Protein kinase C-dependent dephosphorylation of tyrosine hydroxylase requires the B56δ heterotrimeric form of protein phosphatase 2A
Tyrosine hydroxylase, which plays a critical role in regulation of dopamine synthesis, is known to be controlled by phosphorylation at several critical sites. One of these sites, Ser40, is phosphorylated by a number of protein kinases, including protein kinase A. The major protein phosphatase that d...
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| description | Tyrosine hydroxylase, which plays a critical role in regulation of dopamine synthesis, is known to be controlled by phosphorylation at several critical sites. One of these sites, Ser40, is phosphorylated by a number of protein kinases, including protein kinase A. The major protein phosphatase that dephosphorylates Ser40 is protein phosphatase-2A (PP2A). A recent study has also linked protein kinase C to the dephosphorylation of Ser40 [1], but the mechanism is unclear. PP2A isoforms are comprised of catalytic, scaffold, and regulatory subunits, the regulatory B subunits being able to influence cellular localization and substrate selection. In the current study, we find that protein kinase C is able to phosphorylate a key regulatory site in the B56δ subunit leading to activation of PP2A. In turn, activation of the B56δ-containing heterotrimeric form of PP2A is responsible for enhanced dephosphorylation of Ser40 of tyrosine hydroylase in response to stimulation of PKC. In support of this mechanism, down-regulation of B56δ expression in N27 cells using RNAi was found to increase dopamine synthesis. Together these studies reveal molecular details of how protein kinase C is linked to reduced tyrosine hydroxylase activity via control of PP2A, and also add to the complexity of protein kinase/protein phosphatase interactions. |
| doi_str_mv | 10.1371/journal.pone.0026292 |
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One of these sites, Ser40, is phosphorylated by a number of protein kinases, including protein kinase A. The major protein phosphatase that dephosphorylates Ser40 is protein phosphatase-2A (PP2A). A recent study has also linked protein kinase C to the dephosphorylation of Ser40 [1], but the mechanism is unclear. PP2A isoforms are comprised of catalytic, scaffold, and regulatory subunits, the regulatory B subunits being able to influence cellular localization and substrate selection. In the current study, we find that protein kinase C is able to phosphorylate a key regulatory site in the B56δ subunit leading to activation of PP2A. In turn, activation of the B56δ-containing heterotrimeric form of PP2A is responsible for enhanced dephosphorylation of Ser40 of tyrosine hydroylase in response to stimulation of PKC. In support of this mechanism, down-regulation of B56δ expression in N27 cells using RNAi was found to increase dopamine synthesis. Together these studies reveal molecular details of how protein kinase C is linked to reduced tyrosine hydroxylase activity via control of PP2A, and also add to the complexity of protein kinase/protein phosphatase interactions.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0026292</identifier><identifier>PMID: 22046270</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Activation ; Animals ; Biochemistry ; Biology ; Catalysis ; Cell Line ; Chemical synthesis ; Control ; Dephosphorylation ; Dopamine ; Dopamine - biosynthesis ; Enzymes ; Hydroxylase ; Immunoglobulins ; Isoforms ; Kinases ; Laboratories ; Localization ; Medical research ; Medicine ; Mice ; Neurosciences ; Penicillin ; Phosphatase ; Phosphoprotein phosphatase ; Phosphorylation ; Protein kinase A ; Protein kinase C ; Protein Kinase C - metabolism ; Protein phosphatase ; Protein Phosphatase 2 - chemistry ; Protein Phosphatase 2 - metabolism ; Protein Subunits ; Protein-tyrosine-phosphatase ; Proteins ; Regulation ; Regulatory subunits ; RNA-mediated interference ; Rodents ; Studies ; Tyrosine ; Tyrosine 3-monooxygenase ; Tyrosine 3-Monooxygenase - metabolism</subject><ispartof>PloS one, 2011-10, Vol.6 (10), p.e26292-e26292</ispartof><rights>2011 Ahn et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>Ahn et al. 