The phosphorylation of stathmin by MAP kinase
Stathmin, a ubiquitous cytosolic phosphoprotein which may play a role in integrating the effects of diverse signals regulating proliferation, differentiation and other cell functions, was found to be phosphorylated rapidly and stoichiometrically by mitogen-activated protein (MAP) kinase in vitro. Se...
Gespeichert in:
| Veröffentlicht in: | Molecular and cellular biochemistry 1993-11, Vol.127-128 (1), p.151-156 |
|---|---|
| Hauptverfasser: | , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 156 |
|---|---|
| container_issue | 1 |
| container_start_page | 151 |
| container_title | Molecular and cellular biochemistry |
| container_volume | 127-128 |
| creator | Leighton, I A Curmi, P Campbell, D G Cohen, P Sobel, A |
| description | Stathmin, a ubiquitous cytosolic phosphoprotein which may play a role in integrating the effects of diverse signals regulating proliferation, differentiation and other cell functions, was found to be phosphorylated rapidly and stoichiometrically by mitogen-activated protein (MAP) kinase in vitro. Ser-25 was identified as the major site and Ser-38 as a minor site of phosphorylation, while the p42 and p44 isoforms of MAP kinase were the only significant stathmin kinases detected in PC12 cells after stimulation by nerve growth factor (NGF). The results suggest that MAP kinases are the enzymes responsible for increasing the level of phosphorylation of Ser-25, which has been observed previously in PC12 cells following stimulation by NGF. |
| doi_str_mv | 10.1007/bf01076766 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_76309237</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>76309237</sourcerecordid><originalsourceid>FETCH-LOGICAL-c348t-f8887d271f756010a8b053567d1f0d03e71678ab2affe92355fb05113cae36f13</originalsourceid><addsrcrecordid>eNo90D1PwzAQBmALgUopLOxImRiQAne92ueMpWoBqQiGMkdOYquBfJQ4GfrvMWphON3y3HvSK8Q1wj0C8EPmAIEVK3UixiiZ4lmCyakYAwHEGpnPxYX3nxAYII7EiBOSNOOxiDdbG-22rQ_T7SvTl20TtS7yvem3ddlE2T56nb9HX2VjvL0UZ85U3l4d90R8rJabxXO8fnt6WczXcU4z3cdOa83FlNGxVOGn0RlIkooLdFAAWUbF2mRT45xNpiSlCwCRcmNJOaSJuD3k7rr2e7C-T-vS57aqTGPbwaesCMIdB3h3gHnXet9Zl-66sjbdPkVIf7tJH1d_3QR8c0wdstoW__RYBv0ABKRcOg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>76309237</pqid></control><display><type>article</type><title>The phosphorylation of stathmin by MAP kinase</title><source>MEDLINE</source><source>Springer Nature - Complete Springer Journals</source><creator>Leighton, I A ; Curmi, P ; Campbell, D G ; Cohen, P ; Sobel, A</creator><creatorcontrib>Leighton, I A ; Curmi, P ; Campbell, D G ; Cohen, P ; Sobel, A</creatorcontrib><description>Stathmin, a ubiquitous cytosolic phosphoprotein which may play a role in integrating the effects of diverse signals regulating proliferation, differentiation and other cell functions, was found to be phosphorylated rapidly and stoichiometrically by mitogen-activated protein (MAP) kinase in vitro. Ser-25 was identified as the major site and Ser-38 as a minor site of phosphorylation, while the p42 and p44 isoforms of MAP kinase were the only significant stathmin kinases detected in PC12 cells after stimulation by nerve growth factor (NGF). The results suggest that MAP kinases are the enzymes responsible for increasing the level of phosphorylation of Ser-25, which has been observed previously in PC12 cells following stimulation by NGF.