Phosphorylation at Ser²⁶ in the ATP-binding site of Ca²⁺/calmodulin-dependent kinase II as a mechanism for switching off the kinase activity
CaMKII (Ca²⁺/calmodulin-dependent kinase II) is a serine/threonine phosphotransferase that is capable of long-term retention of activity due to autophosphorylation at a specific threonine residue within each subunit of its oligomeric structure. The γ isoform of CaMKII is a significant regulator of v...
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Published in | Bioscience reports Vol. 33; no. 2 |
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Main Authors | , , , , |
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Language | English |
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07.02.2013
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Abstract | CaMKII (Ca²⁺/calmodulin-dependent kinase II) is a serine/threonine phosphotransferase that is capable of long-term retention of activity due to autophosphorylation at a specific threonine residue within each subunit of its oligomeric structure. The γ isoform of CaMKII is a significant regulator of vascular contractility. Here, we show that phosphorylation of CaMKII γ at Ser²⁶, a residue located within the ATP-binding site, terminates the sustained activity of the enzyme. To test the physiological importance of phosphorylation at Ser²⁶, we generated a phosphospecific Ser²⁶ antibody and demonstrated an increase in Ser²⁶ phosphorylation upon depolarization and contraction of blood vessels. To determine if the phosphorylation of Ser²⁶ affects the kinase activity, we mutated Ser²⁶ to alanine or aspartic acid. The S26D mutation mimicking the phosphorylated state of CaMKII causes a dramatic decrease in Thr²⁸⁷ autophosphorylation levels and greatly reduces the catalytic activity towards an exogenous substrate (autocamtide-3), whereas the S26A mutation has no effect. These data combined with molecular modelling indicate that a negative charge at Ser²⁶ of CaMKII γ inhibits the catalytic activity of the enzyme towards its autophosphorylation site at Thr²⁸⁷ most probably by blocking ATP binding. We propose that Ser²⁶ phosphorylation constitutes an important mechanism for switching off CaMKII activity. |
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AbstractList | CaMKII (Ca2+/calmodulin-dependent kinase II) is a serine/threonine phosphotransferase that is capable of long-term retention of activity due to autophosphorylation at a specific threonine residue within each subunit of its oligomeric structure. The γ isoform of CaMKII is a significant regulator of vascular contractility. Here, we show that phosphorylation of CaMKII γ at Ser26, a residue located within the ATP-binding site, terminates the sustained activity of the enzyme. To test the physiological importance of phosphorylation at Ser26, we generated a phosphospecific Ser26 antibody and demonstrated an increase in Ser26 phosphorylation upon depolarization and contraction of blood vessels. To determine if the phosphorylation of Ser26 affects the kinase activity, we mutated Ser26 to alanine or aspartic acid. The S26D mutation mimicking the phosphorylated state of CaMKII causes a dramatic decrease in Thr287 autophosphorylation levels and greatly reduces the catalytic activity towards an exogenous substrate (autocamtide-3), whereas the S26A mutation has no effect. These data combined with molecular modelling indicate that a negative charge at Ser26 of CaMKII γ inhibits the catalytic activity of the enzyme towards its autophosphorylation site at Thr287 most probably by blocking ATP binding. We propose that Ser26 phosphorylation constitutes an important mechanism for switching off CaMKII activity. CaMKII (Ca²⁺/calmodulin-dependent kinase II) is a serine/threonine phosphotransferase that is capable of long-term retention of activity due to autophosphorylation at a specific threonine residue within each subunit of its oligomeric structure. The γ isoform of CaMKII is a significant regulator of vascular contractility. Here, we show that phosphorylation of CaMKII γ at Ser²⁶, a residue located within the ATP-binding site, terminates the sustained activity of the enzyme. To test the physiological importance of phosphorylation at Ser²⁶, we generated a phosphospecific Ser²⁶ antibody and demonstrated an increase in Ser²⁶ phosphorylation upon depolarization and contraction of blood vessels. To determine if the phosphorylation of Ser²⁶ affects the kinase activity, we mutated Ser²⁶ to alanine or aspartic acid. The S26D