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c525t-240a2324811dd140087522d368e518e38e62948e8f3a56e85a11e1638a3156133</citedby><cites>FETCH-LOGICAL-c525t-240a2324811dd140087522d368e518e38e62948e8f3a56e85a11e1638a3156133</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3198769/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3198769/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2102,2928,23866,27924,27925,53791,53793,79600,79601</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22046270$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Gasset, Maria</contributor><creatorcontrib>Ahn, Jung-Hyuck</creatorcontrib><creatorcontrib>Kim, Yong</creatorcontrib><creatorcontrib>Kim, Hee-Sun</creatorcontrib><creatorcontrib>Greengard, Paul</creatorcontrib><creatorcontrib>Nairn, Angus C</creatorcontrib><title>Protein kinase C-dependent dephosphorylation of tyrosine hydroxylase requires the B56δ heterotrimeric form of protein phosphatase 2A</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Tyrosine hydroxylase, which plays a critical role in regulation of dopamine synthesis, is known to be controlled by phosphorylation at several critical sites. One of these sites, Ser40, is phosphorylated by a number of protein kinases, including protein kinase A. The major protein phosphatase that dephosphorylates Ser40 is protein phosphatase-2A (PP2A). A recent study has also linked protein kinase C to the dephosphorylation of Ser40 [1], but the mechanism is unclear. PP2A isoforms are comprised of catalytic, scaffold, and regulatory subunits, the regulatory B subunits being able to influence cellular localization and substrate selection. In the current study, we find that protein kinase C is able to phosphorylate a key regulatory site in the B56δ subunit leading to activation of PP2A. In turn, activation of the B56δ-containing heterotrimeric form of PP2A is responsible for enhanced dephosphorylation of Ser40 of tyrosine hydroylase in response to stimulation of PKC. In support of this mechanism, down-regulation of B56δ expression in N27 cells using RNAi was found to increase dopamine synthesis. Together these studies reveal molecular details of how protein kinase C is linked to reduced tyrosine hydroxylase activity via control of PP2A, and also add to the complexity of protein kinase/protein phosphatase interactions.</description><subject>Activation</subject><subject>Animals</subject><subject>Biochemistry</subject><subject>Biology</subject><subject>Catalysis</subject><subject>Cell Line</subject><subject>Chemical synthesis</subject><subject>Control</subject><subject>Dephosphorylation</subject><subject>Dopamine</subject><subject>Dopamine - biosynthesis</subject><subject>Enzymes</subject><subject>Hydroxylase</subject><subject>Immunoglobulins</subject><subject>Isoforms</subject><subject>Kinases</subject><subject>Laboratories</subject><subject>Localization</subject><subject>Medical research</subject><subject>Medicine</subject><subject>Mice</subject><subject>Neurosciences</subject><subject>Penicillin</subject><subject>Phosphatase</subject><subject>Phosphoprotein phosphatase</subject><subject>Phosphorylation</subject><subject>Protein kinase A</subject><subject>Protein kinase C</subject><subject>Protein Kinase C - metabolism</subject><subject>Protein phosphatase</subject><subject>Protein Phosphatase 2 - chemistry</subject><subject>Protein Phosphatase 2 - metabolism</subject><subject>Protein Subunits</subject><subject>Protein-tyrosine-phosphatase</subject><subject>Proteins</subject><subject>Regulation</subject><subject>Regulatory subunits</subject><subject>RNA-mediated interference</subject><subject>Rodents</subject><subject>Studies</subject><subject>Tyrosine</subject><subject>Tyrosine 3-monooxygenase</subject><subject>Tyrosine 3-Monooxygenase - metabolism</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>DOA</sourceid><recordid>eNptUstu1DAUtRCIloE_QGCJBasMfsSOs0EqIx6VKsEC1paT3DQeMnZqOxXzAfwR38E34WHSqkUsrn3le865D1-EnlOypryib7Z-Ds6M68k7WBPCJKvZA3RKa84KyQh_eMc_QU9i3BIiuJLyMTphjJSSVeQU_fwSfALr8HfrTAS8KTqYwHXgEs7e4GO2sB9Nst5h3-O0Dz5aB3jYd8H_yJHMCnA12wARpwHwOyF__8IDJMjSwe4g2Bb3PuwO9GlJd1Q26cBmZ0_Ro96MEZ4t9wp9-_D-6-ZTcfH54_nm7KJoBROpYCUxjLNSUdp1tCREVYKxjksFgirgCvIQSgWq50ZIUMJQClRyZTgVknK-Qi-PutPoo14mGDXllLBs-Vih8yOi82arp1y-CXvtjdV_H3y41CYk246gm4zvK9H0XPGSqaYmpJElL0kvhDLykO3tkm1udtC1eabBjPdE70ecHfSlv9ac1qqSdRZ4vQgEfzVDTHpnYwvjaBz4OeqaMKKUECQjX_2D_H9z5RHV5j-MAfrbWijRh6W6YenDUullqTLtxd0-bkk3W8T_AF2yy4M</recordid><startdate>20111021</startdate><enddate>20111021</enddate><creator>Ahn, Jung-Hyuck</creator><creator>Kim, Yong</creator><creator>Kim, Hee-Sun</creator><creator>Greengard, Paul</creator><creator>Nairn, Angus