Nogo-B is a new physiological substrate for MAPKAP-K2
The neurite outgrowth inhibitor protein Nogo is one of 300 proteins that contain a reticulon homology domain, which is responsible for their association with the endoplasmic reticulum. Here we have found that the Nogo-B spliceform becomes phosphorylated at Ser107 in response to lipopolysaccharide in...
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| Veröffentlicht in: | Biochemical journal 2005-10, Vol.391 (Pt 2), p.433-440 |
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| container_title | Biochemical journal |
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| creator | Rousseau, Simon Peggie, Mark Campbell, David G Nebreda, Angel R Cohen, Philip |
| description | The neurite outgrowth inhibitor protein Nogo is one of 300 proteins that contain a reticulon homology domain, which is responsible for their association with the endoplasmic reticulum. Here we have found that the Nogo-B spliceform becomes phosphorylated at Ser107 in response to lipopolysaccharide in RAW264 macrophages or anisomycin in HeLa cells. The phosphorylation is prevented by SB 203580, an inhibitor of SAPK2a (stress-activated protein kinase 2a)/p38a and SAPK2b/p38b, and does not occur in embryonic fibroblasts generated from SAPK2a/p38a-deficient mice. Nogo-B is phosphorylated at Ser107 in vitro by MAPKAP-K2 [MAPK (mitogen-activated protein kinase)-activated protein kinase-2] or MAPKAP-K3, but not by other protein kinases that are known to be activated by SAPK2a/p38a. The anisomycin-induced phosphorylation of Ser107 in HeLa cells can be prevented by 'knockdown' of MAPKAP-K2 using siRNA (small interfering RNA). Taken together, our results identify Nogo-B as a new physiological substrate of MAPKAP-K2. |
| doi_str_mv | 10.1042/BJ20050935 |
| format | Article |
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Here we have found that the Nogo-B spliceform becomes phosphorylated at Ser107 in response to lipopolysaccharide in RAW264 macrophages or anisomycin in HeLa cells. The phosphorylation is prevented by SB 203580, an inhibitor of SAPK2a (stress-activated protein kinase 2a)/p38a and SAPK2b/p38b, and does not occur in embryonic fibroblasts generated from SAPK2a/p38a-deficient mice. Nogo-B is phosphorylated at Ser107 in vitro by MAPKAP-K2 [MAPK (mitogen-activated protein kinase)-activated protein kinase-2] or MAPKAP-K3, but not by other protein kinases that are known to be activated by SAPK2a/p38a. The anisomycin-induced phosphorylation of Ser107 in HeLa cells can be prevented by 'knockdown' of MAPKAP-K2 using siRNA (small interfering RNA). 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Here we have found that the Nogo-B spliceform becomes phosphorylated at Ser107 in response to lipopolysaccharide in RAW264 macrophages or anisomycin in HeLa cells. The phosphorylation is prevented by SB 203580, an inhibitor of SAPK2a (stress-activated protein kinase 2a)/p38a and SAPK2b/p38b, and does not occur in embryonic fibroblasts generated from SAPK2a/p38a-deficient mice. Nogo-B is phosphorylated at Ser107 in vitro by MAPKAP-K2 [MAPK (mitogen-activated protein kinase)-activated protein kinase-2] or MAPKAP-K3, but not by other protein kinases that are known to be activated by SAPK2a/p38a. The anisomycin-induced phosphorylation of Ser107 in HeLa cells can be prevented by 'knockdown' of MAPKAP-K2 using siRNA (small interfering RNA). Taken together, our results identify Nogo-B as a new physiological substrate of MAPKAP-K2.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antibodies, Phospho-Specific - immunology</subject><subject>Cell Line</subject><subject>Humans</subject><subject>Intracellular Signaling Peptides and Proteins</subject><subject>Lipopolysaccharides - pharmacology</subject><subject>Mice</subject><subject>Microtubules - metabolism</subject><subject>Mitogen-Activated Protein Kinase 11 - metabolism</subject><subject>Mitogen-Activated Protein Kinase 14 - metabolism</subject><subject>Molecular Weight</subject><subject>Myelin Proteins - chemistry</subject><subject>Myelin Proteins - immunology</subject><subject>Myelin Proteins - isolation & purification</subject><subject>Myelin Proteins - metabolism</subject><subject>Nogo Proteins</subject><subject>Phosphorylation</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>RNA Interference</subject><subject>Substrate