Mapping of the p56^l^c^k-mediated phosphorylation of GAP and analysis of its influence on p21^r^a^s-GTPase activity in vitro
The protein tyrosine kinase p56^l^c^k and other members of the src family can transduce signals from activated cell-surface receptors. As we showed earlier the GTPase-activating protein (GAP), a regulator of p21^r^a^s, is a substrate of p56^l^c^k. Here, tryptic peptides of p56^l^c^k-phosphorylated G...
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E-Artikel |
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Englisch |
| Erschienen: |
1994 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
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| Übergeordnetes Werk: |
in: Biochimica et Biophysica Acta (BBA)/Molecular Cell Research - Amsterdam : Elsevier, 1222(1994), 3, Seite 441-446 |
| Übergeordnetes Werk: |
volume:1222 ; year:1994 ; number:3 ; pages:441-446 |
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| 245 | 1 | 0 | |a Mapping of the p56^l^c^k-mediated phosphorylation of GAP and analysis of its influence on p21^r^a^s-GTPase activity in vitro |
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| 520 | |a The protein tyrosine kinase p56^l^c^k and other members of the src family can transduce signals from activated cell-surface receptors. As we showed earlier the GTPase-activating protein (GAP), a regulator of p21^r^a^s, is a substrate of p56^l^c^k. Here, tryptic peptides of p56^l^c^k-phosphorylated GAP were generated and analyzed by two-dimensional thin layer chromatography and mass spectroscopy. Results revealed that p56^l^c^k phosphorylates GAP specifically on Tyr-460 in vitro and in vivo. The effect of tyrosine phosphorylation of GAP on its GTPase-activating activity versus p21^r^a^s was then tested using a p21^r^a^s-dependent GTPase assay system. Our results demonstrate that p56^l^c^k-mediated tyrosine phosphorylation of GAP is not sufficient to change directly its effect on the intrinsic GTPase activity of p21^r^a^s. | ||
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(DE-627)NLEJ186875096 (DE-599)GBVNLZ186875096 DE-627 ger DE-627 rakwb eng Mapping of the p56^l^c^k-mediated phosphorylation of GAP and analysis of its influence on p21^r^a^s-GTPase activity in vitro 1994 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The protein tyrosine kinase p56^l^c^k and other members of the src family can transduce signals from activated cell-surface receptors. As we showed earlier the GTPase-activating protein (GAP), a regulator of p21^r^a^s, is a substrate of p56^l^c^k. Here, tryptic peptides of p56^l^c^k-phosphorylated GAP were generated and analyzed by two-dimensional thin layer chromatography and mass spectroscopy. Results revealed that p56^l^c^k phosphorylates GAP specifically on Tyr-460 in vitro and in vivo. The effect of tyrosine phosphorylation of GAP on its GTPase-activating activity versus p21^r^a^s was then tested using a p21^r^a^s-dependent GTPase assay system. Our results demonstrate that p56^l^c^k-mediated tyrosine phosphorylation of GAP is not sufficient to change directly its effect on the intrinsic GTPase activity of p21^r^a^s. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Amrein, K.E. oth Panholzer, B. oth Molnos, J. oth Flint, N.A. oth Scheffler, J. oth Lahm, H.-W. oth Bannwarth, W. oth Burn, P. oth in Biochimica et Biophysica Acta (BBA)/Molecular Cell Research Amsterdam : Elsevier 1222(1994), 3, Seite 441-446 (DE-627)NLEJ186863756 (DE-600)2209512-3 0167-4889 nnns volume:1222 year:1994 number:3 pages:441-446 http://linkinghub.elsevier.com/retrieve/pii/0167-4889(94)90052-3 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 1222 1994 3 441-446 |
