Modulation of Spc1 stress-activated protein kinase activity by methylglyoxal through inhibition of protein phosphatase in the fission yeast Schizosaccharomyces pombe
Methylglyoxal, a ubiquitous metabolite derived from glycolysis has diverse physiological functions in yeast cells. Previously, we have reported that extracellularly added methylglyoxal activates Spc1, a stress-activated protein kinase (SAPK), in the fission yeast Schizosaccharomyces pombe [Y. Takats...
Gespeichert in:
| Veröffentlicht in: | Biochemical and biophysical research communications 2007-11, Vol.363 (4), p.942-947 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 947 |
|---|---|
| container_issue | 4 |
| container_start_page | 942 |
| container_title | Biochemical and biophysical research communications |
| container_volume | 363 |
| creator | Takatsume, Yoshifumi Izawa, Shingo Inoue, Yoshiharu |
| description | Methylglyoxal, a ubiquitous metabolite derived from glycolysis has diverse physiological functions in yeast cells. Previously, we have reported that extracellularly added methylglyoxal activates Spc1, a stress-activated protein kinase (SAPK), in the fission yeast
Schizosaccharomyces pombe [Y. Takatsume, S. Izawa, Y. Inoue, J. Biol. Chem. 281 (2006) 9086–9092]. Phosphorylation of Spc1 by treatment with methylglyoxal in
S. pombe cells defective in glyoxalase I, an enzyme crucial for the metabolism of methylglyoxal, continues for a longer period than in wild-type cells. Here we show that methylglyoxal inhibits the activity of the protein phosphatase responsible for the dephosphorylation of Spc1 in vitro. In addition, we found that methylglyoxal inhibits human protein tyrosine phosphatase 1B (PTP1B) also. We propose a model for the regulation of the activity of the Spc1-SAPK signaling pathway by methylglyoxal in
S. pombe. |
| doi_str_mv | 10.1016/j.bbrc.2007.09.071 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_osti_</sourceid><recordid>TN_cdi_osti_scitechconnect_21032994</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0006291X07020499</els_id><sourcerecordid>68400646</sourcerecordid><originalsourceid>FETCH-LOGICAL-c479t-4951afba38934b9c27e494f4d695c524d882a3ba2c5cc412e030ab6566ebb4733</originalsourceid><addsrcrecordid>eNqFkcGK1TAYhYsoznX0BVxIQHDXmqRpegNuZNBRGHExCu5Ckv6d5No2NUkH6_vMe5p67-BOV-En3zlwzimK5wRXBBP--lBpHUxFMW4rLCrckgfFjmCBS0owe1jsMMa8pIJ8OyuexHjAmBDGxePijLSCCNawXXH3yXfLoJLzE_I9up4NQTEFiLFUJrlblaBDc_AJ3IS-u0lFQH8-XFqRXtEIya7DzbD6n2pAyQa_3FjkJuu0uze9l8_Wx9mqtHnkM1lAvYtxo1ZQMaFrY90vH5UxVgU_rgYimv2o4WnxqFdDhGen97z4-v7dl4sP5dXny48Xb69Kw1qRSiYaonqt6r2omRaGtsAE61nHRWMayrr9nqpaK2oaYxihgGusNG84B61ZW9fnxcujr4_JyWhcAmONnyYwSeZSayoEy9SrI5WD_VggJjm6aGAY1AR-iZLvWS6e8f-CFNctF4JkkB5BE3yMAXo5BzeqsEqC5ba1PMhta7ltLbGQeessenFyX_QI3V_JadwMvDkCkCu7dRC2RDAZ6FzYAnXe_cv_NyyGvu0</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>20376991</pqid></control><display><type>article</type><title>Modulation of Spc1 stress-activated protein kinase activity by methylglyoxal through inhibition of protein phosphatase in the fission yeast Schizosaccharomyces pombe</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals Complete</source><creator>Takatsume, Yoshifumi ; Izawa, Shingo ; Inoue, Yoshiharu</creator><creatorcontrib>Takatsume, Yoshifumi ; Izawa, Shingo ; Inoue, Yoshiharu</creatorcontrib><description>Methylglyoxal, a ubiquitous metabolite derived from glycolysis has diverse physiological functions in yeast cells. Previously, we have reported that extracellularly added methylglyoxal activates Spc1, a stress-activated protein kinase (SAPK), in the fission yeast
Schizosaccharomyces pombe [Y. Takatsume, S. Izawa, Y. Inoue, J. Biol. Chem. 281 (2006) 9086–9092]. Phosphorylation of Spc1 by treatment with methylglyoxal in
