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Conference Paper: Requirement of N-linked glycosylation in the luminal domain for optimal proteolytic activation of liver-enriched transcription factor CREB-H

TitleRequirement of N-linked glycosylation in the luminal domain for optimal proteolytic activation of liver-enriched transcription factor CREB-H
Authors
Issue Date2008
PublisherAmerican Society for Cell Biology. The Conference's web site is located at http://www.ascb.org/
Citation
The 48th Annual meeting of the American Society for Cell Biology (ASCB), San Francisco, USA, 13-17 December 2008. In Meeting Abstract p. 592 no. 2045/B510 How to Cite?
Abstract
CREB-H is a liver-enriched bZIP transcription factor closely related to CREB3. CREB-H is activated by intramembrane proteolysis that releases an N-terminal fragment. Aberrant expression of CREB-H is implicated in hepatocellular carcinoma. In this study we characterized N-linked glycosylation of CREB-H which occurs at three sites in the C-terminal luminal domain. When all three sites were disrupted by sitedirected mutagenesis, N-linked glycosylation of CREB-H was completely abrogated. The CREB-H mutants defective for N-linked glycosylation poorly activated transcription driven by unfolded protein response element or C-reactive protein promoter. Upon stimulation with an activator of intramembrane proteolysis such as brefeldin A, unglycosylated CREB-H remained largely uncleaved, anchored to the endoplasmic reticulum membrane, and unable to activate transcription. Taken together, our findings suggest that N-linked glycosylation is necessary for full activation of CREB-H through intramembrane proteolysis. Our work also reveals a novel mechanism for post-translational regulation of the CREB3 subfamily of membrane-associated transcription factors.
DescriptionMechanism of Nuclear Transcription (2035 – 2056) Session: Poster Session 3: no. 2045/B510
Persistent Identifierhttp://hdl.handle.net/10722/140096

 

DC FieldValueLanguage
dc.contributor.authorChan, CPen_US
dc.contributor.authorMak, TYen_US
dc.contributor.authorChin, KTen_US
dc.contributor.authorJin, Den_US
dc.date.accessioned2011-09-23T06:06:32Z-
dc.date.available2011-09-23T06:06:32Z-
dc.date.issued2008en_US
dc.identifier.citationThe 48th Annual meeting of the American Society for Cell Biology (ASCB), San Francisco, USA, 13-17 December 2008. In Meeting Abstract p. 592 no. 2045/B510en_US
dc.identifier.urihttp://hdl.handle.net/10722/140096-
dc.descriptionMechanism of Nuclear Transcription (2035 – 2056) Session: Poster Session 3: no. 2045/B510-
dc.description.abstractCREB-H is a liver-enriched bZIP transcription factor closely related to CREB3. CREB-H is activated by intramembrane proteolysis that releases an N-terminal fragment. Aberrant expression of CREB-H is implicated in hepatocellular carcinoma. In this study we characterized N-linked glycosylation of CREB-H which occurs at three sites in the C-terminal luminal domain. When all three sites were disrupted by sitedirected mutagenesis, N-linked glycosylation of CREB-H was completely abrogated. The CREB-H mutants defective for N-linked glycosylation poorly activated transcription driven by unfolded protein response element or C-reactive protein promoter. Upon stimulation with an activator of intramembrane proteolysis such as brefeldin A, unglycosylated CREB-H remained largely uncleaved, anchored to the endoplasmic reticulum membrane, and unable to activate transcription. Taken together, our findings suggest that N-linked glycosylation is necessary for full activation of CREB-H through intramembrane proteolysis. Our work also reveals a novel mechanism for post-translational regulation of the CREB3 subfamily of membrane-associated transcription factors.-
dc.languageengen_US
dc.publisherAmerican Society for Cell Biology. The Conference's web site is located at http://www.ascb.org/-
dc.relation.ispartofAnnual meeting of the American Society for Cell Biologyen_US
dc.titleRequirement of N-linked glycosylation in the luminal domain for optimal proteolytic activation of liver-enriched transcription factor CREB-Hen_US
dc.typeConference_Paperen_US
dc.identifier.emailChan, CP: chancp10@hku.hken_US
dc.identifier.emailJin, D: dyjin@hku.hken_US
dc.identifier.authorityJin, D=rp00452en_US
dc.identifier.hkuros193222en_US
dc.identifier.hkuros157415-
dc.publisher.placeUnited States-

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