A protein kinase A-dependent molecular switch in synapsins regulates neurite outgrowth
Cyclic AMP (cAMP) promotes neurite outgrowth in a variety of neuronal cell lines through the activation of protein kinase A (PKA). We show here, using both Xenopus laevis embryonic neuronal culture and intact X. laevis embryos, that the nerve growth–promoting action of cAMP/PKA is mediated in part b...
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| Veröffentlicht in: | Nature neuroscience 2002-05, Vol.5 (5), p.431-437 |
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| container_title | Nature neuroscience |
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| creator | Kao, Hung-Teh Song, Hong-jun Porton, Barbara Ming, Guo-li Hoh, Josephine Abraham, Michael Czernik, Andrew J Pieribone, Vincent A Poo, Mu-ming Greengard, Paul |
| description | Cyclic AMP (cAMP) promotes neurite outgrowth in a variety of neuronal cell lines through the activation of protein kinase A (PKA). We show here, using both
Xenopus laevis
embryonic neuronal culture and intact
X. laevis
embryos, that the nerve growth–promoting action of cAMP/PKA is mediated in part by the phosphorylation of synapsins at a single amino acid residue. Expression of a mutated form of synapsin that prevents phosphorylation at this site, or introduction of phospho-specific antibodies directed against this site, decreased basal and dibutyryl cAMP–stimulated neurite outgrowth. Expression of a mutation mimicking constitutive phosphorylation at this site increased neurite outgrowth, both under basal conditions and in the presence of a PKA inhibitor. These results provide a potential molecular approach for stimulating neuron regeneration, after injury and in neurodegenerative diseases. |
| doi_str_mv | 10.1038/nn840 |
| format | Article |
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Xenopus laevis
embryonic neuronal culture and intact
X. laevis
embryos, that the nerve growth–promoting action of cAMP/PKA is mediated in part by the phosphorylation of synapsins at a single amino acid residue. Expression of a mutated form of synapsin that prevents phosphorylation at this site, or introduction of phospho-specific antibodies directed against this site, decreased basal and dibutyryl cAMP–stimulated neurite outgrowth. Expression of a mutation mimicking constitutive phosphorylation at this site increased neurite outgrowth, both under basal conditions and in the presence of a PKA inhibitor. These results provide a potential molecular approach for stimulating neuron regeneration, after injury and in neurodegenerative diseases.</description><identifier>ISSN: 1097-6256</identifier><identifier>EISSN: 1546-1726</identifier><identifier>DOI: 10.1038/nn840</identifier><identifier>PMID: 11976703</identifier><identifier>CODEN: NANEFN</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>Animal Genetics and Genomics ; Animals ; Antibodies - pharmacology ; Behavioral Sciences ; Biological Techniques ; Biomedical and Life Sciences ; Biomedicine ; Bucladesine - pharmacology ; Cells, Cultured ; Conserved Sequence ; Cyclic AMP-Dependent Protein Kinases - antagonists & inhibitors ; Cyclic AMP-Dependent Protein Kinases - metabolism ; Embryo, Nonmammalian ; Enzyme Activators - pharmacology ; Enzyme Inhibitors - pharmacology ; Genes, Reporter ; Microinjections ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Neurites - drug effects ; Neurites - metabolism ; Neurobiology ; Neurons ; Neurons - cytology ; Neurons - drug effects ; Neurons - metabolism ; Neurosciences ; Phosphorylation - drug effects ; Physiological aspects ; Protein kinases ; RNA, Messenger - pharmacology ; Sequence Homology, Amino Acid ; Synapsins - antagonists & inhibitors ; Synapsins - genetics ; Synapsins - metabolism ; Xenopus laevis</subject><ispartof>Nature neuroscience, 2002-05, Vol.5 (5), p.431-437</ispartof><rights>Springer Nature America, Inc. 2002</rights><rights>COPYRIGHT 2002 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group May 2002</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c487t-bf05d0cace9c47128921939cf12b5e1324620bafaaeb8259d05f10451c58c5693</citedby><cites>FETCH-LOGICAL-c487t-bf05d0cace9c47128921939cf12b5e1324620bafaaeb8259d05f10451c58c5693</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,781,785,2728,27926,27927</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11976703$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kao, Hung-Teh</creatorcontrib><creatorcontrib>Song, Hong-jun</creatorcontrib><creatorcontrib>Porton, Barbara</creatorcontrib><creatorcontrib>Ming, Guo-li</creatorcontrib><creatorcontrib>Hoh, Josephine</creatorcontrib><creatorcontrib>Abraham, Michael</creatorcontrib><creatorcontrib>Czernik, Andrew J</creatorcontrib><creatorcontrib>Pieribone, Vincent A</creatorcontrib><creatorcontrib>Poo, Mu-ming</creatorcontrib><creatorcontrib>Greengard, Paul</creatorcontrib><title>A protein kinase A-dependent molecular switch in synapsins regulates neurite outgrowth</title><title>Nature neuroscience</title><addtitle>Nat Neurosci</addtitle><addtitle>Nat Neurosci</addtitle><description>Cyclic AMP (cAMP) promotes neurite outgrowth in a variety of neuronal cell lines through the activation of protein kinase A (PKA). We show here, using both
Xenopus laevis
embryonic neuronal culture and intact
X. laevis
embryos, that the nerve growth–promoting action of cAMP/PKA is mediated in part by the phosphorylation of synapsins at a single amino acid residue. Expression of a mutated form of synapsin that prevents phosphorylation at this site, or introduction of phospho-specific antibodies directed against this site, decreased basal and dibutyryl cAMP–stimulated neurite outgrowth. Expression of a mutation mimicking constitutive phosphorylation at this site increased neurite outgrowth, both under basal conditions and in the presence of a PKA inhibitor. These results provide a potential molecular approach for stimulating neuron regeneration, after injury and in neurodegenerative diseases.</description><subject>Animal Genetics and Genomics</subject><subject>Animals</subject><subject>Antibodies - pharmacology</subject><subject>Behavioral Sciences</subject><subject>Biological Techniques</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Bucladesine - pharmacology</subject><subject>Cells, Cultured</subject><subject>Conserved Sequence</subject><subject>Cyclic AMP-Dependent Protein Kinases - antagonists & inhibitors</subject><subject>Cyclic AMP-Dependent Protein Kinases - metabolism</subject><subject>Embryo, Nonmammalian</subject><subject>Enzyme Activators - pharmacology</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Genes, Reporter</subject><subject>Microinjections</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis, Site-Directed</subject><subject>Neurites - drug effects</subject><subject>Neurites - metabolism</subject><subject>Neurobiology</subject><subject>Neurons</subject><subject>Neurons - cytology</subject><subject>Neurons - drug effects</subject><subject>Neurons - metabolism</subject><subject>Neurosciences</subject><subject>Phosphorylation - drug effects</subject><subject>Physiological aspects</subject><subject>Protein kinases</subject><subject>RNA, Messenger - pharmacology</subject><subject>Sequence Homology, Amino Acid</subject><subject>Synapsins - antagonists & inhibitors</subject><subject>Synapsins - genetics</subject><subject>Synapsins - metabolism</subject><subject>Xenopus laevis</subject><issn>1097-6256</issn><issn>1546-1726</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</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><recordid>eNp9kUlr3TAUhUVpaYbmFxSKKLSlC6eSbE3LR-gQCBQ6bYUsXztKbflFkknz76PUjz6SRVcSOp-O7tFB6ISSU0pq9SEE1ZAn6JDyRlRUMvG07ImWlWBcHKCjlK4IIZIr_RwdUKqlkKQ-RL82eBvnDD7g3z7YBHhTdbCF0EHIeJpHcMtoI043PrtLXLB0G-w2-ZBwhKFoGRIOsESfAc9LHuJ8ky9foGe9HROc7NZj9PPTxx9nX6qLr5_PzzYXlWuUzFXbE94RZx1o10jKlGZU19r1lLUcaM0awUhre2uhVYzrjvCekoZTx5XjQtfH6N3qW0JcL5CymXxyMI42wLwko7iQoiasKeTb_5K0fF95rC7g60fg1bzEUFIYJhvJakV5gU5XaLAjGB_6OUdbctgOJu_mAL0v5xuqOBdU0ftB3z-4UJgMf_Jgl5TM-fdvD9k3K-vinFKE3myjn2y8NZSY-7LN37IL92o36dJO0O2pXbv7zKlIYYC4j_LY6eUKBpuXCP-cVvUObKy4-A</recordid><startdate>20020501</startdate><enddate>20020501</enddate><creator>Kao, Hung-Teh</creator><creator>Song, Hong-jun</creator><creator>Porton, Barbara</creator><creator>Ming, Guo-li</creator><creator>Hoh, Josephine</creator><creator>Abraham, Michael</creator><creator>Czernik, Andrew J</creator><creator>Pieribone, Vincent A</creator><creator>Poo, Mu-ming</creator><creator>Greengard, Paul</creator><general>Nature Publishing Group US</general><general>Nature Publishing Group</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>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U7</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>88G</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</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>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2M</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PSYQQ</scope><scope>Q9U</scope><scope>RC3</scope><scope>F1W</scope><scope>H95</scope><scope>L.G</scope></search><sort><creationdate>20020501</creationdate><title>A protein kinase A-dependent molecular switch in synapsins regulates neurite outgrowth</title><author>Kao, Hung-Teh ; Song, Hong-jun ; Porton, Barbara ; Ming, Guo-li ; Hoh, Josephine ; Abraham, Michael ; Czernik, Andrew J ; Pieribone, Vincent A ; Poo, Mu-ming ; Greengard, Paul</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c487t-bf05d0cace9c47128921939cf12b5e1324620bafaaeb8259d05f10451c58c5693</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Animal Genetics and Genomics</topic><topic>Animals</topic><topic>Antibodies - 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We show here, using both
Xenopus laevis
embryonic neuronal culture and intact
X. laevis
embryos, that the nerve growth–promoting action of cAMP/PKA is mediated in part by the phosphorylation of synapsins at a single amino acid residue. Expression of a mutated form of synapsin that prevents phosphorylation at this site, or introduction of phospho-specific antibodies directed against this site, decreased basal and dibutyryl cAMP–stimulated neurite outgrowth. Expression of a mutation mimicking constitutive phosphorylation at this site increased neurite outgrowth, both under basal conditions and in the presence of a PKA inhibitor. These results provide a potential molecular approach for stimulating neuron regeneration, after injury and in neurodegenerative diseases.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>11976703</pmid><doi>10.1038/nn840</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Nature neuroscience, 2002-05, Vol.5 (5), p.431-437 |
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| source | Nature_系列刊; MEDLINE; Alma/SFX Local Collection |
| subjects | Animal Genetics and Genomics Animals Antibodies - pharmacology Behavioral Sciences Biological Techniques Biomedical and Life Sciences Biomedicine Bucladesine - pharmacology Cells, Cultured Conserved Sequence Cyclic AMP-Dependent Protein Kinases - antagonists & inhibitors Cyclic AMP-Dependent Protein Kinases - metabolism Embryo, Nonmammalian Enzyme Activators - pharmacology Enzyme Inhibitors - pharmacology Genes, Reporter Microinjections Molecular Sequence Data Mutagenesis, Site-Directed Neurites - drug effects Neurites - metabolism Neurobiology Neurons Neurons - cytology Neurons - drug effects Neurons - metabolism Neurosciences Phosphorylation - drug effects Physiological aspects Protein kinases RNA, Messenger - pharmacology Sequence Homology, Amino Acid Synapsins - antagonists & inhibitors Synapsins - genetics Synapsins - metabolism Xenopus laevis |
| title | A protein kinase A-dependent molecular switch in synapsins regulates neurite outgrowth |
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