Activation of stress-activated protein kinase by MEKK1 phosphorylation of its activator SEK1
A kinase distinct from the MEK activator Raf, termed MEK kinase-1 (MEKK), was originally identified by virtue of its homology to kinases involved in yeast mating signal cascades. Like Raf, MEKK is capable of activating MEK in vitro. High-level expression of MEKK in COS-7 cells or using vaccinia viru...
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Veröffentlicht in: | Nature (London) 1994-12, Vol.372 (6508), p.798-800 |
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creator | MINHONG YAN TIANANG DAI DEAK, J. C KYRIAKIS, J. M ZON, L. I WOODGETT, J. R TEMPLETON, D. J |
description | A kinase distinct from the MEK activator Raf, termed MEK kinase-1 (MEKK), was originally identified by virtue of its homology to kinases involved in yeast mating signal cascades. Like Raf, MEKK is capable of activating MEK in vitro. High-level expression of MEKK in COS-7 cells or using vaccinia virus vectors also activates MEK and MAPK, indicating that MEKK and Raf provide alternative means of activating the MAPK signalling pathway. We have derived NIH3T3 cell sublines that can be induced to express active MEKK. Here we show that induction of MEKK does not result in the activation of MAPK, but instead stimulates the stress-activated protein kinases (SAPKs) which are identical to a Jun amino-terminal kinase. We find that MEKK regulates a new signalling cascade by phosphorylating an SAPK activator, SEK1 which in turn phosphorylates and activates SAPK. |
doi_str_mv | 10.1038/372798a0 |
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C ; KYRIAKIS, J. M ; ZON, L. I ; WOODGETT, J. R ; TEMPLETON, D. J</creator><creatorcontrib>MINHONG YAN ; TIANANG DAI ; DEAK, J. C ; KYRIAKIS, J. M ; ZON, L. I ; WOODGETT, J. R ; TEMPLETON, D. J</creatorcontrib><description>A kinase distinct from the MEK activator Raf, termed MEK kinase-1 (MEKK), was originally identified by virtue of its homology to kinases involved in yeast mating signal cascades. Like Raf, MEKK is capable of activating MEK in vitro. High-level expression of MEKK in COS-7 cells or using vaccinia virus vectors also activates MEK and MAPK, indicating that MEKK and Raf provide alternative means of activating the MAPK signalling pathway. We have derived NIH3T3 cell sublines that can be induced to express active MEKK. Here we show that induction of MEKK does not result in the activation of MAPK, but instead stimulates the stress-activated protein kinases (SAPKs) which are identical to a Jun amino-terminal kinase. We find that MEKK regulates a new signalling cascade by phosphorylating an SAPK activator, SEK1 which in turn phosphorylates and activates SAPK.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/372798a0</identifier><identifier>PMID: 7997270</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing</publisher><subject>3T3 Cells ; Animals ; Biological and medical sciences ; Cell physiology ; Cellular biology ; Enzyme Activation ; Enzyme Induction ; Fundamental and applied biological sciences. Psychology ; Heat-Shock Proteins - metabolism ; MAP Kinase Kinase 4 ; MAP Kinase Kinase Kinase 1 ; Mice ; Mitogen-Activated Protein Kinase Kinases ; Molecular and cellular biology ; Phosphorylation ; Protein Kinases - metabolism ; Protein-Serine-Threonine Kinases - biosynthesis ; Protein-Serine-Threonine Kinases - metabolism ; Protein-Tyrosine Kinases - biosynthesis ; Protein-Tyrosine Kinases - metabolism ; Proteins ; Recombinant Fusion Proteins - metabolism ; Signal Transduction ; Stress ; Transfection ; Yeasts</subject><ispartof>Nature (London), 1994-12, Vol.372 (6508), p.798-800</ispartof><rights>1995 INIST-CNRS</rights><rights>Copyright Macmillan Journals Ltd. Dec 22, 1994</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c432t-d0a7dd835b4810820b4c4bb4bd2c055d2af4e49c3b87d0685500ef545d9528583</citedby><cites>FETCH-LOGICAL-c432t-d0a7dd835b4810820b4c4bb4bd2c055d2af4e49c3b87d0685500ef545d9528583</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3409601$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7997270$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>MINHONG YAN</creatorcontrib><creatorcontrib>TIANANG DAI</creatorcontrib><creatorcontrib>DEAK, J. 