S. pombe cells defective in glyoxalase I, an enzyme crucial for the metabolism of methylglyoxal, continues for a longer period than in wild-type cells. Here we show that methylglyoxal inhibits the activity of the protein phosphatase responsible for the dephosphorylation of Spc1 in vitro. In addition, we found that methylglyoxal inhibits human protein tyrosine phosphatase 1B (PTP1B) also. We propose a model for the regulation of the activity of the Spc1-SAPK signaling pathway by methylglyoxal in
S. pombe.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2007.09.071</identifier><identifier>PMID: 17919454</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>60 APPLIED LIFE SCIENCES ; ENZYMES ; Gene Deletion ; GLYCOLYSIS ; Humans ; IN VITRO ; INHIBITION ; MAP kinase ; Methylglyoxal ; Mitogen-Activated Protein Kinases - genetics ; Mitogen-Activated Protein Kinases - metabolism ; MODULATION ; Phosphoprotein Phosphatases - antagonists & inhibitors ; Phosphoprotein Phosphatases - metabolism ; PHOSPHORYLATION ; Protein Kinase Inhibitors - pharmacology ; Protein phosphatase ; Protein Tyrosine Phosphatase, Non-Receptor Type 1 - antagonists & inhibitors ; Protein Tyrosine Phosphatase, Non-Receptor Type 1 - metabolism ; PTP1B ; Pyruvaldehyde - pharmacology ; Schizosaccharomyces - drug effects ; Schizosaccharomyces - enzymology ; Schizosaccharomyces pombe ; Schizosaccharomyces pombe Proteins - genetics ; Schizosaccharomyces pombe Proteins - metabolism ; Signal Transduction ; TYROSINE ; YEASTS</subject><ispartof>Biochemical and biophysical research communications, 2007-11, Vol.363 (4), p.942-947</ispartof><rights>2007 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c479t-4951afba38934b9c27e494f4d695c524d882a3ba2c5cc412e030ab6566ebb4733</citedby><cites>FETCH-LOGICAL-c479t-4951afba38934b9c27e494f4d695c524d882a3ba2c5cc412e030ab6566ebb4733</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006291X07020499$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,776,780,881,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17919454$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/21032994$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Takatsume, Yoshifumi</creatorcontrib><creatorcontrib>Izawa, Shingo</creatorcontrib><creatorcontrib>Inoue, Yoshiharu</creatorcontrib><title>Modulation of Spc1 stress-activated protein kinase activity by methylglyoxal through inhibition of protein phosphatase in the fission yeast Schizosaccharomyces pombe</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Methylglyoxal, a ubiquitous metabolite derived from glycolysis has diverse physiological functions in yeast cells. Previously, we have reported that extracellularly added methylglyoxal activates Spc1, a stress-activated protein kinase (SAPK), in the fission yeast
Schizosaccharomyces pombe [Y. Takatsume, S. Izawa, Y. Inoue, J. Biol. Chem. 281 (2006) 9086–9092]. Phosphorylation of Spc1 by treatment with methylglyoxal in
S. pombe cells defective in glyoxalase I, an enzyme crucial for the metabolism of methylglyoxal, continues for a longer period than in wild-type cells. Here we show that methylglyoxal inhibits the activity of the protein phosphatase responsible for the dephosphorylation of Spc1 in vitro. In addition, we found that methylglyoxal inhibits human protein tyrosine phosphatase 1B (PTP1B) also. We propose a model for the regulation of the activity of the Spc1-SAPK signaling pathway by methylglyoxal in
