Compartmentalization of cAMP-dependent signaling by phosphodiesterase-4D is involved in the regulation of vasopressin-mediated water reabsorption in renal principal cells
The cAMP/protein kinase A (PKA)-dependent insertion of water channel aquaporin-2 (AQP2)-bearing vesicles into the plasma membrane in renal collecting duct principal cells (AQP2 shuttle) constitutes the molecular basis of arginine vasopressin (AVP)-regulated water reabsorption. cAMP/PKA signaling sys...
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| Veröffentlicht in: | Journal of the American Society of Nephrology 2007, Vol.18 (1), p.199-212 |
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| creator | STEFAN, Eduard WIESNER, Burkhard BEYERMANN, Michael KRAUSE, Eberhard POHL, Peter GALL, Irene MACINTYRE, Andrew N BACHMANN, Sebastian HOUSLAY, Miles D ROSENTHAL, Walter KLUSSMANN, Enno BAILLIE, George S MOLLAJEW, Rustam HENN, Volker LORENZ, Dorothea FURKERT, Jens SANTAMARIA, Katja NEDVETSKY, Pavel HUNDSRUCKER, Christian |
| description | The cAMP/protein kinase A (PKA)-dependent insertion of water channel aquaporin-2 (AQP2)-bearing vesicles into the plasma membrane in renal collecting duct principal cells (AQP2 shuttle) constitutes the molecular basis of arginine vasopressin (AVP)-regulated water reabsorption. cAMP/PKA signaling systems are compartmentalized by A kinase anchoring proteins (AKAP) that tether PKA to subcellular sites and by phosphodiesterases (PDE) that terminate PKA signaling through hydrolysis of localized cAMP. In primary cultured principal cells, AVP causes focal activation of PKA. PKA and cAMP-specific phosphodiesterase-4D (PDE4D) are located on AQP2-bearing vesicles. The selective PDE4 inhibitor rolipram increases AKAP-tethered PKA activity on AQP2-bearing vesicles and enhances the AQP2 shuttle and thereby the osmotic water permeability. AKAP18delta, which is located on AQP2-bearing vesicles, directly interacts with PDE4D and PKA. In response to AVP, PDE4D and AQP2 translocate to the plasma membrane. Here PDE4D is activated through PKA phosphorylation and reduces the osmotic water permeability. Taken together, a novel, compartmentalized, and physiologically relevant cAMP-dependent signal transduction module on AQP2-bearing vesicles, comprising anchored PDE4D, AKAP18delta, and PKA, has been identified. |
| doi_str_mv | 10.1681/asn.2006020132 |
| format | Article |
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In primary cultured principal cells, AVP causes focal activation of PKA. PKA and cAMP-specific phosphodiesterase-4D (PDE4D) are located on AQP2-bearing vesicles. The selective PDE4 inhibitor rolipram increases AKAP-tethered PKA activity on AQP2-bearing vesicles and enhances the AQP2 shuttle and thereby the osmotic water permeability. AKAP18delta, which is located on AQP2-bearing vesicles, directly interacts with PDE4D and PKA. In response to AVP, PDE4D and AQP2 translocate to the plasma membrane. Here PDE4D is activated through PKA phosphorylation and reduces the osmotic water permeability. Taken together, a novel, compartmentalized, and physiologically relevant cAMP-dependent signal transduction module on AQP2-bearing vesicles, comprising anchored PDE4D, AKAP18delta, and PKA, has been identified.</description><identifier>ISSN: 1046-6673</identifier><identifier>EISSN: 1533-3450</identifier><identifier>DOI: 10.1681/asn.2006020132</identifier><identifier>PMID: 17135396</identifier><identifier>CODEN: JASNEU</identifier><language>eng</language><publisher>Hagerstown, MD: Lippincott Williams & Wilkins</publisher><subject>3',5'-Cyclic-AMP Phosphodiesterases - antagonists & inhibitors ; 3',5'-Cyclic-AMP Phosphodiesterases - genetics ; 3',5'-Cyclic-AMP Phosphodiesterases - metabolism ; Adaptor Proteins, Signal Transducing - genetics ; Adaptor Proteins, Signal Transducing - metabolism ; Amino Acid Sequence ; Animals ; Aquaporin 2 - metabolism ; Arginine Vasopressin - metabolism ; Arginine Vasopressin - pharmacology ; Biological and medical sciences ; Cells, Cultured ; Cyclic AMP - metabolism ; Cyclic AMP-Dependent Protein Kinases - genetics ; Cyclic AMP-Dependent Protein Kinases - metabolism ; Cyclic Nucleotide Phosphodiesterases, Type 3 ; Cyclic Nucleotide Phosphodiesterases, Type 4 ; Fundamental and applied biological sciences. Psychology ; Humans ; Kidney Tubules, Collecting - cytology ; Kidney Tubules, Collecting - drug effects ; Kidney Tubules, Collecting - metabolism ; Medical sciences ; Models, Biological ; Molecular Sequence Data ; Nephrology. Urinary tract diseases ; Phosphodiesterase Inhibitors - pharmacology ; Rats ; Rats, Sprague-Dawley ; Recombinant Proteins - antagonists & inhibitors ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Rolipram - pharmacology ; Sequence Homology, Amino Acid ; Signal Transduction ; Vertebrates: urinary system ; Water - metabolism</subject><ispartof>Journal of the American Society of Nephrology, 2007, Vol.18 (1), p.199-212</ispartof><rights>2007 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c429t-b19ed870ec0a2af7423a1c96b6acd0687f194823a64bc3dca12fb2b9bfebba773</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,4010,27900,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18422504$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17135396$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>STEFAN, Eduard</creatorcontrib><creatorcontrib>WIESNER, Burkhard</creatorcontrib><creatorcontrib>BEYERMANN, Michael</creatorcontrib><creatorcontrib>KRAUSE, Eberhard</creatorcontrib><creatorcontrib>POHL, Peter</creatorcontrib><creatorcontrib>GALL, Irene</creatorcontrib><creatorcontrib>MACINTYRE, Andrew N</creatorcontrib><creatorcontrib>BACHMANN, Sebastian</creatorcontrib><creatorcontrib>HOUSLAY, Miles D</creatorcontrib><creatorcontrib>ROSENTHAL, Walter</creatorcontrib><creatorcontrib>KLUSSMANN, Enno</creatorcontrib><creatorcontrib>BAILLIE, George S</creatorcontrib><creatorcontrib>MOLLAJEW, Rustam</creatorcontrib><creatorcontrib>HENN, Volker</creatorcontrib><creatorcontrib>LORENZ, Dorothea</creatorcontrib><creatorcontrib>FURKERT, Jens</creatorcontrib><creatorcontrib>SANTAMARIA, Katja</creatorcontrib><creatorcontrib>NEDVETSKY, Pavel</creatorcontrib><creatorcontrib>HUNDSRUCKER, Christian</creatorcontrib><title>Compartmentalization of cAMP-dependent signaling by phosphodiesterase-4D is involved in the regulation of vasopressin-mediated water reabsorption in renal principal cells</title><title>Journal of the American Society of Nephrology</title><addtitle>J Am Soc Nephrol</addtitle><description>The cAMP/protein kinase A (PKA)-dependent insertion of water channel aquaporin-2 (AQP2)-bearing vesicles into the plasma membrane in renal collecting duct principal cells (AQP2 shuttle) constitutes the molecular basis of arginine vasopressin (AVP)-regulated water reabsorption. cAMP/PKA signaling systems are compartmentalized by A kinase anchoring proteins (AKAP) that tether PKA to subcellular sites and by phosphodiesterases (PDE) that terminate PKA signaling through hydrolysis of localized cAMP. In primary cultured principal cells, AVP causes focal activation of PKA. PKA and cAMP-specific phosphodiesterase-4D (PDE4D) are located on AQP2-bearing vesicles. The selective PDE4 inhibitor rolipram increases AKAP-tethered PKA activity on AQP2-bearing vesicles and enhances the AQP2 shuttle and thereby the osmotic water permeability. AKAP18delta, which is located on AQP2-bearing vesicles, directly interacts with PDE4D and PKA. In response to AVP, PDE4D and AQP2 translocate to the plasma membrane. Here PDE4D is activated through PKA phosphorylation and reduces the osmotic water permeability. Taken together, a novel, compartmentalized, and physiologically relevant cAMP-dependent signal transduction module on AQP2-bearing vesicles, comprising anchored PDE4D, AKAP18delta, and PKA, has been identified.</description><subject>3',5'-Cyclic-AMP Phosphodiesterases - antagonists & inhibitors</subject><subject>3',5'-Cyclic-AMP Phosphodiesterases - genetics</subject><subject>3',5'-Cyclic-AMP Phosphodiesterases - metabolism</subject><subject>Adaptor Proteins, Signal Transducing - genetics</subject><subject>Adaptor Proteins, Signal Transducing - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Aquaporin 2 - metabolism</subject><subject>Arginine Vasopressin - metabolism</subject><subject>Arginine Vasopressin - pharmacology</subject><subject>Biological and medical sciences</subject><subject>Cells, Cultured</subject><subject>Cyclic AMP - metabolism</subject><subject>Cyclic AMP-Dependent Protein Kinases - genetics</subject><subject>Cyclic AMP-Dependent Protein Kinases - metabolism</subject><subject>Cyclic Nucleotide Phosphodiesterases, Type 3</subject><subject>Cyclic Nucleotide Phosphodiesterases, Type 4</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Kidney Tubules, Collecting - cytology</subject><subject>Kidney Tubules, Collecting - drug effects</subject><subject>Kidney Tubules, Collecting - metabolism</subject><subject>Medical sciences</subject><subject>Models, Biological</subject><subject>Molecular Sequence Data</subject><subject>Nephrology. Urinary tract diseases</subject><subject>Phosphodiesterase Inhibitors - pharmacology</subject><subject>Rats</subject><subject>Rats, Sprague-Dawley</subject><subject>Recombinant Proteins - antagonists & inhibitors</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>Rolipram - pharmacology</subject><subject>Sequence Homology, Amino Acid</subject><subject>Signal Transduction</subject><subject>Vertebrates: urinary system</subject><subject>Water - metabolism</subject><issn>1046-6673</issn><issn>1533-3450</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkU1v1DAQhiNERT_gyhH5Arcs_oqTHFdbKEilRQLO0dhxtkaJHTzZReUn8Ss7pSv2YPuV55nX45mieC34SphGvAeMK8m54ZILJZ8VZ6JSqlS64s9Jc21KY2p1Wpwj_uRcVLKuXxSnohaqUq05K_5u0jRDXiYfFxjDH1hCiiwNzK2_fC17P_vYU4hh2EaKxy2z92y-S0irDx4XnwF9qS9ZQBbiPo1735Ngy51n2W9343_HPWCas0cMsZx8H2Ah8jftmUCwmPL8D6Xk7OkxNucQXZhJOT-O-LI4GWBE_-pwXhQ_Pn74vvlUXt9efd6sr0unZbuUVrS-b2ruHQcJQ62lAuFaYw24npumHkSrG7o02jrVOxBysNK2dvDWQl2ri-Ldk--c068dfbGbAj5WANGnHXamUQ3XTUXg6gl0OSFmP3RU8QT5vhO8e5xOt_520x2nQwlvDs47Sx044odxEPD2AAA6GIcM1AA8co2WsuJaPQCyIJ1I</recordid><startdate>2007</startdate><enddate>2007</enddate><creator>STEFAN, Eduard</creator><creator>WIESNER, Burkhard</creator><creator>BEYERMANN, Michael</creator><creator>KRAUSE, Eberhard</creator><creator>POHL, Peter</creator><creator>GALL, Irene</creator><creator>MACINTYRE, Andrew N</creator><creator>BACHMANN, Sebastian</creator><creator>HOUSLAY, Miles D</creator><creator>ROSENTHAL, Walter</creator><creator>KLUSSMANN, Enno</creator><creator>BAILLIE, George S</creator><creator>MOLLAJEW, Rustam</creator><creator>HENN, Volker</creator><creator>LORENZ, Dorothea</creator><creator>FURKERT, Jens</creator><creator>SANTAMARIA, Katja</creator><creator>NEDVETSKY, Pavel</creator><creator>HUNDSRUCKER, Christian</creator><general>Lippincott Williams & Wilkins</general><scope>IQODW</scope><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>2007</creationdate><title>Compartmentalization of cAMP-dependent signaling by phosphodiesterase-4D is involved in the regulation of vasopressin-mediated water reabsorption