Optimization of the cellular import of functionally active SH2-domain-interacting phosphopeptides
Phosphopeptides interacting with src homology 2 (SH2) domains can activate essential signaling enzymes in vitro. When delivered to cells, they may disrupt protein-protein interactions, thereby influencing intracellular signaling. We showed earlier that phosphopeptides corresponding to the inhibitory...
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| Veröffentlicht in: | Cellular and molecular life sciences : CMLS 2006-11, Vol.63 (22), p.2682-2693 |
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| creator | Kertész, A Váradi, G Tóth, G K Fajka-Boja, R Monostori, E Sármay, G |
| description | Phosphopeptides interacting with src homology 2 (SH2) domains can activate essential signaling enzymes in vitro. When delivered to cells, they may disrupt protein-protein interactions, thereby influencing intracellular signaling. We showed earlier that phosphopeptides corresponding to the inhibitory motif of Fcgamma receptor IIb and a motif of the Grb2-associated binder 1 adaptor protein activate SH2-containing tyrosine phosphatase 2 in vitro. To study the ex vivo effects of these peptides, we have now compared different methods for peptide delivery: (i) permeabilization of the target cells and (ii) the use of cell-permeable vectors, which are potentially able to transport biologically active compounds into B cells. We found octanoyl-Arg(8) to be an optimal carrier for the delivery of phosphopeptides to the cells. With this strategy, the function of cell-permeable SHP-2-binding phosphopeptides was analyzed. These peptides modulated the protein phosphorylation in B cells in a dose- and time-dependent manner. |
| doi_str_mv | 10.1007/s00018-006-6346-6 |
| format | Article |
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When delivered to cells, they may disrupt protein-protein interactions, thereby influencing intracellular signaling. We showed earlier that phosphopeptides corresponding to the inhibitory motif of Fcgamma receptor IIb and a motif of the Grb2-associated binder 1 adaptor protein activate SH2-containing tyrosine phosphatase 2 in vitro. To study the ex vivo effects of these peptides, we have now compared different methods for peptide delivery: (i) permeabilization of the target cells and (ii) the use of cell-permeable vectors, which are potentially able to transport biologically active compounds into B cells. We found octanoyl-Arg(8) to be an optimal carrier for the delivery of phosphopeptides to the cells. With this strategy, the function of cell-permeable SHP-2-binding phosphopeptides was analyzed. These peptides modulated the protein phosphorylation in B cells in a dose- and time-dependent manner.</description><identifier>ISSN: 1420-682X</identifier><identifier>EISSN: 1420-9071</identifier><identifier>DOI: 10.1007/s00018-006-6346-6</identifier><identifier>PMID: 17075693</identifier><language>eng</language><publisher>Switzerland: Springer Nature B.V</publisher><subject>Adaptor Proteins, Signal Transducing - metabolism ; Amino Acid Motifs ; B-Lymphocytes - metabolism ; Burkitt Lymphoma - metabolism ; Cellular biology ; Enzymes ; Humans ; Peptides ; Permeability ; Phosphopeptides - chemistry ; Phosphopeptides - metabolism ; Phosphopeptides - pharmacology ; Phosphoproteins - metabolism ; Phosphorylation ; Phosphotyrosine - metabolism ; Signal Transduction ; src Homology Domains</subject><ispartof>Cellular and molecular life sciences : CMLS, 2006-11, Vol.63 (22), p.2682-2693</ispartof><rights>Birkhäuser Verlag, Basel 2006</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c425t-8267caf705fa556b5fef77a05ef061c1b6f7c013770ff0ae047c4c9a6e3d0f593</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC11136065/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC11136065/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17075693$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kertész, A</creatorcontrib><creatorcontrib>Váradi, G</creatorcontrib><creatorcontrib>Tóth, G