S. pombe.</description><subject>60 APPLIED LIFE SCIENCES</subject><subject>ENZYMES</subject><subject>Gene Deletion</subject><subject>GLYCOLYSIS</subject><subject>Humans</subject><subject>IN VITRO</subject><subject>INHIBITION</subject><subject>MAP kinase</subject><subject>Methylglyoxal</subject><subject>Mitogen-Activated Protein Kinases - genetics</subject><subject>Mitogen-Activated Protein Kinases - metabolism</subject><subject>MODULATION</subject><subject>Phosphoprotein Phosphatases - antagonists & inhibitors</subject><subject>Phosphoprotein Phosphatases - metabolism</subject><subject>PHOSPHORYLATION</subject><subject>Protein Kinase Inhibitors - pharmacology</subject><subject>Protein phosphatase</subject><subject>Protein Tyrosine Phosphatase, Non-Receptor Type 1 - antagonists & inhibitors</subject><subject>Protein Tyrosine Phosphatase, Non-Receptor Type 1 - metabolism</subject><subject>PTP1B</subject><subject>Pyruvaldehyde - pharmacology</subject><subject>Schizosaccharomyces - drug effects</subject><subject>Schizosaccharomyces - enzymology</subject><subject>Schizosaccharomyces pombe</subject><subject>Schizosaccharomyces pombe Proteins - genetics</subject><subject>Schizosaccharomyces pombe Proteins - metabolism</subject><subject>Signal Transduction</subject><subject>TYROSINE</subject><subject>YEASTS</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkcGK1TAYhYsoznX0BVxIQHDXmqRpegNuZNBRGHExCu5Ckv6d5No2NUkH6_vMe5p67-BOV-En3zlwzimK5wRXBBP--lBpHUxFMW4rLCrckgfFjmCBS0owe1jsMMa8pIJ8OyuexHjAmBDGxePijLSCCNawXXH3yXfLoJLzE_I9up4NQTEFiLFUJrlblaBDc_AJ3IS-u0lFQH8-XFqRXtEIya7DzbD6n2pAyQa_3FjkJuu0uze9l8_Wx9mqtHnkM1lAvYtxo1ZQMaFrY90vH5UxVgU_rgYimv2o4WnxqFdDhGen97z4-v7dl4sP5dXny48Xb69Kw1qRSiYaonqt6r2omRaGtsAE61nHRWMayrr9nqpaK2oaYxihgGusNG84B61ZW9fnxcujr4_JyWhcAmONnyYwSeZSayoEy9SrI5WD_VggJjm6aGAY1AR-iZLvWS6e8f-CFNctF4JkkB5BE3yMAXo5BzeqsEqC5ba1PMhta7ltLbGQeessenFyX_QI3V_JadwMvDkCkCu7dRC2RDAZ6FzYAnXe_cv_NyyGvu0</recordid><startdate>20071130</startdate><enddate>20071130</enddate><creator>Takatsume, Yoshifumi</creator><creator>Izawa, Shingo</creator><creator>Inoue, Yoshiharu</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>M7N</scope><scope>7X8</scope><scope>OTOTI</scope></search><sort><creationdate>20071130</creationdate><title>Modulation of Spc1 stress-activated protein kinase activity by methylglyoxal through inhibition of protein phosphatase in the fission yeast Schizosaccharomyces pombe</title><author>Takatsume, Yoshifumi ; Izawa, Shingo ; Inoue, Yoshiharu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c479t-4951afba38934b9c27e494f4d695c524d882a3ba2c5cc412e030ab6566ebb4733</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>60 APPLIED LIFE SCIENCES</topic><topic>ENZYMES</topic><topic>Gene Deletion</topic><topic>GLYCOLYSIS</topic><topic>Humans</topic><topic>IN VITRO</topic><topic>INHIBITION</topic><topic>MAP kinase</topic><topic>Methylglyoxal</topic><topic>Mitogen-Activated Protein Kinases - genetics</topic><topic>Mitogen-Activated Protein Kinases - metabolism</topic><topic>MODULATION</topic><topic>Phosphoprotein Phosphatases - antagonists & inhibitors</topic><topic>Phosphoprotein Phosphatases - metabolism</topic><topic>PHOSPHORYLATION</topic><topic>Protein Kinase Inhibitors - pharmacology</topic><topic>Protein phosphatase</topic><topic>Protein Tyrosine Phosphatase, Non-Receptor Type 1 - antagonists & inhibitors</topic><topic>Protein Tyrosine Phosphatase, Non-Receptor Type 1 - metabolism</topic><topic>PTP1B</topic><topic>Pyruvaldehyde - pharmacology</topic><topic>Schizosaccharomyces - drug effects</topic><topic>Schizosaccharomyces - enzymology</topic><topic>Schizosaccharomyces pombe</topic><topic>Schizosaccharomyces pombe Proteins - genetics</topic><topic>Schizosaccharomyces pombe Proteins - metabolism</topic><topic>Signal Transduction</topic><topic>TYROSINE</topic><topic>YEASTS</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Takatsume, Yoshifumi</creatorcontrib><creatorcontrib>Izawa, Shingo</creatorcontrib><creatorcontrib>Inoue, Yoshiharu</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Takatsume, Yoshifumi</au><au>Izawa, Shingo</au><au>Inoue, Yoshiharu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Modulation