Specificity</subject><issn>0264-6021</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkDtPwzAUhS0EoqWw8ANQJgakwHXs-LEgtRXPFugAs-U4dhuUxiVOQP33BLWiMN3hfvrO0UHoFMMlBppcjR4TgBQkSfdQH1MOseCJ2Ed9SBiNGSS4h45CeAfAFCgcoh5mIFNKZB-lz37u41FUhEhHlf2KVot1KHzp54XRZRTaLDS1bmzkfB09DWeT4SyeJMfowOky2JPtHaC325vX8X08fbl7GA-nsSGcNTGHlGGrM42ZMblmArNcOilIJqXVzlohNWDGnMsFhYRYbKTAWSqcBM0NkAG63nhXbba0ubFVV6ZUq7pY6nqtvC7U_09VLNTcfyqccCYp6QTnW0HtP1obGrUsgrFlqSvr26CYYBw4TzvwYgOa2odQW_cbgkH9rKx2K3fw2d9aO3Q7K_kG-iF2XA</recordid><startdate>20051015</startdate><enddate>20051015</enddate><creator>Rousseau, Simon</creator><creator>Peggie, Mark</creator><creator>Campbell, David G</creator><creator>Nebreda, Angel R</creator><creator>Cohen, Philip</creator><general>Portland Press Ltd</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>7X8</scope><scope>5PM</scope></search><sort><creationdate>20051015</creationdate><title>Nogo-B is a new physiological substrate for MAPKAP-K2</title><author>Rousseau, Simon ; Peggie, Mark ; Campbell, David G ; Nebreda, Angel R ; Cohen, Philip</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c376t-70561eaba16ccda6816d9f983b99eafee89a0166ffd84023e1c981b58f90a7c03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antibodies, Phospho-Specific - immunology</topic><topic>Cell Line</topic><topic>Humans</topic><topic>Intracellular Signaling Peptides and Proteins</topic><topic>Lipopolysaccharides - pharmacology</topic><topic>Mice</topic><topic>Microtubules - metabolism</topic><topic>Mitogen-Activated Protein Kinase 11 - metabolism</topic><topic>Mitogen-Activated Protein Kinase 14 - metabolism</topic><topic>Molecular Weight</topic><topic>Myelin Proteins - chemistry</topic><topic>Myelin Proteins - immunology</topic><topic>Myelin Proteins - isolation & purification</topic><topic>Myelin Proteins - metabolism</topic><topic>Nogo Proteins</topic><topic>Phosphorylation</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>RNA Interference</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rousseau, Simon</creatorcontrib><creatorcontrib>Peggie, Mark</creatorcontrib><creatorcontrib>Campbell, David G</creatorcontrib><creatorcontrib>Nebreda, Angel R</creatorcontrib><creatorcontrib>Cohen, Philip</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochemical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rousseau, Simon</au><au>Peggie, Mark</au><au>Campbell, David G</au><au>Nebreda, Angel R</au><au>Cohen, Philip</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Nogo-B is a new physiological substrate for MAPKAP-K2</atitle><jtitle>Biochemical journal</jtitle><addtitle>Biochem J</addtitle><date>2005-10-15</date><risdate>2005</risdate><volume>391</volume><issue>Pt 2</issue><spage>433</spage><epage>440</epage><pages>433-440</pages><issn>0264-6021</issn><eissn>1470-8728</eissn><abstract>The neurite outgrowth inhibitor protein Nogo is one of 300 proteins that contain a reticulon homology domain, which is responsible for their association with the endoplasmic reticulum. Here we have found that the Nogo-B spliceform becomes phosphorylated at Ser107 in response to lipopolysaccharide in RAW264 macrophages or anisomycin in HeLa cells. The phosphorylation is prevented by SB 203580, an inhibitor of SAPK2a (stress-activated protein kinase 2a)/p38a and SAPK2b/p38b, and does not occur in embryonic fibroblasts generated from SAPK2a/p38a-deficient mice. Nogo-B is phosphorylated at Ser107 in vitro by MAPKAP-K2 [MAPK (mitogen-activated protein kinase)-activated protein kinase-2] or MAPKAP-K3, but not by other protein kinases that are known to be activated by SAPK2a/p38a. The anisomycin-induced phosphorylation of Ser107 in HeLa cells can be prevented by 'knockdown' of MAPKAP-K2 using siRNA (small interfering RNA). Taken together, our results identify Nogo-B as a new physiological substrate of MAPKAP-K2.</abstract><cop>England</cop><pub>Portland Press Ltd</pub><pmid>16095439</pmid><doi>10.1042/BJ20050935</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Animals Antibodies, Phospho-Specific - immunology Cell Line Humans Intracellular Signaling Peptides and Proteins Lipopolysaccharides - pharmacology Mice Microtubules - metabolism Mitogen-Activated Protein Kinase 11 - metabolism Mitogen-Activated Protein Kinase 14 - metabolism Molecular Weight Myelin Proteins - chemistry Myelin Proteins - immunology Myelin Proteins - isolation & purification Myelin Proteins - metabolism Nogo Proteins Phosphorylation Protein-Serine-Threonine Kinases - metabolism RNA Interference Substrate Specificity |
| title | Nogo-B is a new physiological substrate for MAPKAP-K2 |
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