K</creatorcontrib><creatorcontrib>Fajka-Boja, R</creatorcontrib><creatorcontrib>Monostori, E</creatorcontrib><creatorcontrib>Sármay, G</creatorcontrib><title>Optimization of the cellular import of functionally active SH2-domain-interacting phosphopeptides</title><title>Cellular and molecular life sciences : CMLS</title><addtitle>Cell Mol Life Sci</addtitle><description>Phosphopeptides interacting with src homology 2 (SH2) domains can activate essential signaling enzymes in vitro. 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These peptides modulated the protein phosphorylation in B cells in a dose- and time-dependent manner.</description><subject>Adaptor Proteins, Signal Transducing - metabolism</subject><subject>Amino Acid Motifs</subject><subject>B-Lymphocytes - metabolism</subject><subject>Burkitt Lymphoma - metabolism</subject><subject>Cellular biology</subject><subject>Enzymes</subject><subject>Humans</subject><subject>Peptides</subject><subject>Permeability</subject><subject>Phosphopeptides - chemistry</subject><subject>Phosphopeptides - metabolism</subject><subject>Phosphopeptides - pharmacology</subject><subject>Phosphoproteins - metabolism</subject><subject>Phosphorylation</subject><subject>Phosphotyrosine - metabolism</subject><subject>Signal Transduction</subject><subject>src Homology Domains</subject><issn>1420-682X</issn><issn>1420-9071</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNpdkd9LwzAQx4MoTqd_gC9SfPCtemmbpHsSGeqEwR5U8C1kabJltE1N2sH8601Z8ddDLsfdJ18u90XoAsMNBmC3HgBwHgPQmKZZCAfoBGcJxBNg-HDIaZ68j9Cp95sAkzyhx2iEGTBCJ-kJEoumNZX5FK2xdWR11K5VJFVZdqVwkaka69q-rLta9ogoy10kQrpV0cssiQtbCVPHpm6V68v1KmrW1ofTqKBcKH-GjrQovTof7jF6e3x4nc7i-eLpeXo_j2WWkDYOgzEpNAOiBSF0SbTSjAkgSgPFEi-pZhJwyhhoDUJBxmQmJ4KqtABNJukY3e11m25ZqUKqunWi5I0zlXA7boXhfzu1WfOV3XKMcUqBkqBwPSg4-9Ep3_LK-H4Xola285zmmIU15wG8-gdubOfCbjzv-xnDeRogvIeks947pb9HwcB7-_jePh7s4719IYzR5e8__LwY_Eq_AAbqmIo</recordid><startdate>20061101</startdate><enddate>20061101</enddate><creator>Kertész, A</creator><creator>Váradi, G</creator><creator>Tóth, G K</creator><creator>Fajka-Boja, R</creator><creator>Monostori, E</creator><creator>Sármay, G</creator><general>Springer Nature B.V</general><general>Birkhäuser-Verlag</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>3V.</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SS</scope><scope>7T5</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U7</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ATCPS</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>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PATMY</scope><scope>PHGZM</scope><scope>PHGZT</scope><scope>PJZUB</scope><scope>PKEHL</scope><scope>PPXIY</scope><scope>PQEST</scope><scope>PQGLB</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20061101</creationdate><title>Optimization of the cellular import of functionally active SH2-domain-interacting phosphopeptides</title><author>Kertész, A ; Váradi, G ; Tóth, G K ; Fajka-Boja, R ; Monostori, E ; Sármay, G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c425t-8267caf705fa556b5fef77a05ef061c1b6f7c013770ff0ae047c4c9a6e3d0f593</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Adaptor Proteins, Signal Transducing - 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| subjects | Adaptor Proteins, Signal Transducing - metabolism Amino Acid Motifs B-Lymphocytes - metabolism Burkitt Lymphoma - metabolism Cellular biology Enzymes Humans Peptides Permeability Phosphopeptides - chemistry Phosphopeptides - metabolism Phosphopeptides - pharmacology Phosphoproteins - metabolism Phosphorylation Phosphotyrosine - metabolism Signal Transduction src Homology Domains |
| title | Optimization of the cellular import of functionally active SH2-domain-interacting phosphopeptides |
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