in renal principal cells</title><author>STEFAN, Eduard ; WIESNER, Burkhard ; BEYERMANN, Michael ; KRAUSE, Eberhard ; POHL, Peter ; GALL, Irene ; MACINTYRE, Andrew N ; BACHMANN, Sebastian ; HOUSLAY, Miles D ; ROSENTHAL, Walter ; KLUSSMANN, Enno ; BAILLIE, George S ; MOLLAJEW, Rustam ; HENN, Volker ; LORENZ, Dorothea ; FURKERT, Jens ; SANTAMARIA, Katja ; NEDVETSKY, Pavel ; HUNDSRUCKER, Christian</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c429t-b19ed870ec0a2af7423a1c96b6acd0687f194823a64bc3dca12fb2b9bfebba773</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>3',5'-Cyclic-AMP Phosphodiesterases - antagonists & inhibitors</topic><topic>3',5'-Cyclic-AMP Phosphodiesterases - genetics</topic><topic>3',5'-Cyclic-AMP Phosphodiesterases - metabolism</topic><topic>Adaptor Proteins, Signal Transducing - genetics</topic><topic>Adaptor Proteins, Signal Transducing - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Aquaporin 2 - metabolism</topic><topic>Arginine Vasopressin - metabolism</topic><topic>Arginine Vasopressin - pharmacology</topic><topic>Biological and medical sciences</topic><topic>Cells, Cultured</topic><topic>Cyclic AMP - metabolism</topic><topic>Cyclic AMP-Dependent Protein Kinases - genetics</topic><topic>Cyclic AMP-Dependent Protein Kinases - metabolism</topic><topic>Cyclic Nucleotide Phosphodiesterases, Type 3</topic><topic>Cyclic Nucleotide Phosphodiesterases, Type 4</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Kidney Tubules, Collecting - cytology</topic><topic>Kidney Tubules, Collecting - drug effects</topic><topic>Kidney Tubules, Collecting - metabolism</topic><topic>Medical sciences</topic><topic>Models, Biological</topic><topic>Molecular Sequence Data</topic><topic>Nephrology. Urinary tract diseases</topic><topic>Phosphodiesterase Inhibitors - pharmacology</topic><topic>Rats</topic><topic>Rats, Sprague-Dawley</topic><topic>Recombinant Proteins - antagonists & inhibitors</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - metabolism</topic><topic>Rolipram - pharmacology</topic><topic>Sequence Homology, Amino Acid</topic><topic>Signal Transduction</topic><topic>Vertebrates: urinary system</topic><topic>Water - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>STEFAN, Eduard</creatorcontrib><creatorcontrib>WIESNER, Burkhard</creatorcontrib><creatorcontrib>BEYERMANN, Michael</creatorcontrib><creatorcontrib>KRAUSE, Eberhard</creatorcontrib><creatorcontrib>POHL, Peter</creatorcontrib><creatorcontrib>GALL, Irene</creatorcontrib><creatorcontrib>MACINTYRE, Andrew N</creatorcontrib><creatorcontrib>BACHMANN, Sebastian</creatorcontrib><creatorcontrib>HOUSLAY, Miles D</creatorcontrib><creatorcontrib>ROSENTHAL, Walter</creatorcontrib><creatorcontrib>KLUSSMANN, Enno</creatorcontrib><creatorcontrib>BAILLIE, George S</creatorcontrib><creatorcontrib>MOLLAJEW, Rustam</creatorcontrib><creatorcontrib>HENN, Volker</creatorcontrib><creatorcontrib>LORENZ, Dorothea</creatorcontrib><creatorcontrib>FURKERT, Jens</creatorcontrib><creatorcontrib>SANTAMARIA, Katja</creatorcontrib><creatorcontrib>NEDVETSKY, Pavel</creatorcontrib><creatorcontrib>HUNDSRUCKER, Christian</creatorcontrib><collection>Pascal-Francis</collection><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>Journal of the American Society of Nephrology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>STEFAN, Eduard</au><au>WIESNER, Burkhard</au><au>BEYERMANN, Michael</au><au>KRAUSE, Eberhard</au><au>POHL, Peter</au><au>GALL, Irene</au><au>MACINTYRE, Andrew N</au><au>BACHMANN, Sebastian</au><au>HOUSLAY, Miles D</au><au>ROSENTHAL, Walter</au><au>KLUSSMANN, Enno</au><au>BAILLIE, George