Water channel aquaporin-2 directly binds to actin
Water channel aquaporin-2 (AQP2) strictly regulates body water homeostasis in mammals. Trafficking of AQP2 to the apical membrane is critical to the reabsorption of water in renal collecting ducts. Controlled apical positioning of AQP2 suggests the interaction of AQP2 with other proteins. To isolate...
Gespeichert in:
| Veröffentlicht in: | Biochemical and biophysical research communications 2004-09, Vol.322 (3), p.740-745 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 745 |
|---|---|
| container_issue | 3 |
| container_start_page | 740 |
| container_title | Biochemical and biophysical research communications |
| container_volume | 322 |
| creator | Noda, Yumi Horikawa, Saburo Katayama, Yoshifumi Sasaki, Sei |
| description | Water channel aquaporin-2 (AQP2) strictly regulates body water homeostasis in mammals. Trafficking of AQP2 to the apical membrane is critical to the reabsorption of water in renal collecting ducts. Controlled apical positioning of AQP2 suggests the interaction of AQP2 with other proteins. To isolate AQP2-binding proteins, immunoaffinity chromatography of extracts from rat kidney papilla was performed using a column covalently coupled with anti-AQP2 antibody. Using this method 42-kDa protein was purified and subsequently identified as β- and γ-isoforms of actin by two-dimensional gel analysis and matrix-assisted laser desorption-ionization time-of-flight mass spectrometry. AQP2 was indeed coimmunoprecipitated with actin from cell lysates of rat kidney papilla. In addition, surface plasmon resonance analyses showed that the C-terminal fragment of AQP2 strongly bound to actin and the
K
D value was 3.18
×
10
−8
M. In this experiment we have elucidated the direct binding of channel protein AQP2 to cytoskeletal protein actin, providing a novel mechanism for trafficking of not only AQP2 but also recycling channel proteins. |
| doi_str_mv | 10.1016/j.bbrc.2004.07.195 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_66824741</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0006291X0401722X</els_id><sourcerecordid>66824741</sourcerecordid><originalsourceid>FETCH-LOGICAL-c352t-520e96824a7543c8c9f9b5174fb1f4024e12fbc3b36a3c4bcd3bc020d99c04ca3</originalsourceid><addsrcrecordid>eNp9kEtLw0AURgdRbK3-AReSlbvEO49MOuBGii8ouFF0N8zcTHBKmrQzidB_b0IK7lzdzfkO3EPINYWMApV3m8zagBkDEBkUGVX5CZlTUJAyCuKUzAFApkzRrxm5iHEDQKmQ6pzMaM65zJmcE_ppOhcS_DZN4-rE7Huza4NvUpaUPjjs6kNifVPGpGsTg51vLslZZeroro53QT6eHt9XL-n67fl19bBOkeesS3MGTsklE6bIBcclqkrZnBaisrQSwISjrLLILZeGo7BYcovAoFQKQaDhC3I7eXeh3fcudnrrI7q6No1r-6jlKC8EHUA2gRjaGIOr9C74rQkHTUGPofRGj6H0GEpDoYdQw-jmaO_t1pV_k2OZAbifADf8-ONd0BG9a9BNWXTZ-v_8vyRseGI</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>66824741</pqid></control><display><type>article</type><title>Water channel aquaporin-2 directly binds to actin</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Noda, Yumi ; Horikawa, Saburo ; Katayama, Yoshifumi ; Sasaki, Sei</creator><creatorcontrib>Noda, Yumi ; Horikawa, Saburo ; Katayama, Yoshifumi ; Sasaki, Sei</creatorcontrib><description>Water channel aquaporin-2 (AQP2) strictly regulates body water homeostasis in mammals. Trafficking of AQP2 to the apical membrane is critical to the reabsorption of water in renal collecting ducts. Controlled apical positioning of AQP2 suggests the interaction of AQP2 with other proteins. To isolate AQP2-binding proteins, immunoaffinity chromatography of extracts from rat kidney papilla was performed using a column covalently coupled with anti-AQP2 antibody. Using this method 42-kDa protein was purified and subsequently identified as β- and γ-isoforms of actin by two-dimensional gel analysis and matrix-assisted laser desorption-ionization time-of-flight mass spectrometry. AQP2 was indeed coimmunoprecipitated with actin from cell lysates of rat kidney papilla. In addition, surface plasmon resonance analyses showed that the C-terminal fragment of AQP2 strongly bound to actin and the
K
D value was 3.18
×
10
−8