</description><identifier>ISSN: 0300-8177</identifier><identifier>EISSN: 1573-4919</identifier><identifier>DOI: 10.1007/bf01076766</identifier><identifier>PMID: 7935347</identifier><language>eng</language><publisher>Netherlands</publisher><subject>Amino Acid Sequence ; Animals ; Calcium-Calmodulin-Dependent Protein Kinases - metabolism ; Kinetics ; Microtubule Proteins ; Molecular Sequence Data ; Nerve Growth Factors - pharmacology ; PC12 Cells ; Peptide Fragments - chemistry ; Peptide Fragments - metabolism ; Phosphopeptides - chemistry ; Phosphopeptides - metabolism ; Phosphoproteins - metabolism ; Phosphorus Radioisotopes ; Phosphorylation ; Phosphoserine - analysis ; Rats ; Recombinant Proteins - metabolism ; Serine ; Signal Transduction ; Stathmin</subject><ispartof>Molecular and cellular biochemistry, 1993-11, Vol.127-128 (1), p.151-156</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c348t-f8887d271f756010a8b053567d1f0d03e71678ab2affe92355fb05113cae36f13</citedby><cites>FETCH-LOGICAL-c348t-f8887d271f756010a8b053567d1f0d03e71678ab2affe92355fb05113cae36f13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7935347$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Leighton, I A</creatorcontrib><creatorcontrib>Curmi, P</creatorcontrib><creatorcontrib>Campbell, D G</creatorcontrib><creatorcontrib>Cohen, P</creatorcontrib><creatorcontrib>Sobel, A</creatorcontrib><title>The phosphorylation of stathmin by MAP kinase</title><title>Molecular and cellular biochemistry</title><addtitle>Mol Cell Biochem</addtitle><description>Stathmin, a ubiquitous cytosolic phosphoprotein which may play a role in integrating the effects of diverse signals regulating proliferation, differentiation and other cell functions, was found to be phosphorylated rapidly and stoichiometrically by mitogen-activated protein (MAP) kinase in vitro. Ser-25 was identified as the major site and Ser-38 as a minor site of phosphorylation, while the p42 and p44 isoforms of MAP kinase were the only significant stathmin kinases detected in PC12 cells after stimulation by nerve growth factor (NGF). The results suggest that MAP kinases are the enzymes responsible for increasing the level of phosphorylation of Ser-25, which has been observed previously in PC12 cells following stimulation by NGF.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Calcium-Calmodulin-Dependent Protein Kinases - metabolism</subject><subject>Kinetics</subject><subject>Microtubule Proteins</subject><subject>Molecular Sequence Data</subject><subject>Nerve Growth Factors - pharmacology</subject><subject>PC12 Cells</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - metabolism</subject><subject>Phosphopeptides - chemistry</subject><subject>Phosphopeptides - metabolism</subject><subject>Phosphoproteins - metabolism</subject><subject>Phosphorus Radioisotopes</subject><subject>Phosphorylation</subject><subject>Phosphoserine - analysis</subject><subject>Rats</subject><subject>Recombinant Proteins - metabolism</subject><subject>Serine</subject><subject>Signal Transduction</subject><subject>Stathmin</subject><issn>0300-8177</issn><issn>1573-4919</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo90D1PwzAQBmALgUopLOxImRiQAne92ueMpWoBqQiGMkdOYquBfJQ4GfrvMWphON3y3HvSK8Q1wj0C8EPmAIEVK3UixiiZ4lmCyakYAwHEGpnPxYX3nxAYII7EiBOSNOOxiDdbG-22rQ_T7SvTl20TtS7yvem3ddlE2T56nb9HX2VjvL0UZ85U3l4d90R8rJabxXO8fnt6WczXcU4z3cdOa83FlNGxVOGn0RlIkooLdFAAWUbF2mRT45xNpiSlCwCRcmNJOaSJuD3k7rr2e7C-T-vS57aqTGPbwaesCMIdB3h3gHnXet9Zl-66sjbdPkVIf7tJH1d_3QR8c0wdstoW__RYBv0ABKRcOg</recordid><startdate>199311</startdate><enddate>199311</enddate><creator>Leighton, I A</creator><creator>Curmi, P</creator><creator>Campbell, D G</creator><creator>Cohen, P</creator><creator>Sobel, A</creator><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>7X8</scope></search><sort><creationdate>199311</creationdate><title>The phosphorylation of stathmin by MAP kinase</title><author>Leighton, I A ; Curmi, P ; Campbell, D G ; Cohen, P ; Sobel, A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c348t-f8887d271f756010a8b053567d1f0d03e71678ab2affe92355fb05113cae36f13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Calcium-Calmodulin-Dependent