Amino-terminal palmitate or polybasic domain can provide required second signal to myristate for membrane binding of p56lck
Recent work has shown that several members of the src family of protein tyrosine kinases (PTKs) are modified by palmitoylation, including p56lck and p59fyn but not p60src. Mapping of the sites of palmitoylation in p56lck identified cys3 as the major site and cys5 as a minor site of palmitoylation. A...
Gespeichert in:
| Veröffentlicht in: | Biochemical and biophysical research communications 1995-02, Vol.207 (2), p.868-876 |
|---|---|
| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 876 |
|---|---|
| container_issue | 2 |
| container_start_page | 868 |
| container_title | Biochemical and biophysical research communications |
| container_volume | 207 |
| creator | Kwong, J Lublin, D M |
| description | Recent work has shown that several members of the src family of protein tyrosine kinases (PTKs) are modified by palmitoylation, including p56lck and p59fyn but not p60src. Mapping of the sites of palmitoylation in p56lck identified cys3 as the major site and cys5 as a minor site of palmitoylation. A non-palmitoylated p56lck(cys3,5-->ser) mutant was localized exclusively in the cytoplasm despite the presence of amino-terminal myristoylation, thus indicating that palmitoylation of p56lck was necessary for membrane binding. The addition of a domain of six lysine residues to a non-palmitoylated p56lck mutant was sufficient to re-establish membrane binding but not to target the non-palmitoylated p56lck to caveolae. These results establish that two signals, myristoylation plus either palmitoylation or a polybasic domain, are necessary for membrane binding of src family PTKs. |
| doi_str_mv | 10.1006/bbrc.1995.1266 |
| format | Article |
| fullrecord | <record><control><sourceid>pubmed_cross</sourceid><recordid>TN_cdi_crossref_primary_10_1006_bbrc_1995_1266</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>7864883</sourcerecordid><originalsourceid>FETCH-LOGICAL-c1373-fb68d36e6df3ab8f8c14e474db73c63f52ebec9f2d12ebcad7d930b92ead82b43</originalsourceid><addsrcrecordid>eNo9kDtPwzAUhT2ASimsbEj-Awl2nDrJWFW8pEosILFFflxXhtgOdooU8edJaMV0rq7O-YYPoRtKckoIv5Myqpw2zTqnBednaEmmb1Y09P0CXab0QQilJW8WaFHVvKxrtkQ_G2d9yAaIU4oO96JzdhAD4BBxH7pRimQV1sEJ67ESHvcxfFsNOMLXwUbQOIEKfgq7nwFDwG6MNv0xzARx4GQUHrC0Xlu_x8Hgfs079XmFzo3oElyfcoXeHu5ft0_Z7uXxebvZZYqyimVG8lozDlwbJmRtakVLKKtSy4opzsy6AAmqMYWm06WErnTDiGwKELouZMlWKD9yVQwpRTBtH60TcWwpaWdx7SyuncW1s7hpcHsc9AfpQP_XT9bYL1Qyb68</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Amino-terminal palmitate or polybasic domain can provide required second signal to myristate for membrane binding of p56lck</title><source>MEDLINE</source><source>ScienceDirect Journals (5 years ago - present)</source><creator>Kwong, J ; Lublin, D M</creator><creatorcontrib>Kwong, J ; Lublin, D M</creatorcontrib><description>Recent work has shown that several members of the src family of protein tyrosine kinases (PTKs) are modified by palmitoylation, including p56lck and p59fyn but not p60src. Mapping of the sites of palmitoylation in p56lck identified cys3 as the major site and cys5 as a minor site of palmitoylation. A non-palmitoylated p56lck(cys3,5-->ser) mutant was localized exclusively in the cytoplasm despite the presence of amino-terminal myristoylation, thus indicating that palmitoylation of p56lck was necessary for membrane binding. The addition of a domain of six lysine residues to a non-palmitoylated p56lck mutant was sufficient to re-establish membrane binding but not to target the non-palmitoylated p56lck to caveolae. These results establish that two signals, myristoylation plus either palmitoylation or a polybasic domain, are necessary for membrane binding of src family PTKs.