Cbl-associated protein is tyrosine phosphorylated by c-Abl and c-Src kinases

Background The c-Cbl-associated protein (CAP), also known as ponsin, localizes to focal adhesions and stress fibers and is involved in signaling events. Phosphorylation has been described for the other two members of the sorbin homology family, vinexin and ArgBP2, but no data exist about the putativ...
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Autor*in:	Fernow, Inga [verfasserIn] Tomasovic, Ana Siehoff-Icking, Ann Tikkanen, Ritva

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2009

Schlagwörter:	Focal Adhesion Stress Fiber Cell Spreading Hep3B Cell Major Phosphorylation Site

Anmerkung:	© Fernow et al; licensee BioMed Central Ltd. 2009. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (

Übergeordnetes Werk:	Enthalten in: BMC cell biology - London : BioMed Central, 2000, 10(2009), 1 vom: 05. Nov.
Übergeordnetes Werk:	volume:10 ; year:2009 ; number:1 ; day:05 ; month:11

Links:	Volltext

DOI / URN:	10.1186/1471-2121-10-80

Katalog-ID:	SPR026935244

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520			\|a Background The c-Cbl-associated protein (CAP), also known as ponsin, localizes to focal adhesions and stress fibers and is involved in signaling events. Phosphorylation has been described for the other two members of the sorbin homology family, vinexin and ArgBP2, but no data exist about the putative phosphorylation of CAP. According to previous findings, CAP binds to tyrosine kinase c-Abl. However, it is not known if CAP is a substrate of c-Abl or other tyrosine kinases or if phosphorylation regulates its localization. Results We here show that CAP is Tyr phosphorylated by and interacts with both c-Abl and c-Src. One major phosphorylation site, Tyr360, and two minor contributors Tyr326 and Tyr632 were identified as Abl phosphorylation sites, whereas Src preferentially phosphorylates Tyr326 and Tyr360. Phosphorylation of CAP was not necessary for its localization to focal adhesions and stress fibers, but Tyr326Phe substitution alters the function of CAP during cell spreading. Conclusion This is the first demonstration of phosphorylation of CAP by any kinase. Our findings suggest that coordinated action of Src and Abl might regulate the function of CAP and reveal a functional role especially for the Src-mediated Tyr phosphorylation of CAP in cell spreading.
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Indexfelder

