File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: A human suppressor of c-Jun N-terminal kinase 1 activation by tumor necrosis factor α

TitleA human suppressor of c-Jun N-terminal kinase 1 activation by tumor necrosis factor α
Authors
Issue Date1997
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 1997, v. 272 n. 41, p. 25816-25823 How to Cite?
AbstractTumor necrosis factor α (TNFα) has pleiotropic effects on cellular metabolism. One of the signaling paths from the TNFα receptor induces a stress-activated protein kinase cascade. Components within this TNFα kinase cascade include mitogen-activated protein kinase/extracellular signal- regulated kinase kinase kinase 1 (MEKK1) and stress-activated protein kinase/extracellular signal-regulated kinase kinase (SEK), which regulate the activity of c-Jun N-terminal kinase 1 (JNK1). Currently, molecules upstream of MEKK1 that link TNFα receptor to downstream kinases are not well understood. Besides TNFα, many other stimuli including several oncoproteins can activate JNK1. In most cases, the signaling cascade(s) leading from oncoproteins to JNK1 is poorly elucidated. We report here that the human T- cell lymphotrophic virus, type I (HTLV-I) oncoprotein, Tax, can activate JNK1. We isolated a novel human cell factor, G-protein pathway suppressor 2 (GPS2), by its ability to bind the HTLV-I oncoprotein, and we show that this factor can potently suppress Tax activation of JNK1. In trying to understand the mechanism of GPS2 activity, we found that it also suppressed TNFα activation of JNK1 but not TNFα activation of p38 kinase nor phorbol activation of extracellular signal-regulated kinase 2. Because GPS2 has minimal effect on MEKK1- or SEK-regulated JNK1 activity, it could act at a point between the TNFα receptor and MEKK1 in the initial step(s) of this kinase cascade. Alternatively, it is not excluded that GPS2 could work in a parallel pathway that leads from TNFα to JNK1. GPS2 represents a new molecule that could contribute important insights toward how cytokine- and oncoprotein-mediated signal transduction might converge.
Persistent Identifierhttp://hdl.handle.net/10722/147412
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorJin, DYen_US
dc.contributor.authorTeramoto, Hen_US
dc.contributor.authorGiam, CZen_US
dc.contributor.authorChun, RFen_US
dc.contributor.authorGutkind, JSen_US
dc.contributor.authorJeang, KTen_US
dc.date.accessioned2012-05-29T06:03:32Z-
dc.date.available2012-05-29T06:03:32Z-
dc.date.issued1997en_US
dc.identifier.citationJournal Of Biological Chemistry, 1997, v. 272 n. 41, p. 25816-25823en_US
dc.identifier.issn0021-9258en_US
dc.identifier.urihttp://hdl.handle.net/10722/147412-
dc.description.abstractTumor necrosis factor α (TNFα) has pleiotropic effects on cellular metabolism. One of the signaling paths from the TNFα receptor induces a stress-activated protein kinase cascade. Components within this TNFα kinase cascade include mitogen-activated protein kinase/extracellular signal- regulated kinase kinase kinase 1 (MEKK1) and stress-activated protein kinase/extracellular signal-regulated kinase kinase (SEK), which regulate the activity of c-Jun N-terminal kinase 1 (JNK1). Currently, molecules upstream of MEKK1 that link TNFα receptor to downstream kinases are not well understood. Besides TNFα, many other stimuli including several oncoproteins can activate JNK1. In most cases, the signaling cascade(s) leading from oncoproteins to JNK1 is poorly elucidated. We report here that the human T- cell lymphotrophic virus, type I (HTLV-I) oncoprotein, Tax, can activate JNK1. We isolated a novel human cell factor, G-protein pathway suppressor 2 (GPS2), by its ability to bind the HTLV-I oncoprotein, and we show that this factor can potently suppress Tax activation of JNK1. In trying to understand the mechanism of GPS2 activity, we found that it also suppressed TNFα activation of JNK1 but not TNFα activation of p38 kinase nor phorbol activation of extracellular signal-regulated kinase 2. Because GPS2 has minimal effect on MEKK1- or SEK-regulated JNK1 activity, it could act at a point between the TNFα receptor and MEKK1 in the initial step(s) of this kinase cascade. Alternatively, it is not excluded that GPS2 could work in a parallel pathway that leads from TNFα to JNK1. GPS2 represents a new molecule that could contribute important insights toward how cytokine- and oncoprotein-mediated signal transduction might converge.en_US
dc.languageengen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_US
dc.relation.ispartofJournal of Biological Chemistryen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshBase Sequenceen_US
dc.subject.meshCalcium-Calmodulin-Dependent Protein Kinases - Antagonists & Inhibitors - Metabolismen_US
dc.subject.meshEnzyme Activationen_US
dc.subject.meshFungal Proteins - Metabolismen_US
dc.subject.meshGene Products, Tax - Metabolism - Pharmacologyen_US
dc.subject.meshHela Cellsen_US
dc.subject.meshHumansen_US
dc.subject.meshIntracellular Signaling Peptides And Proteinsen_US
dc.subject.meshJnk Mitogen-Activated Protein Kinasesen_US
dc.subject.meshJurkat Cellsen_US
dc.subject.meshMap Kinase Kinase Kinase 1en_US
dc.subject.meshMitogen-Activated Protein Kinasesen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshProtein-Serine-Threonine Kinases - Metabolismen_US
dc.subject.meshProtein-Tyrosine Kinases - Metabolismen_US
dc.subject.meshRepressor Proteinsen_US
dc.subject.meshTumor Necrosis Factor-Alpha - Metabolism - Pharmacologyen_US
dc.subject.meshP38 Mitogen-Activated Protein Kinasesen_US
dc.titleA human suppressor of c-Jun N-terminal kinase 1 activation by tumor necrosis factor αen_US
dc.typeArticleen_US
dc.identifier.emailJin, DY:dyjin@hkucc.hku.hken_US
dc.identifier.authorityJin, DY=rp00452en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1074/jbc.272.41.25816en_US
dc.identifier.pmid9325311-
dc.identifier.scopuseid_2-s2.0-0030754827en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0030754827&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume272en_US
dc.identifier.issue41en_US
dc.identifier.spage25816en_US
dc.identifier.epage25823en_US
dc.identifier.isiWOS:A1997YA35800066-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridJin, DY=7201973614en_US
dc.identifier.scopusauthoridTeramoto, H=7005933439en_US
dc.identifier.scopusauthoridGiam, CZ=7006154106en_US
dc.identifier.scopusauthoridChun, RF=7005563719en_US
dc.identifier.scopusauthoridGutkind, JS=8844600700en_US
dc.identifier.scopusauthoridJeang, KT=7004824803en_US

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats