/TonEBP under isotonicity. Disruption of NES-A increases nuclear translocation of OREBP/TonEBP, yet hypotonicity is able to direct nuclear export of this mutant. Moreover, we identified a second protein motif (designated NES-B) that is critical for OREBP/TonEBP nuclear export under both isotonic and hypotonic conditions. Disruption of the NES-B alone is sufficient to cause aberrant nuclear translocation of OREBP/TonEBP irrespective of extracellular tonicity. Our study provides novel insights on the regulation of nucleo-cytoplasmic trafficking of OREBP/TonEBP.
Persistent Identifierhttp://hdl.handle.net/10722/105190
ISSN
2015 Impact Factor: 5.299
2015 SCImago Journal Rankings: 2.775

 

DC FieldValueLanguage
dc.contributor.authorKo, CBen_HK
dc.contributor.authorTong, HYen_HK
dc.contributor.authorGuo, Jen_HK
dc.contributor.authorChung, SSMen_HK
dc.date.accessioned2010-09-25T22:23:51Z-
dc.date.available2010-09-25T22:23:51Z-
dc.date.issued2006en_HK
dc.identifier.citationExperimental Biology 2006, San Francisco, CA, 1-5 April 2006. In The FASEB Journal, 2006, v, 20 n. 5, p. A823-A824-
dc.identifier.issn0892-6638-
dc.identifier.urihttp://hdl.handle.net/10722/105190-
dc.description.abstractThe Osmotic Response Element-Binding Protein (OREBP), also known as the Tonicity Enhancer-Binding Protein (TonEBP) or NFAT5, regulates the hypertonicity-induced expression of a battery of genes crucial for the adaptation of mammalian cells to extracellular hypertonic stress. The activity of OREBP/TonEBP is regulated at multiple levels including nucleocytoplasmic trafficking. Specifically, OREBP/TonEBP undergoes nuclear translocation and export under hypertonic and hypotonic condition respectively. Here we show that, by immunocytochemistry and GFP fusion, the transactivation domain of OREBP/TonEBP is dispensable for proper subcellular localization of OREBP/TonEBP in response to change in osmolality. Under isotonicity, OREBP/TonEBP undergoes nucleocytoplasmic shuttling which can be blocked by leptomycin B (LMB) treatment. Unexpectedly, two leucine-rich motifs that exhibit significant sequence similarity to canonical nuclear export signal (NES) located in the N-terminal of OREBP/TonEBP are not responsible for the export. Nevertheless, we identified a CRM1 responsive protein domain (designated NES-A) responsible for the nucleocytoplasmic shuttling of OREBP/TonEBP under isotonicity. Disruption of NES-A increases nuclear translocation of OREBP/TonEBP, yet hypotonicity is able to direct nuclear export of this mutant. Moreover, we identified a second protein motif (designated NES-B) that is critical for OREBP/TonEBP nuclear export under both isotonic and hypotonic conditions. Disruption of the NES-B alone is sufficient to cause aberrant nuclear translocation of OREBP/TonEBP irrespective of extracellular tonicity. Our study provides novel insights on the regulation of nucleo-cytoplasmic trafficking of OREBP/TonEBP.-
dc.languageengen_HK
dc.publisherFederation of American Societies for Experimental Biology-
dc.relation.ispartofThe FASEB Journalen_HK
dc.titleIdentification of novel nuclear export domains of transcription factor OREBP/TonEBP/NFAT5en_HK
dc.typeConference_Paperen_HK
dc.identifier.emailKo, CB: cbko@hkucc.hku.hken_HK
dc.identifier.emailGuo, J: guojinjun1972@hotmail.comen_HK
dc.identifier.emailChung, SSM: smchung@hkucc.hku.hken_HK
dc.identifier.authorityChung, SSM=rp00376en_HK
dc.identifier.hkuros117995en_HK

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