File Download
 
 
Supplementary

Conference Paper: Requirement of N-linked glycosylation in the luminal domain for optimal proteolytic activation of liver-enriched transcription factor CREB-H
  • Basic View
  • Metadata View
  • XML View
TitleRequirement of N-linked glycosylation in the luminal domain for optimal proteolytic activation of liver-enriched transcription factor CREB-H
 
AuthorsChan, CP
Mak, TY
Chin, KT
Jin, D
 
Issue Date2008
 
PublisherAmerican Society for Cell Biology. The Conference's web site is located at http://www.ascb.org/
 
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/B510 [How to Cite?]
 
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.
 
DescriptionMechanism of Nuclear Transcription (2035 – 2056) Session: Poster Session 3: no. 2045/B510
 
DC FieldValue
dc.contributor.authorChan, CP
 
dc.contributor.authorMak, TY
 
dc.contributor.authorChin, KT
 
dc.contributor.authorJin, D
 
dc.date.accessioned2011-09-23T06:06:32Z
 
dc.date.available2011-09-23T06:06:32Z
 
dc.date.issued2008
 
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.descriptionMechanism of Nuclear Transcription (2035 – 2056) Session: Poster Session 3: no. 2045/B510
 
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/B510 [How to Cite?]
 
dc.identifier.hkuros193222
 
dc.identifier.hkuros157415
 
dc.identifier.urihttp://hdl.handle.net/10722/140096
 
dc.languageeng
 
dc.publisherAmerican Society for Cell Biology. The Conference's web site is located at http://www.ascb.org/
 
dc.publisher.placeUnited States
 
dc.relation.ispartofAnnual meeting of the American Society for Cell Biology
 
dc.titleRequirement of N-linked glycosylation in the luminal domain for optimal proteolytic activation of liver-enriched transcription factor CREB-H
 
dc.typeConference_Paper
 
<?xml encoding="utf-8" version="1.0"?>
<item><contributor.author>Chan, CP</contributor.author>
<contributor.author>Mak, TY</contributor.author>
<contributor.author>Chin, KT</contributor.author>
<contributor.author>Jin, D</contributor.author>
<date.accessioned>2011-09-23T06:06:32Z</date.accessioned>
<date.available>2011-09-23T06:06:32Z</date.available>
<date.issued>2008</date.issued>
<identifier.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</identifier.citation>
<identifier.uri>http://hdl.handle.net/10722/140096</identifier.uri>
<description>Mechanism of Nuclear Transcription (2035 &#8211; 2056) Session: Poster Session 3: no. 2045/B510</description>
<description.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.</description.abstract>
<language>eng</language>
<publisher>American Society for Cell Biology. The Conference&apos;s web site is located at http://www.ascb.org/</publisher>
<relation.ispartof>Annual meeting of the American Society for Cell Biology</relation.ispartof>
<title>Requirement of N-linked glycosylation in the luminal domain for optimal proteolytic activation of liver-enriched transcription factor CREB-H</title>
<type>Conference_Paper</type>
<identifier.hkuros>193222</identifier.hkuros>
<identifier.hkuros>157415</identifier.hkuros>
<publisher.place>United States</publisher.place>
</item>