Structural insights into the function of human caveolin 1
Caveolin-1 (Cav-1) is emerging as the central protein controlling caveolae formation, caveolae trafficking, and cellular signalling. In particular, it is known that Cav-1 interacts and modulates the activity of several signalling proteins through the so-called caveolin scaffolding domain. In this pa...
Gespeichert in:
| Veröffentlicht in: | Biochemical and biophysical research communications 2005-12, Vol.338 (3), p.1383-1390 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1390 |
|---|---|
| container_issue | 3 |
| container_start_page | 1383 |
| container_title | Biochemical and biophysical research communications |
| container_volume | 338 |
| creator | Spisni, Enzo Tomasi, Vittorio Cestaro, Alessandro Tosatto, Silvio C.E. |
| description | Caveolin-1 (Cav-1) is emerging as the central protein controlling caveolae formation, caveolae trafficking, and cellular signalling. In particular, it is known that Cav-1 interacts and modulates the activity of several signalling proteins through the so-called caveolin scaffolding domain. In this paper, we used a bioinformatics approach to assess the validity of some long-standing structural features of Cav-1. We could confirm the existence of a membrane spanning region of Cav-1 and highlight an interesting pattern of palmitoylated cysteine residues explaining the structural features of the Cav-1 C-terminal region. Moreover, the scaffolding domain is predicted to have a different structure than previously reported. |
| doi_str_mv | 10.1016/j.bbrc.2005.10.099 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_68808119</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0006291X05023491</els_id><sourcerecordid>68808119</sourcerecordid><originalsourceid>FETCH-LOGICAL-c354t-23f4ce392f0fd16a36fb5d32bfbb1c0473e75f65a27551c00ae7459955a8a4e43</originalsourceid><addsrcrecordid>eNp9kE1LxDAQhoMo7rr6BzxIT966TtImbcCLiF-w4EEFbyFNJ26WfqxJuuC_t2UXvHma4eWZF-Yh5JLCkgIVN5tlVXmzZAB8DJYg5RGZU5CQMgr5MZkDgEiZpJ8zchbCBoDSXMhTMqOCiQyKYk7kW_SDiYPXTeK64L7WMYxL7JO4xsQOnYmu75LeJuuh1V1i9A77xnUJPScnVjcBLw5zQT4eH97vn9PV69PL_d0qNRnPY8oymxvMJLNgayp0JmzF64xVtqqogbzIsOBWcM0KzscANBY5l5JzXeoc82xBrve9W99_Dxiial0w2DS6w34ISpQllJTKEWR70Pg-BI9Wbb1rtf9RFNQkTG3UJExNwqZsFDYeXR3ah6rF-u_kYGgEbvcAjj_uHHoVjMPOYO08mqjq3v3X_wsl-3uP</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>68808119</pqid></control><display><type>article</type><title>Structural insights into the function of human caveolin 1</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Spisni, Enzo ; Tomasi, Vittorio ; Cestaro, Alessandro ; Tosatto, Silvio C.E.</creator><creatorcontrib>Spisni, Enzo ; Tomasi, Vittorio ; Cestaro, Alessandro ; Tosatto, Silvio C.E.</creatorcontrib><description>Caveolin-1 (Cav-1) is emerging as the central protein controlling caveolae formation, caveolae trafficking, and cellular signalling. In particular, it is known that Cav-1 interacts and modulates the activity of several signalling proteins through the so-called caveolin scaffolding domain. In this paper, we used a bioinformatics approach to assess the validity of some long-standing structural features of Cav-1. We could confirm the existence of a membrane spanning region of Cav-1 and highlight an interesting pattern of palmitoylated cysteine residues explaining the structural features of the Cav-1 C-terminal region. Moreover, the scaffolding domain is predicted to have a different structure than previously reported.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2005.10.099</identifier><identifier>PMID: 16263077</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Caveolin 1 ; Caveolin 1 - chemistry ; Caveolin 1 - metabolism ; Cell Membrane - chemistry ; Cell Membrane - metabolism ; Computational Biology ; Humans ; Molecular Sequence Data ; Plasma membrane microdomains ; Protein interactions ; Sequence Alignment ; Sequence Homology, Amino Acid ; Structure prediction ; Transmembrane prediction</subject><ispartof>Biochemical and biophysical research communications, 2005-12, Vol.338 (3), p.1383-1390</ispartof><rights>2005 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c354t-23f4ce392f0fd16a36fb5d32bfbb1c0473e75f65a27551c00ae7459955a8a4e43</citedby><cites>FETCH-LOGICAL-c354t-23f4ce392f0fd16a36fb5d32bfbb1c0473e75f65a27551c00ae7459955a8a4e43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006291X05023491$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16263077$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Spisni, Enzo</creatorcontrib><creatorcontrib>Tomasi, Vittorio</creatorcontrib><creatorcontrib>Cestaro, Alessandro</creatorcontrib><creatorcontrib>Tosatto, Silvio C.E.</creatorcontrib><title>Structural insights into the function of human caveolin 1</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Caveolin-1 (Cav-1) is emerging as the central protein controlling caveolae formation, caveolae trafficking, and cellular signalling. In particular, it is known that Cav-1 interacts and modulates the activity of several signalling proteins through the so-called caveolin scaffolding domain. In this paper, we used a bioinformatics approach to assess the validity of some long-standing structural features of Cav-1. We could confirm the existence of a membrane spanning region of Cav-1 and highlight an interesting pattern of palmitoylated cysteine residues explaining the structural features of the Cav-1 C-terminal region. Moreover, the scaffolding domain is predicted to have a different structure than previously reported.