of Spc1 stress-activated protein kinase activity by methylglyoxal through inhibition of protein phosphatase in the fission yeast Schizosaccharomyces pombe</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2007-11-30</date><risdate>2007</risdate><volume>363</volume><issue>4</issue><spage>942</spage><epage>947</epage><pages>942-947</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Methylglyoxal, a ubiquitous metabolite derived from glycolysis has diverse physiological functions in yeast cells. Previously, we have reported that extracellularly added methylglyoxal activates Spc1, a stress-activated protein kinase (SAPK), in the fission yeast
Schizosaccharomyces pombe [Y. Takatsume, S. Izawa, Y. Inoue, J. Biol. Chem. 281 (2006) 9086–9092]. Phosphorylation of Spc1 by treatment with methylglyoxal in
S. pombe cells defective in glyoxalase I, an enzyme crucial for the metabolism of methylglyoxal, continues for a longer period than in wild-type cells. Here we show that methylglyoxal inhibits the activity of the protein phosphatase responsible for the dephosphorylation of Spc1 in vitro. In addition, we found that methylglyoxal inhibits human protein tyrosine phosphatase 1B (PTP1B) also. We propose a model for the regulation of the activity of the Spc1-SAPK signaling pathway by methylglyoxal in
S. pombe.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>17919454</pmid><doi>10.1016/j.bbrc.2007.09.071</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-291X |
| ispartof | Biochemical and biophysical research communications, 2007-11, Vol.363 (4), p.942-947 |
| issn | 0006-291X 1090-2104 |
| language | eng |
| recordid | cdi_osti_scitechconnect_21032994 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | 60 APPLIED LIFE SCIENCES ENZYMES Gene Deletion GLYCOLYSIS Humans IN VITRO INHIBITION MAP kinase Methylglyoxal Mitogen-Activated Protein Kinases - genetics Mitogen-Activated Protein Kinases - metabolism MODULATION Phosphoprotein Phosphatases - antagonists & inhibitors Phosphoprotein Phosphatases - metabolism PHOSPHORYLATION Protein Kinase Inhibitors - pharmacology Protein phosphatase Protein Tyrosine Phosphatase, Non-Receptor Type 1 - antagonists & inhibitors Protein Tyrosine Phosphatase, Non-Receptor Type 1 - metabolism PTP1B Pyruvaldehyde - pharmacology Schizosaccharomyces - drug effects Schizosaccharomyces - enzymology Schizosaccharomyces pombe Schizosaccharomyces pombe Proteins - genetics Schizosaccharomyces pombe Proteins - metabolism Signal Transduction TYROSINE YEASTS |
| title | Modulation of Spc1 stress-activated protein kinase activity by methylglyoxal through inhibition of protein phosphatase in the fission yeast Schizosaccharomyces pombe |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-19T10%3A42%3A41IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_osti_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Modulation%20of%20Spc1%20stress-activated%20protein%20kinase%20activity%20by%20methylglyoxal%20through%20inhibition%20of%20protein%20phosphatase%20in%20the%20fission%20yeast%20Schizosaccharomyces%20pombe&rft.jtitle=Biochemical%20and%20biophysical%20research%20communications&rft.au=Takatsume,%20Yoshifumi&rft.date=2007-11-30&rft.volume=363&rft.issue=4&rft.spage=942&rft.epage=947&rft.pages=942-947&rft.issn=0006-291X&rft.eissn=1090-2104&rft_id=info:doi/10.1016/j.bbrc.2007.09.071&rft_dat=%3Cproquest_osti_%3E68400646%3C/proquest_osti_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=20376991&rft_id=info:pmid/17919454&rft_els_id=S0006291X07020499&rfr_iscdi=true |