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(DE-627)NLEJ186875096 (DE-599)GBVNLZ186875096 DE-627 ger DE-627 rakwb eng Mapping of the p56^l^c^k-mediated phosphorylation of GAP and analysis of its influence on p21^r^a^s-GTPase activity in vitro 1994 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The protein tyrosine kinase p56^l^c^k and other members of the src family can transduce signals from activated cell-surface receptors. As we showed earlier the GTPase-activating protein (GAP), a regulator of p21^r^a^s, is a substrate of p56^l^c^k. Here, tryptic peptides of p56^l^c^k-phosphorylated GAP were generated and analyzed by two-dimensional thin layer chromatography and mass spectroscopy. Results revealed that p56^l^c^k phosphorylates GAP specifically on Tyr-460 in vitro and in vivo. The effect of tyrosine phosphorylation of GAP on its GTPase-activating activity versus p21^r^a^s was then tested using a p21^r^a^s-dependent GTPase assay system. Our results demonstrate that p56^l^c^k-mediated tyrosine phosphorylation of GAP is not sufficient to change directly its effect on the intrinsic GTPase activity of p21^r^a^s. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Amrein, K.E. oth Panholzer, B. oth Molnos, J. oth Flint, N.A. oth Scheffler, J. oth Lahm, H.-W. oth Bannwarth, W. oth Burn, P. oth in Biochimica et Biophysica Acta (BBA)/Molecular Cell Research Amsterdam : Elsevier 1222(1994), 3, Seite 441-446 (DE-627)NLEJ186863756 (DE-600)2209512-3 0167-4889 nnns volume:1222 year:1994 number:3 pages:441-446 http://linkinghub.elsevier.com/retrieve/pii/0167-4889(94)90052-3 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 1222 1994 3 441-446 |
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(DE-627)NLEJ186875096 (DE-599)GBVNLZ186875096 DE-627 ger DE-627 rakwb eng Mapping of the p56^l^c^k-mediated phosphorylation of GAP and analysis of its influence on p21^r^a^s-GTPase activity in vitro 1994 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The protein tyrosine kinase p56^l^c^k and other members of the src family can transduce signals from activated cell-surface receptors. As we showed earlier the GTPase-activating protein (GAP), a regulator of p21^r^a^s, is a substrate of p56^l^c^k. Here, tryptic peptides of p56^l^c^k-phosphorylated GAP were generated and analyzed by two-dimensional thin layer chromatography and mass spectroscopy. Results revealed that p56^l^c^k phosphorylates GAP specifically on Tyr-460 in vitro and in vivo. The effect of tyrosine phosphorylation of GAP on its GTPase-activating activity versus p21^r^a^s was then tested using a p21^r^a^s-dependent GTPase assay system. Our results demonstrate that p56^l^c^k-mediated tyrosine phosphorylation of GAP is not sufficient to change directly its effect on the intrinsic GTPase activity of p21^r^a^s. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Amrein, K.E. oth Panholzer, B. oth Molnos, J. oth Flint, N.A. oth Scheffler, J. oth Lahm, H.-W. oth Bannwarth, W. oth Burn, P. oth in Biochimica et Biophysica Acta (BBA)/Molecular Cell Research Amsterdam : Elsevier 1222(1994), 3, Seite 441-446 (DE-627)NLEJ186863756 (DE-600)2209512-3 0167-4889 nnns volume:1222 year:1994 number:3 pages:441-446 http://linkinghub.elsevier.com/retrieve/pii/0167-4889(94)90052-3 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 1222 1994 3 441-446 |
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(DE-627)NLEJ186875096 (DE-599)GBVNLZ186875096 DE-627 ger DE-627 rakwb eng Mapping of the p56^l^c^k-mediated phosphorylation of GAP and analysis of its influence on p21^r^a^s-GTPase activity in vitro 1994 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The protein tyrosine kinase p56^l^c^k and other members of the src family can transduce signals from activated cell-surface receptors. As we showed earlier the GTPase-activating protein (GAP), a regulator of p21^r^a^s, is a substrate of p56^l^c^k. Here, tryptic peptides of p56^l^c^k-phosphorylated GAP were generated and analyzed by two-dimensional thin layer chromatography and mass spectroscopy. Results revealed that p56^l^c^k phosphorylates GAP specifically on Tyr-460 in vitro and in vivo. The effect of tyrosine phosphorylation of GAP on its GTPase-activating activity versus p21^r^a^s was then tested using a p21^r^a^s-dependent GTPase assay system. Our results demonstrate that p56^l^c^k-mediated tyrosine phosphorylation of GAP is not sufficient to change directly its effect on the intrinsic GTPase activity of p21^r^a^s. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Amrein, K.E. oth Panholzer, B. oth Molnos, J. oth Flint, N.A. oth Scheffler, J. oth Lahm, H.-W. oth Bannwarth, W. oth Burn, P. oth in Biochimica et Biophysica Acta (BBA)/Molecular Cell Research Amsterdam : Elsevier 1222(1994), 3, Seite 441-446 (DE-627)NLEJ186863756 (DE-600)2209512-3 0167-4889 nnns volume:1222 year:1994 number:3 pages:441-446 http://linkinghub.elsevier.com/retrieve/pii/0167-4889(94)90052-3 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 1222 1994 3 441-446 |