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Here we show that induction of MEKK does not result in the activation of MAPK, but instead stimulates the stress-activated protein kinases (SAPKs) which are identical to a Jun amino-terminal kinase. We find that MEKK regulates a new signalling cascade by phosphorylating an SAPK activator, SEK1 which in turn phosphorylates and activates SAPK.</description><subject>3T3 Cells</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cell physiology</subject><subject>Cellular biology</subject><subject>Enzyme Activation</subject><subject>Enzyme Induction</subject><subject>Fundamental and applied biological sciences. 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Psychology</topic><topic>Heat-Shock Proteins - metabolism</topic><topic>MAP Kinase Kinase 4</topic><topic>MAP Kinase Kinase Kinase 1</topic><topic>Mice</topic><topic>Mitogen-Activated Protein Kinase Kinases</topic><topic>Molecular and cellular biology</topic><topic>Phosphorylation</topic><topic>Protein Kinases - metabolism</topic><topic>Protein-Serine-Threonine Kinases - biosynthesis</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>Protein-Tyrosine Kinases - biosynthesis</topic><topic>Protein-Tyrosine Kinases - metabolism</topic><topic>Proteins</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Signal Transduction</topic><topic>Stress</topic><topic>Transfection</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>MINHONG YAN</creatorcontrib><creatorcontrib>TIANANG DAI</creatorcontrib><creatorcontrib>DEAK, J. C</creatorcontrib><creatorcontrib>KYRIAKIS, J. 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Academic</collection><jtitle>Nature (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>MINHONG YAN</au><au>TIANANG DAI</au><au>DEAK, J. C</au><au>KYRIAKIS, J. M</au><au>ZON, L. I</au><au>WOODGETT, J. R</au><au>TEMPLETON, D. J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Activation of stress-activated protein kinase by MEKK1 phosphorylation of its activator SEK1</atitle><jtitle>Nature (London)</jtitle><addtitle>Nature</addtitle><date>1994-12-22</date><risdate>1994</risdate><volume>372</volume><issue>6508</issue><spage>798</spage><epage>800</epage><pages>798-800</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><coden>NATUAS</coden><abstract>A kinase distinct from the MEK activator Raf, termed MEK kinase-1 (MEKK), was originally identified by virtue of its homology to kinases involved in yeast mating signal cascades. Like Raf, MEKK is capable of activating MEK in vitro. High-level expression of MEKK in COS-7 cells or using vaccinia virus vectors also activates MEK and MAPK, indicating that MEKK and Raf provide alternative means of activating the MAPK signalling pathway. We have derived NIH3T3 cell sublines that can be induced to express active MEKK. Here we show that induction of MEKK does not result in the activation of MAPK, but instead stimulates the stress-activated protein kinases (SAPKs) which are identical to a Jun amino-terminal kinase. We find that MEKK regulates a new signalling cascade by phosphorylating an SAPK activator, SEK1 which in turn phosphorylates and activates SAPK.</abstract><cop>London</cop><pub>Nature Publishing</pub><pmid>7997270</pmid><doi>10.1038/372798a0</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record> |
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subjects | 3T3 Cells Animals Biological and medical sciences Cell physiology Cellular biology Enzyme Activation Enzyme Induction Fundamental and applied biological sciences. Psychology Heat-Shock Proteins - metabolism MAP Kinase Kinase 4 MAP Kinase Kinase Kinase 1 Mice Mitogen-Activated Protein Kinase Kinases Molecular and cellular biology Phosphorylation Protein Kinases - metabolism Protein-Serine-Threonine Kinases - biosynthesis Protein-Serine-Threonine Kinases - metabolism Protein-Tyrosine Kinases - biosynthesis Protein-Tyrosine Kinases - metabolism Proteins Recombinant Fusion Proteins - metabolism Signal Transduction Stress Transfection Yeasts |
title | Activation of stress-activated protein kinase by MEKK1 phosphorylation of its activator SEK1 |
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