author_variant	i f if a t at a s i asi r t rt
matchkey_str	article:14712121:2009----::bascaepoensyoiehshrltdya
hierarchy_sort_str	2009
publishDate	2009
allfields	10.1186/1471-2121-10-80 doi (DE-627)SPR026935244 (SPR)1471-2121-10-80-e DE-627 ger DE-627 rakwb eng Fernow, Inga verfasserin aut Cbl-associated protein is tyrosine phosphorylated by c-Abl and c-Src kinases 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Fernow et al; licensee BioMed Central Ltd. 2009. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( Background The c-Cbl-associated protein (CAP), also known as ponsin, localizes to focal adhesions and stress fibers and is involved in signaling events. Phosphorylation has been described for the other two members of the sorbin homology family, vinexin and ArgBP2, but no data exist about the putative phosphorylation of CAP. According to previous findings, CAP binds to tyrosine kinase c-Abl. However, it is not known if CAP is a substrate of c-Abl or other tyrosine kinases or if phosphorylation regulates its localization. Results We here show that CAP is Tyr phosphorylated by and interacts with both c-Abl and c-Src. One major phosphorylation site, Tyr360, and two minor contributors Tyr326 and Tyr632 were identified as Abl phosphorylation sites, whereas Src preferentially phosphorylates Tyr326 and Tyr360. Phosphorylation of CAP was not necessary for its localization to focal adhesions and stress fibers, but Tyr326Phe substitution alters the function of CAP during cell spreading. Conclusion This is the first demonstration of phosphorylation of CAP by any kinase. Our findings suggest that coordinated action of Src and Abl might regulate the function of CAP and reveal a functional role especially for the Src-mediated Tyr phosphorylation of CAP in cell spreading. Focal Adhesion (dpeaa)DE-He213 Stress Fiber (dpeaa)DE-He213 Cell Spreading (dpeaa)DE-He213 Hep3B Cell (dpeaa)DE-He213 Major Phosphorylation Site (dpeaa)DE-He213 Tomasovic, Ana aut Siehoff-Icking, Ann aut Tikkanen, Ritva aut Enthalten in BMC cell biology London : BioMed Central, 2000 10(2009), 1 vom: 05. Nov. (DE-627)326644830 (DE-600)2041486-9 1471-2121 nnns volume:10 year:2009 number:1 day:05 month:11 https://dx.doi.org/10.1186/1471-2121-10-80 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 10 2009 1 05 11
spelling	10.1186/1471-2121-10-80 doi (DE-627)SPR026935244 (SPR)1471-2121-10-80-e DE-627 ger DE-627 rakwb eng Fernow, Inga verfasserin aut Cbl-associated protein is tyrosine phosphorylated by c-Abl and c-Src kinases 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Fernow et al; licensee BioMed Central Ltd. 2009. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( Background The c-Cbl-associated protein (CAP), also known as ponsin, localizes to focal adhesions and stress fibers and is involved in signaling events. Phosphorylation has been described for the other two members of the sorbin homology family, vinexin and ArgBP2, but no data exist about the putative phosphorylation of CAP. According to previous findings, CAP binds to tyrosine kinase c-Abl. However, it is not known if CAP is a substrate of c-Abl or other tyrosine kinases or if phosphorylation regulates its localization. Results We here show that CAP is Tyr phosphorylated by and interacts with both c-Abl and c-Src. One major phosphorylation site, Tyr360, and two minor contributors Tyr326 and Tyr632 were identified as Abl phosphorylation sites, whereas Src preferentially phosphorylates Tyr326 and Tyr360. Phosphorylation of CAP was not necessary for its localization to focal adhesions and stress fibers, but Tyr326Phe substitution alters the function of CAP during cell spreading. Conclusion This is the first demonstration of phosphorylation of CAP by any kinase. Our findings suggest that coordinated action of Src and Abl might regulate the function of CAP and reveal a functional role especially for the Src-mediated Tyr phosphorylation of CAP in cell spreading. Focal Adhesion (dpeaa)DE-He213 Stress Fiber (dpeaa)DE-He213 Cell Spreading (dpeaa)DE-He213 Hep3B Cell (dpeaa)DE-He213 Major Phosphorylation Site (dpeaa)DE-He213 Tomasovic, Ana aut Siehoff-Icking, Ann aut Tikkanen, Ritva aut Enthalten in BMC cell biology London : BioMed Central, 2000 10(2009), 1 vom: 05. Nov. (DE-627)326644830 (DE-600)2041486-9 1471-2121 nnns volume:10 year:2009 number:1 day:05 month:11 https://dx.doi.org/10.1186/1471-2121-10-80 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 10 2009 1 05 11