S</au><au>MOLLAJEW, Rustam</au><au>HENN, Volker</au><au>LORENZ, Dorothea</au><au>FURKERT, Jens</au><au>SANTAMARIA, Katja</au><au>NEDVETSKY, Pavel</au><au>HUNDSRUCKER, Christian</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Compartmentalization of cAMP-dependent signaling by phosphodiesterase-4D is involved in the regulation of vasopressin-mediated water reabsorption in renal principal cells</atitle><jtitle>Journal of the American Society of Nephrology</jtitle><addtitle>J Am Soc Nephrol</addtitle><date>2007</date><risdate>2007</risdate><volume>18</volume><issue>1</issue><spage>199</spage><epage>212</epage><pages>199-212</pages><issn>1046-6673</issn><eissn>1533-3450</eissn><coden>JASNEU</coden><abstract>The cAMP/protein kinase A (PKA)-dependent insertion of water channel aquaporin-2 (AQP2)-bearing vesicles into the plasma membrane in renal collecting duct principal cells (AQP2 shuttle) constitutes the molecular basis of arginine vasopressin (AVP)-regulated water reabsorption. cAMP/PKA signaling systems are compartmentalized by A kinase anchoring proteins (AKAP) that tether PKA to subcellular sites and by phosphodiesterases (PDE) that terminate PKA signaling through hydrolysis of localized cAMP. In primary cultured principal cells, AVP causes focal activation of PKA. PKA and cAMP-specific phosphodiesterase-4D (PDE4D) are located on AQP2-bearing vesicles. The selective PDE4 inhibitor rolipram increases AKAP-tethered PKA activity on AQP2-bearing vesicles and enhances the AQP2 shuttle and thereby the osmotic water permeability. AKAP18delta, which is located on AQP2-bearing vesicles, directly interacts with PDE4D and PKA. In response to AVP, PDE4D and AQP2 translocate to the plasma membrane. Here PDE4D is activated through PKA phosphorylation and reduces the osmotic water permeability. Taken together, a novel, compartmentalized, and physiologically relevant cAMP-dependent signal transduction module on AQP2-bearing vesicles, comprising anchored PDE4D, AKAP18delta, and PKA, has been identified.</abstract><cop>Hagerstown, MD</cop><pub>Lippincott Williams & Wilkins</pub><pmid>17135396</pmid><doi>10.1681/asn.2006020132</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Journal of the American Society of Nephrology, 2007, Vol.18 (1), p.199-212 |
| issn | 1046-6673 1533-3450 |
| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | 3',5'-Cyclic-AMP Phosphodiesterases - antagonists & inhibitors 3',5'-Cyclic-AMP Phosphodiesterases - genetics 3',5'-Cyclic-AMP Phosphodiesterases - metabolism Adaptor Proteins, Signal Transducing - genetics Adaptor Proteins, Signal Transducing - metabolism Amino Acid Sequence Animals Aquaporin 2 - metabolism Arginine Vasopressin - metabolism Arginine Vasopressin - pharmacology Biological and medical sciences Cells, Cultured Cyclic AMP - metabolism Cyclic AMP-Dependent Protein Kinases - genetics Cyclic AMP-Dependent Protein Kinases - metabolism Cyclic Nucleotide Phosphodiesterases, Type 3 Cyclic Nucleotide Phosphodiesterases, Type 4 Fundamental and applied biological sciences. Psychology Humans Kidney Tubules, Collecting - cytology Kidney Tubules, Collecting - drug effects Kidney Tubules, Collecting - metabolism Medical sciences Models, Biological Molecular Sequence Data Nephrology. Urinary tract diseases Phosphodiesterase Inhibitors - pharmacology Rats Rats, Sprague-Dawley Recombinant Proteins - antagonists & inhibitors Recombinant Proteins - genetics Recombinant Proteins - metabolism Rolipram - pharmacology Sequence Homology, Amino Acid Signal Transduction Vertebrates: urinary system Water - metabolism |
| title | Compartmentalization of cAMP-dependent signaling by phosphodiesterase-4D is involved in the regulation of vasopressin-mediated water reabsorption in renal principal cells |
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