</description><identifier>ISSN: 0006-291X</identifier><identifier>DOI: 10.1006/bbrc.1995.1266</identifier><identifier>PMID: 7864883</identifier><language>eng</language><publisher>United States</publisher><subject>Amino Acid Sequence ; Binding Sites ; Cell Membrane - metabolism ; Cysteine ; HeLa Cells ; Humans ; Lymphocyte Specific Protein Tyrosine Kinase p56(lck) ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Myristic Acid ; Myristic Acids - metabolism ; Plasmids ; Point Mutation ; Protein-Tyrosine Kinases - biosynthesis ; Protein-Tyrosine Kinases - chemistry ; Protein-Tyrosine Kinases - metabolism ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - chemistry ; Recombinant Proteins - metabolism ; Serine ; Signal Transduction ; Transfection</subject><ispartof>Biochemical and biophysical research communications, 1995-02, Vol.207 (2), p.868-876</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c1373-fb68d36e6df3ab8f8c14e474db73c63f52ebec9f2d12ebcad7d930b92ead82b43</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27922,27923</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7864883$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kwong, J</creatorcontrib><creatorcontrib>Lublin, D M</creatorcontrib><title>Amino-terminal palmitate or polybasic domain can provide required second signal to myristate for membrane binding of p56lck</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Recent work has shown that several members of the src family of protein tyrosine kinases (PTKs) are modified by palmitoylation, including p56lck and p59fyn but not p60src. Mapping of the sites of palmitoylation in p56lck identified cys3 as the major site and cys5 as a minor site of palmitoylation. A non-palmitoylated p56lck(cys3,5-->ser) mutant was localized exclusively in the cytoplasm despite the presence of amino-terminal myristoylation, thus indicating that palmitoylation of p56lck was necessary for membrane binding. The addition of a domain of six lysine residues to a non-palmitoylated p56lck mutant was sufficient to re-establish membrane binding but not to target the non-palmitoylated p56lck to caveolae. These results establish that two signals, myristoylation plus either palmitoylation or a polybasic domain, are necessary for membrane binding of src family PTKs.</description><subject>Amino Acid Sequence</subject><subject>Binding Sites</subject><subject>Cell Membrane - metabolism</subject><subject>Cysteine</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Lymphocyte Specific Protein Tyrosine Kinase p56(lck)</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis, Site-Directed</subject><subject>Myristic Acid</subject><subject>Myristic Acids - metabolism</subject><subject>Plasmids</subject><subject>Point Mutation</subject><subject>Protein-Tyrosine Kinases - biosynthesis</subject><subject>Protein-Tyrosine Kinases - chemistry</subject><subject>Protein-Tyrosine Kinases - metabolism</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - metabolism</subject><subject>Serine</subject><subject>Signal Transduction</subject><subject>Transfection</subject><issn>0006-291X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kDtPwzAUhT2ASimsbEj-Awl2nDrJWFW8pEosILFFflxXhtgOdooU8edJaMV0rq7O-YYPoRtKckoIv5Myqpw2zTqnBednaEmmb1Y09P0CXab0QQilJW8WaFHVvKxrtkQ_G2d9yAaIU4oO96JzdhAD4BBxH7pRimQV1sEJ67ESHvcxfFsNOMLXwUbQOIEKfgq7nwFDwG6MNv0xzARx4GQUHrC0Xlu_x8Hgfs079XmFzo3oElyfcoXeHu5ft0_Z7uXxebvZZYqyimVG8lozDlwbJmRtakVLKKtSy4opzsy6AAmqMYWm06WErnTDiGwKELouZMlWKD9yVQwpRTBtH60TcWwpaWdx7SyuncW1s7hpcHsc9AfpQP_XT9bYL1Qyb68</recordid><startdate>19950215</startdate><enddate>19950215</enddate><creator>Kwong, J</creator><creator>Lublin, D M</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>19950215</creationdate><title>Amino-terminal palmitate or polybasic domain can provide required second signal to myristate for membrane binding of p56lck</title><author>Kwong, J ; Lublin, D M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c1373-fb68d36e6df3ab8f8c14e474db73c63f52ebec9f2d12ebcad7d930b92ead82b43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Amino Acid