M. In this experiment we have elucidated the direct binding of channel protein AQP2 to cytoskeletal protein actin, providing a novel mechanism for trafficking of not only AQP2 but also recycling channel proteins.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2004.07.195</identifier><identifier>PMID: 15336526</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Actins - metabolism ; Amino Acid Sequence ; Animals ; Aquaporin ; Aquaporin 2 ; Aquaporins - chemistry ; Aquaporins - isolation & purification ; Aquaporins - metabolism ; Channel protein ; Chromatography, Affinity ; Cytoskeleton ; Electrophoresis, Gel, Two-Dimensional ; Kidney - metabolism ; Kinetics ; Membrane protein ; Molecular Sequence Data ; Peptide Fragments - chemistry ; Protein Binding ; Rats ; Renal collecting duct ; Sorting ; Trafficking ; Vasopressin ; Water homeostasis</subject><ispartof>Biochemical and biophysical research communications, 2004-09, Vol.322 (3), p.740-745</ispartof><rights>2004 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c352t-520e96824a7543c8c9f9b5174fb1f4024e12fbc3b36a3c4bcd3bc020d99c04ca3</citedby><cites>FETCH-LOGICAL-c352t-520e96824a7543c8c9f9b5174fb1f4024e12fbc3b36a3c4bcd3bc020d99c04ca3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006291X0401722X$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15336526$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Noda, Yumi</creatorcontrib><creatorcontrib>Horikawa, Saburo</creatorcontrib><creatorcontrib>Katayama, Yoshifumi</creatorcontrib><creatorcontrib>Sasaki, Sei</creatorcontrib><title>Water channel aquaporin-2 directly binds to actin</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Water channel aquaporin-2 (AQP2) strictly regulates body water homeostasis in mammals. Trafficking of AQP2 to the apical membrane is critical to the reabsorption of water in renal collecting ducts. Controlled apical positioning of AQP2 suggests the interaction of AQP2 with other proteins. To isolate AQP2-binding proteins, immunoaffinity chromatography of extracts from rat kidney papilla was performed using a column covalently coupled with anti-AQP2 antibody. Using this method 42-kDa protein was purified and subsequently identified as β- and γ-isoforms of actin by two-dimensional gel analysis and matrix-assisted laser desorption-ionization time-of-flight mass spectrometry. AQP2 was indeed coimmunoprecipitated with actin from cell lysates of rat kidney papilla. In addition, surface plasmon resonance analyses showed that the C-terminal fragment of AQP2 strongly bound to actin and the
K
D value was 3.18
×
10
−8
M. In this experiment we have elucidated the direct binding of channel protein AQP2 to cytoskeletal protein actin, providing a novel mechanism for trafficking of not only AQP2 but also recycling channel proteins.</description><subject>Actins - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Aquaporin</subject><subject>Aquaporin 2</subject><subject>Aquaporins - chemistry</subject><subject>Aquaporins - isolation & purification</subject><subject>Aquaporins - metabolism</subject><subject>Channel protein</subject><subject>Chromatography, Affinity</subject><subject>Cytoskeleton</subject><subject>Electrophoresis, Gel, Two-Dimensional</subject><subject>Kidney - metabolism</subject><subject>Kinetics</subject><subject>Membrane protein</subject><subject>Molecular Sequence Data</subject><subject>Peptide Fragments - chemistry</subject><subject>Protein Binding</subject><subject>Rats</subject><subject>Renal collecting duct</subject><subject>Sorting</subject><subject>Trafficking</subject><subject>Vasopressin</subject><subject>Water homeostasis</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEtLw0AURgdRbK3-AReSlbvEO49MOuBGii8ouFF0N8zcTHBKmrQzidB_b0IK7lzdzfkO3EPINYWMApV3m8zagBkDEBkUGVX5CZlTUJAyCuKUzAFApkzRrxm5iHEDQKmQ6pzMaM65zJmcE_ppOhcS_DZN4-rE7Huza4NvUpaUPjjs6kNifVPGpGsTg51vLslZZeroro53QT6eHt9XL-n67fl19bBOkeesS3MGTsklE6bIBcclqkrZnBaisrQSwISjrLLILZeGo7BYcovAoFQKQaDhC3I7eXeh3fcudnrrI7q6No1r-6jlKC8EHUA2gRjaGIOr9C74rQkHTUGPofRGj6H0GEpDoYdQw-jmaO_t1pV_k2OZAbifADf8-ONd0BG9a9BNWXTZ-v_8vyRseGI</recordid><startdate>20040924</startdate><enddate>20040924</enddate><creator>Noda, Yumi</creator><creator>Horikawa, Saburo</creator><creator>Katayama, Yoshifumi</creator><creator>Sasaki, Sei</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>20040924</creationdate><title>Water channel aquaporin-2 directly binds to actin</title><author>Noda, Yumi ; Horikawa, Saburo ; Katayama, Yoshifumi ; Sasaki, Sei</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c352t-520e96824a7543c8c9f9b5174fb1f4024e12fbc3b36a3c4bcd3bc020d99c04ca3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Actins - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Aquaporin</topic><topic>Aquaporin 2</topic><topic>Aquaporins - chemistry</topic><topic>Aquaporins - isolation & purification</topic><topic>Aquaporins - metabolism</topic><topic>Channel protein</topic><topic>Chromatography, Affinity</topic><topic>Cytoskeleton</topic><topic>Electrophoresis, Gel, Two-Dimensional</topic><topic>Kidney - metabolism</topic><topic>Kinetics</topic><topic>Membrane protein</topic><topic>Molecular Sequence Data</topic><topic>Peptide Fragments - chemistry</topic><topic>Protein Binding</topic><topic>Rats</topic><topic>Renal collecting duct</topic><topic>Sorting</topic><topic>Trafficking</topic><topic>Vasopressin</topic><topic>Water homeostasis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Noda, Yumi</creatorcontrib><creatorcontrib>Horikawa, Saburo</creatorcontrib><creatorcontrib>Katayama, Yoshifumi</creatorcontrib><creatorcontrib>Sasaki, Sei</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>Noda, Yumi</au><au>Horikawa, Saburo</au><au>Katayama, Yoshifumi</au><au>Sasaki, Sei</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Water channel aquaporin-2 directly binds to actin</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2004-09-24</date><risdate>2004</risdate><volume>322</volume><issue>3</issue><spage>740</spage><epage>745</epage><pages>740-745</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Water channel aquaporin-2 (AQP2) strictly regulates body water homeostasis in mammals. Trafficking of AQP2 to the apical membrane is critical to the reabsorption of water in renal collecting ducts. Controlled apical positioning of AQP2 suggests the interaction of AQP2 with other proteins. To isolate AQP2-binding proteins, immunoaffinity chromatography of extracts from rat kidney papilla was performed using a column covalently coupled with anti-AQP2 antibody. Using this method 42-kDa protein was purified and subsequently identified as β- and γ-isoforms of actin by two-dimensional gel analysis and matrix-assisted laser desorption-ionization time-of-flight mass spectrometry. AQP2 was indeed coimmunoprecipitated with actin from cell lysates of rat kidney papilla. In addition, surface plasmon resonance analyses showed that the C-terminal fragment of AQP2 strongly bound to actin and the
K
D value was 3.18
×
10
−8
M. In this experiment we have elucidated the direct binding of channel protein AQP2 to cytoskeletal protein actin, providing a novel mechanism for trafficking of not only AQP2 but also recycling channel proteins.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>15336526</pmid><doi>10.1016/j.bbrc.2004.07.195</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-291X |
| ispartof | Biochemical and biophysical research communications, 2004-09, Vol.322 (3), p.740-745 |
| issn | 0006-291X 1090-2104 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_66824741 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Actins - metabolism Amino Acid Sequence Animals Aquaporin Aquaporin 2 Aquaporins - chemistry Aquaporins - isolation & purification Aquaporins - metabolism Channel protein Chromatography, Affinity Cytoskeleton Electrophoresis, Gel, Two-Dimensional Kidney - metabolism Kinetics Membrane protein Molecular Sequence Data Peptide Fragments - chemistry Protein Binding Rats Renal collecting duct Sorting Trafficking Vasopressin Water homeostasis |
| title | Water channel aquaporin-2 directly binds to actin |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-27T17%3A56%3A14IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Water%20channel%20aquaporin-2%20directly%20binds%20to%20actin&rft.jtitle=Biochemical%20and%20biophysical%20research%20communications&rft.au=Noda,%20Yumi&rft.date=2004-09-24&rft.volume=322&rft.issue=3&rft.spage=740&rft.epage=745&rft.pages=740-745&rft.issn=0006-291X&rft.eissn=1090-2104&rft_id=info:doi/10.1016/j.bbrc.2004.07.195&rft_dat=%3Cproquest_cross%3E66824741%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=66824741&rft_id=info:pmid/15336526&rft_els_id=S0006291X0401722X&rfr_iscdi=true |