Protein Kinases - metabolism</topic><topic>Kinetics</topic><topic>Microtubule Proteins</topic><topic>Molecular Sequence Data</topic><topic>Nerve Growth Factors - pharmacology</topic><topic>PC12 Cells</topic><topic>Peptide Fragments - chemistry</topic><topic>Peptide Fragments - metabolism</topic><topic>Phosphopeptides - chemistry</topic><topic>Phosphopeptides - metabolism</topic><topic>Phosphoproteins - metabolism</topic><topic>Phosphorus Radioisotopes</topic><topic>Phosphorylation</topic><topic>Phosphoserine - analysis</topic><topic>Rats</topic><topic>Recombinant Proteins - metabolism</topic><topic>Serine</topic><topic>Signal Transduction</topic><topic>Stathmin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Leighton, I A</creatorcontrib><creatorcontrib>Curmi, P</creatorcontrib><creatorcontrib>Campbell, D G</creatorcontrib><creatorcontrib>Cohen, P</creatorcontrib><creatorcontrib>Sobel, A</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular and cellular biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Leighton, I A</au><au>Curmi, P</au><au>Campbell, D G</au><au>Cohen, P</au><au>Sobel, A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The phosphorylation of stathmin by MAP kinase</atitle><jtitle>Molecular and cellular biochemistry</jtitle><addtitle>Mol Cell Biochem</addtitle><date>1993-11</date><risdate>1993</risdate><volume>127-128</volume><issue>1</issue><spage>151</spage><epage>156</epage><pages>151-156</pages><issn>0300-8177</issn><eissn>1573-4919</eissn><abstract>Stathmin, a ubiquitous cytosolic phosphoprotein which may play a role in integrating the effects of diverse signals regulating proliferation, differentiation and other cell functions, was found to be phosphorylated rapidly and stoichiometrically by mitogen-activated protein (MAP) kinase in vitro. Ser-25 was identified as the major site and Ser-38 as a minor site of phosphorylation, while the p42 and p44 isoforms of MAP kinase were the only significant stathmin kinases detected in PC12 cells after stimulation by nerve growth factor (NGF). The results suggest that MAP kinases are the enzymes responsible for increasing the level of phosphorylation of Ser-25, which has been observed previously in PC12 cells following stimulation by NGF.</abstract><cop>Netherlands</cop><pmid>7935347</pmid><doi>10.1007/bf01076766</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0300-8177 |
| ispartof | Molecular and cellular biochemistry, 1993-11, Vol.127-128 (1), p.151-156 |
| issn | 0300-8177 1573-4919 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76309237 |
| source | MEDLINE; Springer Nature - Complete Springer Journals |
| subjects | Amino Acid Sequence Animals Calcium-Calmodulin-Dependent Protein Kinases - metabolism Kinetics Microtubule Proteins Molecular Sequence Data Nerve Growth Factors - pharmacology PC12 Cells Peptide Fragments - chemistry Peptide Fragments - metabolism Phosphopeptides - chemistry Phosphopeptides - metabolism Phosphoproteins - metabolism Phosphorus Radioisotopes Phosphorylation Phosphoserine - analysis Rats Recombinant Proteins - metabolism Serine Signal Transduction Stathmin |
| title | The phosphorylation of stathmin by MAP kinase |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-10T00%3A29%3A00IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20phosphorylation%20of%20stathmin%20by%20MAP%20kinase&rft.jtitle=Molecular%20and%20cellular%20biochemistry&rft.au=Leighton,%20I%20A&rft.date=1993-11&rft.volume=127-128&rft.issue=1&rft.spage=151&rft.epage=156&rft.pages=151-156&rft.issn=0300-8177&rft.eissn=1573-4919&rft_id=info:doi/10.1007/bf01076766&rft_dat=%3Cproquest_cross%3E76309237%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=76309237&rft_id=info:pmid/7935347&rfr_iscdi=true |