Sequence</topic><topic>Binding Sites</topic><topic>Cell Membrane - metabolism</topic><topic>Cysteine</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Lymphocyte Specific Protein Tyrosine Kinase p56(lck)</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis, Site-Directed</topic><topic>Myristic Acid</topic><topic>Myristic Acids - metabolism</topic><topic>Plasmids</topic><topic>Point Mutation</topic><topic>Protein-Tyrosine Kinases - biosynthesis</topic><topic>Protein-Tyrosine Kinases - chemistry</topic><topic>Protein-Tyrosine Kinases - metabolism</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - metabolism</topic><topic>Serine</topic><topic>Signal Transduction</topic><topic>Transfection</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kwong, J</creatorcontrib><creatorcontrib>Lublin, D M</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kwong, J</au><au>Lublin, D M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Amino-terminal palmitate or polybasic domain can provide required second signal to myristate for membrane binding of p56lck</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1995-02-15</date><risdate>1995</risdate><volume>207</volume><issue>2</issue><spage>868</spage><epage>876</epage><pages>868-876</pages><issn>0006-291X</issn><abstract>Recent work has shown that several members of the src family of protein tyrosine kinases (PTKs) are modified by palmitoylation, including p56lck and p59fyn but not p60src. Mapping of the sites of palmitoylation in p56lck identified cys3 as the major site and cys5 as a minor site of palmitoylation. A non-palmitoylated p56lck(cys3,5-->ser) mutant was localized exclusively in the cytoplasm despite the presence of amino-terminal myristoylation, thus indicating that palmitoylation of p56lck was necessary for membrane binding. The addition of a domain of six lysine residues to a non-palmitoylated p56lck mutant was sufficient to re-establish membrane binding but not to target the non-palmitoylated p56lck to caveolae. These results establish that two signals, myristoylation plus either palmitoylation or a polybasic domain, are necessary for membrane binding of src family PTKs.</abstract><cop>United States</cop><pmid>7864883</pmid><doi>10.1006/bbrc.1995.1266</doi><tpages>9</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-291X |
| ispartof | Biochemical and biophysical research communications, 1995-02, Vol.207 (2), p.868-876 |
| issn | 0006-291X |
| language | eng |
| recordid | cdi_crossref_primary_10_1006_bbrc_1995_1266 |
| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Amino Acid Sequence Binding Sites Cell Membrane - metabolism Cysteine HeLa Cells Humans Lymphocyte Specific Protein Tyrosine Kinase p56(lck) Molecular Sequence Data Mutagenesis, Site-Directed Myristic Acid Myristic Acids - metabolism Plasmids Point Mutation Protein-Tyrosine Kinases - biosynthesis Protein-Tyrosine Kinases - chemistry Protein-Tyrosine Kinases - metabolism Recombinant Proteins - biosynthesis Recombinant Proteins - chemistry Recombinant Proteins - metabolism Serine Signal Transduction Transfection |
| title | Amino-terminal palmitate or polybasic domain can provide required second signal to myristate for membrane binding of p56lck |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-10T00%3A43%3A58IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-pubmed_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Amino-terminal%20palmitate%20or%20polybasic%20domain%20can%20provide%20required%20second%20signal%20to%20myristate%20for%20membrane%20binding%20of%20p56lck&rft.jtitle=Biochemical%20and%20biophysical%20research%20communications&rft.au=Kwong,%20J&rft.date=1995-02-15&rft.volume=207&rft.issue=2&rft.spage=868&rft.epage=876&rft.pages=868-876&rft.issn=0006-291X&rft_id=info:doi/10.1006/bbrc.1995.1266&rft_dat=%3Cpubmed_cross%3E7864883%3C/pubmed_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_id=info:pmid/7864883&rfr_iscdi=true |