C</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</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>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20111021</creationdate><title>Protein kinase C-dependent dephosphorylation of tyrosine hydroxylase requires the B56δ heterotrimeric form of protein phosphatase 2A</title><author>Ahn, Jung-Hyuck ; Kim, Yong ; Kim, Hee-Sun ; Greengard, Paul ; Nairn, Angus C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c525t-240a2324811dd140087522d368e518e38e62948e8f3a56e85a11e1638a3156133</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Activation</topic><topic>Animals</topic><topic>Biochemistry</topic><topic>Biology</topic><topic>Catalysis</topic><topic>Cell Line</topic><topic>Chemical synthesis</topic><topic>Control</topic><topic>Dephosphorylation</topic><topic>Dopamine</topic><topic>Dopamine - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ahn, Jung-Hyuck</au><au>Kim, Yong</au><au>Kim, Hee-Sun</au><au>Greengard, Paul</au><au>Nairn, Angus C</au><au>Gasset, Maria</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Protein kinase C-dependent dephosphorylation of tyrosine hydroxylase requires the B56δ heterotrimeric form of protein phosphatase 2A</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2011-10-21</date><risdate>2011</risdate><volume>6</volume><issue>10</issue><spage>e26292</spage><epage>e26292</epage><pages>e26292-e26292</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Tyrosine hydroxylase, which plays a critical role in regulation of dopamine synthesis, is known to be controlled by phosphorylation at several critical sites. One of these sites, Ser40, is phosphorylated by a number of protein kinases, including protein kinase A. The major protein phosphatase that dephosphorylates Ser40 is protein phosphatase-2A (PP2A). A recent study has also linked protein kinase C to the dephosphorylation of Ser40 [1], but the mechanism is unclear. PP2A isoforms are comprised of catalytic, scaffold, and regulatory subunits, the regulatory B subunits being able to influence cellular localization and substrate selection. In the current study, we find that protein kinase C is able to phosphorylate a key regulatory site in the B56δ subunit leading to activation of PP2A. In turn, activation of the B56δ-containing heterotrimeric form of PP2A is responsible for enhanced dephosphorylation of Ser40 of tyrosine hydroylase in response to stimulation of PKC. In support of this mechanism, down-regulation of B56δ expression in N27 cells using RNAi was found to increase dopamine synthesis. Together these studies reveal molecular details of how protein kinase C is linked to reduced tyrosine hydroxylase activity via control of PP2A, and also add to the complexity of protein kinase/protein phosphatase interactions.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>22046270</pmid><doi>10.1371/journal.pone.0026292</doi><oa>free_for_read</oa></addata></record> |
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| subjects | Activation Animals Biochemistry Biology Catalysis Cell Line Chemical synthesis Control Dephosphorylation Dopamine Dopamine - biosynthesis Enzymes Hydroxylase Immunoglobulins Isoforms Kinases Laboratories Localization Medical research Medicine Mice Neurosciences Penicillin Phosphatase Phosphoprotein phosphatase Phosphorylation Protein kinase A Protein kinase C Protein Kinase C - metabolism Protein phosphatase Protein Phosphatase 2 - chemistry Protein Phosphatase 2 - metabolism Protein Subunits Protein-tyrosine-phosphatase Proteins Regulation Regulatory subunits RNA-mediated interference Rodents Studies Tyrosine Tyrosine 3-monooxygenase Tyrosine 3-Monooxygenase - metabolism |
| title | Protein kinase C-dependent dephosphorylation of tyrosine hydroxylase requires the B56δ heterotrimeric form of protein phosphatase 2A |
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