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(DE-627)NLEJ186875096 (DE-599)GBVNLZ186875096 DE-627 ger DE-627 rakwb eng Mapping of the p56^l^c^k-mediated phosphorylation of GAP and analysis of its influence on p21^r^a^s-GTPase activity in vitro 1994 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The protein tyrosine kinase p56^l^c^k and other members of the src family can transduce signals from activated cell-surface receptors. As we showed earlier the GTPase-activating protein (GAP), a regulator of p21^r^a^s, is a substrate of p56^l^c^k. Here, tryptic peptides of p56^l^c^k-phosphorylated GAP were generated and analyzed by two-dimensional thin layer chromatography and mass spectroscopy. Results revealed that p56^l^c^k phosphorylates GAP specifically on Tyr-460 in vitro and in vivo. The effect of tyrosine phosphorylation of GAP on its GTPase-activating activity versus p21^r^a^s was then tested using a p21^r^a^s-dependent GTPase assay system. Our results demonstrate that p56^l^c^k-mediated tyrosine phosphorylation of GAP is not sufficient to change directly its effect on the intrinsic GTPase activity of p21^r^a^s. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Amrein, K.E. oth Panholzer, B. oth Molnos, J. oth Flint, N.A. oth Scheffler, J. oth Lahm, H.-W. oth Bannwarth, W. oth Burn, P. oth in Biochimica et Biophysica Acta (BBA)/Molecular Cell Research Amsterdam : Elsevier 1222(1994), 3, Seite 441-446 (DE-627)NLEJ186863756 (DE-600)2209512-3 0167-4889 nnns volume:1222 year:1994 number:3 pages:441-446 http://linkinghub.elsevier.com/retrieve/pii/0167-4889(94)90052-3 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 1222 1994 3 441-446 |
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mapping of the p56^l^c^k-mediated phosphorylation of gap and analysis of its influence on p21^r^a^s-gtpase activity in vitro |
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Mapping of the p56^l^c^k-mediated phosphorylation of GAP and analysis of its influence on p21^r^a^s-GTPase activity in vitro |
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The protein tyrosine kinase p56^l^c^k and other members of the src family can transduce signals from activated cell-surface receptors. As we showed earlier the GTPase-activating protein (GAP), a regulator of p21^r^a^s, is a substrate of p56^l^c^k. Here, tryptic peptides of p56^l^c^k-phosphorylated GAP were generated and analyzed by two-dimensional thin layer chromatography and mass spectroscopy. Results revealed that p56^l^c^k phosphorylates GAP specifically on Tyr-460 in vitro and in vivo. The effect of tyrosine phosphorylation of GAP on its GTPase-activating activity versus p21^r^a^s was then tested using a p21^r^a^s-dependent GTPase assay system. Our results demonstrate that p56^l^c^k-mediated tyrosine phosphorylation of GAP is not sufficient to change directly its effect on the intrinsic GTPase activity of p21^r^a^s. |
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The protein tyrosine kinase p56^l^c^k and other members of the src family can transduce signals from activated cell-surface receptors. As we showed earlier the GTPase-activating protein (GAP), a regulator of p21^r^a^s, is a substrate of p56^l^c^k. Here, tryptic peptides of p56^l^c^k-phosphorylated GAP were generated and analyzed by two-dimensional thin layer chromatography and mass spectroscopy. Results revealed that p56^l^c^k phosphorylates GAP specifically on Tyr-460 in vitro and in vivo. The effect of tyrosine phosphorylation of GAP on its GTPase-activating activity versus p21^r^a^s was then tested using a p21^r^a^s-dependent GTPase assay system. Our results demonstrate that p56^l^c^k-mediated tyrosine phosphorylation of GAP is not sufficient to change directly its effect on the intrinsic GTPase activity of p21^r^a^s. |