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Caveolin 1</subject><subject>Caveolin 1 - chemistry</subject><subject>Caveolin 1 - metabolism</subject><subject>Cell Membrane - chemistry</subject><subject>Cell Membrane - metabolism</subject><subject>Computational Biology</subject><subject>Humans</subject><subject>Molecular Sequence Data</subject><subject>Plasma membrane microdomains</subject><subject>Protein interactions</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Amino Acid</subject><subject>Structure prediction</subject><subject>Transmembrane prediction</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1LxDAQhoMo7rr6BzxIT966TtImbcCLiF-w4EEFbyFNJ26WfqxJuuC_t2UXvHma4eWZF-Yh5JLCkgIVN5tlVXmzZAB8DJYg5RGZU5CQMgr5MZkDgEiZpJ8zchbCBoDSXMhTMqOCiQyKYk7kW_SDiYPXTeK64L7WMYxL7JO4xsQOnYmu75LeJuuh1V1i9A77xnUJPScnVjcBLw5zQT4eH97vn9PV69PL_d0qNRnPY8oymxvMJLNgayp0JmzF64xVtqqogbzIsOBWcM0KzscANBY5l5JzXeoc82xBrve9W99_Dxiial0w2DS6w34ISpQllJTKEWR70Pg-BI9Wbb1rtf9RFNQkTG3UJExNwqZsFDYeXR3ah6rF-u_kYGgEbvcAjj_uHHoVjMPOYO08mqjq3v3X_wsl-3uP</recordid><startdate>20051223</startdate><enddate>20051223</enddate><creator>Spisni, Enzo</creator><creator>Tomasi, Vittorio</creator><creator>Cestaro, Alessandro</creator><creator>Tosatto, Silvio C.E.</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>20051223</creationdate><title>Structural insights into the function of human caveolin 1</title><author>Spisni, Enzo ; Tomasi, Vittorio ; Cestaro, Alessandro ; Tosatto, Silvio C.E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c354t-23f4ce392f0fd16a36fb5d32bfbb1c0473e75f65a27551c00ae7459955a8a4e43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Caveolin 1</topic><topic>Caveolin 1 - chemistry</topic><topic>Caveolin 1 - metabolism</topic><topic>Cell Membrane - chemistry</topic><topic>Cell Membrane - metabolism</topic><topic>Computational Biology</topic><topic>Humans</topic><topic>Molecular Sequence Data</topic><topic>Plasma membrane microdomains</topic><topic>Protein interactions</topic><topic>Sequence Alignment</topic><topic>Sequence Homology, Amino Acid</topic><topic>Structure prediction</topic><topic>Transmembrane prediction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Spisni, Enzo</creatorcontrib><creatorcontrib>Tomasi, Vittorio</creatorcontrib><creatorcontrib>Cestaro, Alessandro</creatorcontrib><creatorcontrib>Tosatto, Silvio C.E.</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>Spisni, Enzo</au><au>Tomasi, Vittorio</au><au>Cestaro, Alessandro</au><au>Tosatto, Silvio C.E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural insights into the function of human caveolin 1</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2005-12-23</date><risdate>2005</risdate><volume>338</volume><issue>3</issue><spage>1383</spage><epage>1390</epage><pages>1383-1390</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Caveolin-1 (Cav-1) is emerging as the central protein controlling caveolae formation, caveolae trafficking, and cellular signalling. In particular, it is known that Cav-1 interacts and modulates the activity of several signalling proteins through the so-called caveolin scaffolding domain. In this paper, we used a bioinformatics approach to assess the validity of some long-standing structural features of Cav-1. We could confirm the existence of a membrane spanning region of Cav-1 and highlight an interesting pattern of palmitoylated cysteine residues explaining the structural features of the Cav-1 C-terminal region. Moreover, the scaffolding domain is predicted to have a different structure than previously reported.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>16263077</pmid><doi>10.1016/j.bbrc.2005.10.099</doi><tpages>8</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-291X |
| ispartof | Biochemical and biophysical research communications, 2005-12, Vol.338 (3), p.1383-1390 |
| issn | 0006-291X 1090-2104 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_68808119 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Amino Acid Sequence Animals Caveolin 1 Caveolin 1 - chemistry Caveolin 1 - metabolism Cell Membrane - chemistry Cell Membrane - metabolism Computational Biology Humans Molecular Sequence Data Plasma membrane microdomains Protein interactions Sequence Alignment Sequence Homology, Amino Acid Structure prediction Transmembrane prediction |
| title | Structural insights into the function of human caveolin 1 |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-28T23%3A32%3A27IST&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=Structural%20insights%20into%20the%20function%20of%20human%20caveolin%201&rft.jtitle=Biochemical%20and%20biophysical%20research%20communications&rft.au=Spisni,%20Enzo&rft.date=2005-12-23&rft.volume=338&rft.issue=3&rft.spage=1383&rft.epage=1390&rft.pages=1383-1390&rft.issn=0006-291X&rft.eissn=1090-2104&rft_id=info:doi/10.1016/j.bbrc.2005.10.099&rft_dat=%3Cproquest_cross%3E68808119%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=68808119&rft_id=info:pmid/16263077&rft_els_id=S0006291X05023491&rfr_iscdi=true |