mutation mimicking the phosphorylated state of CaMKII causes a dramatic decrease in Thr²⁸⁷ autophosphorylation levels and greatly reduces the catalytic activity towards an exogenous substrate (autocamtide-3), whereas the S26A mutation has no effect. These data combined with molecular modelling indicate that a negative charge at Ser²⁶ of CaMKII γ inhibits the catalytic activity of the enzyme towards its autophosphorylation site at Thr²⁸⁷ most probably by blocking ATP binding. We propose that Ser²⁶ phosphorylation constitutes an important mechanism for switching off CaMKII activity. CaMKII (Ca 2+ /calmodulin-dependent kinase II) is a serine/threonine phosphotransferase that is capable of long-term retention of activity due to autophosphorylation at a specific threonine residue within each subunit of its oligomeric structure. The γ isoform of CaMKII is a significant regulator of vascular contractility. Here, we show that phosphorylation of CaMKII γ at Ser 26 , a residue located within the ATP-binding site, terminates the sustained activity of the enzyme. To test the physiological importance of phosphorylation at Ser 26 , we generated a phosphospecific Ser 26 antibody and demonstrated an increase in Ser 26 phosphorylation upon depolarization and contraction of blood vessels. To determine if the phosphorylation of Ser 26 affects the kinase activity, we mutated Ser 26 to alanine or aspartic acid. The S26D mutation mimicking the phosphorylated state of CaMKII causes a dramatic decrease in Thr 287 autophosphorylation levels and greatly reduces the catalytic activity towards an exogenous substrate (autocamtide-3), whereas the S26A mutation has no effect. These data combined with molecular modelling indicate that a negative charge at Ser 26 of CaMKII γ inhibits the catalytic activity of the enzyme towards its autophosphorylation site at Thr 287 most probably by blocking ATP binding. We propose that Ser 26 phosphorylation constitutes an important mechanism for switching off CaMKII activity. |
Author | Leavis, Paul Yilmaz, Mehtap Gangopadhyay, Samudra S Grabarek, Zenon Morgan, Kathleen G |
Author_xml | – sequence: 1 givenname: Mehtap surname: Yilmaz fullname: Yilmaz, Mehtap organization: Department of Health Sciences, Boston University, 635 Commonwealth Avenue, Boston, MA 02215, U.S.A – sequence: 2 givenname: Samudra S surname: Gangopadhyay fullname: Gangopadhyay, Samudra S – sequence: 3 givenname: Paul surname: Leavis fullname: Leavis, Paul organization: §Boston Biomedical Research Institute, 64 Grove Street, Watertown, MA 02472, U.S.A – sequence: 4 givenname: Zenon surname: Grabarek fullname: Grabarek, Zenon organization: §Boston Biomedical Research Institute, 64 Grove Street, Watertown, MA 02472, U.S.A – sequence: 5 givenname: Kathleen G surname: Morgan fullname: Morgan, Kathleen G organization: Department of Health Sciences, Boston University, 635 Commonwealth Avenue, Boston, MA 02215, U.S.A |
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CitedBy_id | crossref_primary_10_1021_acs_jmedchem_9b01779 crossref_primary_10_1124_pr_115_010652 crossref_primary_10_1371_journal_pbio_3001813 crossref_primary_10_3892_mmr_2019_10309 crossref_primary_10_1002_marc_202200195 |
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Snippet | CaMKII (Ca²⁺/calmodulin-dependent kinase II) is a serine/threonine phosphotransferase that is capable of long-term retention of activity due to... CaMKII (Ca2+/calmodulin-dependent kinase II) is a serine/threonine phosphotransferase that is capable of long-term retention of activity due to... CaMKII (Ca 2+ /calmodulin-dependent kinase II) is a serine/threonine phosphotransferase that is capable of long-term retention of activity due to... |
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SubjectTerms | Adenosine Triphosphate - metabolism Animals Binding Sites Calcium - metabolism Calcium-Calmodulin-Dependent Protein Kinase Type 2 - genetics Calcium-Calmodulin-Dependent Protein Kinase Type 2 - metabolism Calmodulin - genetics Calmodulin - metabolism Ferrets - genetics Ferrets - metabolism Mutation Original Paper Phosphorylation - genetics Protein Isoforms - genetics Protein Isoforms - metabolism Serine - genetics Serine - metabolism Signal Transduction Threonine - genetics Threonine - metabolism |
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Title | Phosphorylation at Ser²⁶ in the ATP-binding site of Ca²⁺/calmodulin-dependent kinase II as a mechanism for switching off the kinase activity |
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