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The protein tyrosine kinase p56^l^c^k and other members of the src family can transduce signals from activated cell-surface receptors. As we showed earlier the GTPase-activating protein (GAP), a regulator of p21^r^a^s, is a substrate of p56^l^c^k. Here, tryptic peptides of p56^l^c^k-phosphorylated GAP were generated and analyzed by two-dimensional thin layer chromatography and mass spectroscopy. Results revealed that p56^l^c^k phosphorylates GAP specifically on Tyr-460 in vitro and in vivo. The effect of tyrosine phosphorylation of GAP on its GTPase-activating activity versus p21^r^a^s was then tested using a p21^r^a^s-dependent GTPase assay system. Our results demonstrate that p56^l^c^k-mediated tyrosine phosphorylation of GAP is not sufficient to change directly its effect on the intrinsic GTPase activity of p21^r^a^s. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ186875096</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707061812.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1994 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ186875096</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ186875096</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Mapping of the p56^l^c^k-mediated phosphorylation of GAP and analysis of its influence on p21^r^a^s-GTPase activity in vitro</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1994</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">The protein tyrosine kinase p56^l^c^k and other members of the src family can transduce signals from activated cell-surface receptors. As we showed earlier the GTPase-activating protein (GAP), a regulator of p21^r^a^s, is a substrate of p56^l^c^k. Here, tryptic peptides of p56^l^c^k-phosphorylated GAP were generated and analyzed by two-dimensional thin layer chromatography and mass spectroscopy. Results revealed that p56^l^c^k phosphorylates GAP specifically on Tyr-460 in vitro and in vivo. The effect of tyrosine phosphorylation of GAP on its GTPase-activating activity versus p21^r^a^s was then tested using a p21^r^a^s-dependent GTPase assay system. Our results demonstrate that p56^l^c^k-mediated tyrosine phosphorylation of GAP is not sufficient to change directly its effect on the intrinsic GTPase activity of p21^r^a^s.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Elsevier Journal Backfiles on ScienceDirect 1907 - 2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Amrein, K.E.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Panholzer, B.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Molnos, J.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Flint, N.A.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Scheffler, J.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Lahm, H.-W.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Bannwarth, W.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Burn, P.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Biochimica et Biophysica Acta (BBA)/Molecular Cell Research</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">1222(1994), 3, Seite 441-446</subfield><subfield code="w">(DE-627)NLEJ186863756</subfield><subfield code="w">(DE-600)2209512-3</subfield><subfield code="x">0167-4889</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:1222</subfield><subfield code="g">year:1994</subfield><subfield code="g">number:3</subfield><subfield code="g">pages:441-446</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://linkinghub.elsevier.com/retrieve/pii/0167-4889(94)90052-3</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_H</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-SDJ</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">1222</subfield><subfield code="j">1994</subfield><subfield code="e">3</subfield><subfield code="h">441-446</subfield></datafield></record></collection>
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