Autophosphorylation of brain microtubule protein: Evidence for endogenous protein kinase/phosphoprotein phosphatase cycling and multiple phosphorylation of a microtubule associated protein
Brain microtubule protein, prepared by two types of recycling methods, undergoes “flash” phosphorylation in the presence of [γ- 32p]ATP through sequential action of protein kinase and phosphoprotein phosphatase present in microtubule protein. SDS electrophoretic analysis indicates that MAP 1, tau pr...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1980-01, Vol.92 (1), p.89-94 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Coughlin, Beth A. White, Hillary D. Purich, Daniel L. |
| description | Brain microtubule protein, prepared by two types of recycling methods, undergoes “flash” phosphorylation in the presence of [γ-
32p]ATP through sequential action of protein kinase and phosphoprotein phosphatase present in microtubule protein. SDS electrophoretic analysis indicates that MAP
1, tau protein, and tubulin are poorly phosphorylated, and MAP
2 is the major site of phosphorylation. To improve [
32P]phosphoprotein stability in the presence of the kinase/phosphatase cycle, 3′,5′-cyclicAMP, orthophosphate, or fluoride ion may be added. After separation from tubulin by phosphocellulose chromatography, the MAP fraction exhibits autophosphorylation. Finally, the maximal extent of autophosphorylation is observed with an ATP regenerating system using ADP, [
32P]acetyl-P, and bacterial acetate kinase; this results in the incorporation of 3–4 phosphoryl groups per MAP
2 subunit. |
| doi_str_mv | 10.1016/0006-291X(80)91523-5 |
| format | Article |
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32p]ATP through sequential action of protein kinase and phosphoprotein phosphatase present in microtubule protein. SDS electrophoretic analysis indicates that MAP
1, tau protein, and tubulin are poorly phosphorylated, and MAP
2 is the major site of phosphorylation. To improve [
32P]phosphoprotein stability in the presence of the kinase/phosphatase cycle, 3′,5′-cyclicAMP, orthophosphate, or fluoride ion may be added. After separation from tubulin by phosphocellulose chromatography, the MAP fraction exhibits autophosphorylation. Finally, the maximal extent of autophosphorylation is observed with an ATP regenerating system using ADP, [
32P]acetyl-P, and bacterial acetate kinase; this results in the incorporation of 3–4 phosphoryl groups per MAP
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32p]ATP through sequential action of protein kinase and phosphoprotein phosphatase present in microtubule protein. SDS electrophoretic analysis indicates that MAP
1, tau protein, and tubulin are poorly phosphorylated, and MAP
2 is the major site of phosphorylation. To improve [
32P]phosphoprotein stability in the presence of the kinase/phosphatase cycle, 3′,5′-cyclicAMP, orthophosphate, or fluoride ion may be added. After separation from tubulin by phosphocellulose chromatography, the MAP fraction exhibits autophosphorylation. Finally, the maximal extent of autophosphorylation is observed with an ATP regenerating system using ADP, [
32P]acetyl-P, and bacterial acetate kinase; this results in the incorporation of 3–4 phosphoryl groups per MAP
2 subunit.</description><subject>Animals</subject><subject>Brain - metabolism</subject><subject>Cattle</subject><subject>Kinetics</subject><subject>Microtubules - metabolism</subject><subject>Phosphoprotein Phosphatases - metabolism</subject><subject>Phosphorylation</subject><subject>Protein Kinases - metabolism</subject><subject>Tubulin - metabolism</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1980</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9UV1LHDEUDaLY9eMfWMiTtA_jJpOZ2YkPgsjaCoIvLfgWMsmNTTuTrElG2P_WH9eMuysUwYeQ3Jxzz7mXg9AZJReU0GZOCGmKktPHLy35ymldsqLeQzNKOClKSqp9NHujfEJHMf4mhNKq4YfosCkrxhmfob_XY_KrXz7mE9a9TNY77A3ugrQOD1YFn8Zu7AGv8gusu8TLF6vBKcDGBwxO-ydwfow7Av5jnYww34rufjelTBnCaq16656wdBoPY5_satJ_P4T8bwAZo1dWJtA7qxN0YGQf4XR7H6Oft8sfN9-L-4dvdzfX94Vi9SIVQNtG1bw2ZaNrbYiSirJWd4wxYAvOzYJU2kBHtVacttSwirUlqJJJaHIfO0bnG93s-zxCTGKwUUHfSwd5c7GoOK_bss3EakPMU8cYwIhVsIMMa0GJmEITUyJiSkS0RLyGJib9z1v9sRtAvzVtU8r41QaHvOSLhSCislME2gZQSWhvPzb4B9i7rlw</recordid><startdate>19800115</startdate><enddate>19800115</enddate><creator>Coughlin, Beth A.</creator><creator>White, Hillary D.</creator><creator>Purich, Daniel L.</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>7X8</scope></search><sort><creationdate>19800115</creationdate><title>Autophosphorylation of brain microtubule protein: Evidence for endogenous protein kinase/phosphoprotein phosphatase cycling and multiple phosphorylation of a microtubule associated protein</title><author>Coughlin, Beth A. ; White, Hillary D. ; Purich, Daniel L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357t-e186c595f26d5df0cac138db333e3799f704dfeb1ddc9181f34382ec23ae65953</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1980</creationdate><topic>Animals</topic><topic>Brain - metabolism</topic><topic>Cattle</topic><topic>Kinetics</topic><topic>Microtubules - metabolism</topic><topic>Phosphoprotein Phosphatases - metabolism</topic><topic>Phosphorylation</topic><topic>Protein Kinases - metabolism</topic><topic>Tubulin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Coughlin, Beth A.</creatorcontrib><creatorcontrib>White, Hillary D.</creatorcontrib><creatorcontrib>Purich, Daniel L.</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>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Coughlin, Beth A.</au><au>White, Hillary D.</au><au>Purich, Daniel L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Autophosphorylation of brain microtubule protein: Evidence for endogenous protein kinase/phosphoprotein phosphatase cycling and multiple phosphorylation of a microtubule associated protein</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1980-01-15</date><risdate>1980</risdate><volume>92</volume><issue>1</issue><spage>89</spage><epage>94</epage><pages>89-94</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Brain microtubule protein, prepared by two types of recycling methods, undergoes “flash” phosphorylation in the presence of [γ-
32p]ATP through sequential action of protein kinase and phosphoprotein phosphatase present in microtubule protein. SDS electrophoretic analysis indicates that MAP
1, tau protein, and tubulin are poorly phosphorylated, and MAP
2 is the major site of phosphorylation. To improve [
32P]phosphoprotein stability in the presence of the kinase/phosphatase cycle, 3′,5′-cyclicAMP, orthophosphate, or fluoride ion may be added. After separation from tubulin by phosphocellulose chromatography, the MAP fraction exhibits autophosphorylation. Finally, the maximal extent of autophosphorylation is observed with an ATP regenerating system using ADP, [
32P]acetyl-P, and bacterial acetate kinase; this results in the incorporation of 3–4 phosphoryl groups per MAP
2 subunit.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>6243939</pmid><doi>10.1016/0006-291X(80)91523-5</doi><tpages>6</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 1980-01, Vol.92 (1), p.89-94 |
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| language | eng |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Animals Brain - metabolism Cattle Kinetics Microtubules - metabolism Phosphoprotein Phosphatases - metabolism Phosphorylation Protein Kinases - metabolism Tubulin - metabolism |
| title | Autophosphorylation of brain microtubule protein: Evidence for endogenous protein kinase/phosphoprotein phosphatase cycling and multiple phosphorylation of a microtubule associated protein |
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