allfields_unstemmed	10.1186/1471-2121-10-80 doi (DE-627)SPR026935244 (SPR)1471-2121-10-80-e DE-627 ger DE-627 rakwb eng Fernow, Inga verfasserin aut Cbl-associated protein is tyrosine phosphorylated by c-Abl and c-Src kinases 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Fernow et al; licensee BioMed Central Ltd. 2009. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( Background The c-Cbl-associated protein (CAP), also known as ponsin, localizes to focal adhesions and stress fibers and is involved in signaling events. Phosphorylation has been described for the other two members of the sorbin homology family, vinexin and ArgBP2, but no data exist about the putative phosphorylation of CAP. According to previous findings, CAP binds to tyrosine kinase c-Abl. However, it is not known if CAP is a substrate of c-Abl or other tyrosine kinases or if phosphorylation regulates its localization. Results We here show that CAP is Tyr phosphorylated by and interacts with both c-Abl and c-Src. One major phosphorylation site, Tyr360, and two minor contributors Tyr326 and Tyr632 were identified as Abl phosphorylation sites, whereas Src preferentially phosphorylates Tyr326 and Tyr360. Phosphorylation of CAP was not necessary for its localization to focal adhesions and stress fibers, but Tyr326Phe substitution alters the function of CAP during cell spreading. Conclusion This is the first demonstration of phosphorylation of CAP by any kinase. Our findings suggest that coordinated action of Src and Abl might regulate the function of CAP and reveal a functional role especially for the Src-mediated Tyr phosphorylation of CAP in cell spreading. Focal Adhesion (dpeaa)DE-He213 Stress Fiber (dpeaa)DE-He213 Cell Spreading (dpeaa)DE-He213 Hep3B Cell (dpeaa)DE-He213 Major Phosphorylation Site (dpeaa)DE-He213 Tomasovic, Ana aut Siehoff-Icking, Ann aut Tikkanen, Ritva aut Enthalten in BMC cell biology London : BioMed Central, 2000 10(2009), 1 vom: 05. Nov. (DE-627)326644830 (DE-600)2041486-9 1471-2121 nnns volume:10 year:2009 number:1 day:05 month:11 https://dx.doi.org/10.1186/1471-2121-10-80 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 10 2009 1 05 11
allfieldsGer	10.1186/1471-2121-10-80 doi (DE-627)SPR026935244 (SPR)1471-2121-10-80-e DE-627 ger DE-627 rakwb eng Fernow, Inga verfasserin aut Cbl-associated protein is tyrosine phosphorylated by c-Abl and c-Src kinases 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Fernow et al; licensee BioMed Central Ltd. 2009. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( Background The c-Cbl-associated protein (CAP), also known as ponsin, localizes to focal adhesions and stress fibers and is involved in signaling events. Phosphorylation has been described for the other two members of the sorbin homology family, vinexin and ArgBP2, but no data exist about the putative phosphorylation of CAP. According to previous findings, CAP binds to tyrosine kinase c-Abl. However, it is not known if CAP is a substrate of c-Abl or other tyrosine kinases or if phosphorylation regulates its localization. Results We here show that CAP is Tyr phosphorylated by and interacts with both c-Abl and c-Src. One major phosphorylation site, Tyr360, and two minor contributors Tyr326 and Tyr632 were identified as Abl phosphorylation sites, whereas Src preferentially phosphorylates Tyr326 and Tyr360. Phosphorylation of CAP was not necessary for its localization to focal adhesions and stress fibers, but Tyr326Phe substitution alters the function of CAP during cell spreading. Conclusion This is the first demonstration of phosphorylation of CAP by any kinase. Our findings suggest that coordinated action of Src and Abl might regulate the function of CAP and reveal a functional role especially for the Src-mediated Tyr phosphorylation of CAP in cell spreading. Focal Adhesion (dpeaa)DE-He213 Stress Fiber (dpeaa)DE-He213 Cell Spreading (dpeaa)DE-He213 Hep3B Cell (dpeaa)DE-He213 Major Phosphorylation Site (dpeaa)DE-He213 Tomasovic, Ana aut Siehoff-Icking, Ann aut Tikkanen, Ritva aut Enthalten in BMC cell biology London : BioMed Central, 2000 10(2009), 1 vom: 05. Nov. (DE-627)326644830 (DE-600)2041486-9 1471-2121 nnns volume:10 year:2009 number:1 day:05 month:11 https://dx.doi.org/10.1186/1471-2121-10-80 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 10 2009 1 05 11
allfieldsSound	10.1186/1471-2121-10-80 doi (DE-627)SPR026935244 (SPR)1471-2121-10-80-e DE-627 ger DE-627 rakwb eng Fernow, Inga verfasserin aut Cbl-associated protein is tyrosine phosphorylated by c-Abl and c-Src kinases 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Fernow et al; licensee BioMed Central Ltd. 2009. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( Background The c-Cbl-associated protein (CAP), also known as ponsin, localizes to focal adhesions and stress fibers and is involved in signaling events. Phosphorylation has been described for the other two members of the sorbin homology family, vinexin and ArgBP2, but no data exist about the putative phosphorylation of CAP. According to previous findings, CAP binds to tyrosine kinase c-Abl. However, it is not known if CAP is a substrate of c-Abl or other tyrosine kinases or if phosphorylation regulates its localization. Results We here show that CAP is Tyr phosphorylated by and interacts with both c-Abl and c-Src. One major phosphorylation site, Tyr360, and two minor contributors Tyr326 and Tyr632 were identified as Abl phosphorylation sites, whereas Src preferentially phosphorylates Tyr326 and Tyr360. Phosphorylation of CAP was not necessary for its localization to focal adhesions and stress fibers, but Tyr326Phe substitution alters the function of CAP during cell spreading. Conclusion This is the first demonstration of phosphorylation of CAP by any kinase. Our findings suggest that coordinated action of Src and Abl might regulate the function of CAP and reveal a functional role especially for the Src-mediated Tyr phosphorylation of CAP in cell spreading. Focal Adhesion (dpeaa)DE-He213 Stress Fiber (dpeaa)DE-He213 Cell Spreading (dpeaa)DE-He213 Hep3B Cell (dpeaa)DE-He213 Major Phosphorylation Site (dpeaa)DE-He213 Tomasovic, Ana aut Siehoff-Icking, Ann aut Tikkanen, Ritva aut Enthalten in BMC cell biology London : BioMed Central, 2000 10(2009), 1 vom: 05. Nov. (DE-627)326644830 (DE-600)2041486-9 1471-2121 nnns volume:10 year:2009 number:1 day:05 month:11 https://dx.doi.org/10.1186/1471-2121-10-80 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 10 2009 1 05 11
language	English
source	Enthalten in BMC cell biology 10(2009), 1 vom: 05. Nov. volume:10 year:2009 number:1 day:05 month:11
sourceStr	Enthalten in BMC cell biology 10(2009), 1 vom: 05. Nov. volume:10 year:2009 number:1 day:05 month:11
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Focal Adhesion Stress Fiber Cell Spreading Hep3B Cell Major Phosphorylation Site
isfreeaccess_bool	true
container_title	BMC cell biology
authorswithroles_txt_mv	Fernow, Inga @@aut@@ Tomasovic, Ana @@aut@@ Siehoff-Icking, Ann @@aut@@ Tikkanen, Ritva @@aut@@
publishDateDaySort_date	2009-11-05T00:00:00Z
hierarchy_top_id	326644830
id	SPR026935244
language_de	englisch
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author	Fernow, Inga
spellingShingle	Fernow, Inga misc Focal Adhesion misc Stress Fiber misc Cell Spreading misc Hep3B Cell misc Major Phosphorylation Site Cbl-associated protein is tyrosine phosphorylated by c-Abl and c-Src kinases
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topic_title	Cbl-associated protein is tyrosine phosphorylated by c-Abl and c-Src kinases Focal Adhesion (dpeaa)DE-He213 Stress Fiber (dpeaa)DE-He213 Cell Spreading (dpeaa)DE-He213 Hep3B Cell (dpeaa)DE-He213 Major Phosphorylation Site (dpeaa)DE-He213
topic	misc Focal Adhesion misc Stress Fiber misc Cell Spreading misc Hep3B Cell misc Major Phosphorylation Site
topic_unstemmed	misc Focal Adhesion misc Stress Fiber misc Cell Spreading misc Hep3B Cell misc Major Phosphorylation Site
topic_browse	misc Focal Adhesion misc Stress Fiber misc Cell Spreading misc Hep3B Cell misc Major Phosphorylation Site
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title	Cbl-associated protein is tyrosine phosphorylated by c-Abl and c-Src kinases
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title_full	Cbl-associated protein is tyrosine phosphorylated by c-Abl and c-Src kinases
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journal	BMC cell biology
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title_sort	cbl-associated protein is tyrosine phosphorylated by c-abl and c-src kinases
title_auth	Cbl-associated protein is tyrosine phosphorylated by c-Abl and c-Src kinases
abstract	Background The c-Cbl-associated protein (CAP), also known as ponsin, localizes to focal adhesions and stress fibers and is involved in signaling events. Phosphorylation has been described for the other two members of the sorbin homology family, vinexin and ArgBP2, but no data exist about the putative phosphorylation of CAP. According to previous findings, CAP binds to tyrosine kinase c-Abl. However, it is not known if CAP is a substrate of c-Abl or other tyrosine kinases or if phosphorylation regulates its localization. Results We here show that CAP is Tyr phosphorylated by and interacts with both c-Abl and c-Src. One major phosphorylation site, Tyr360, and two minor contributors Tyr326 and Tyr632 were identified as Abl phosphorylation sites, whereas Src preferentially phosphorylates Tyr326 and Tyr360. Phosphorylation of CAP was not necessary for its localization to focal adhesions and stress fibers, but Tyr326Phe substitution alters the function of CAP during cell spreading. Conclusion This is the first demonstration of phosphorylation of CAP by any kinase. Our findings suggest that coordinated action of Src and Abl might regulate the function of CAP and reveal a functional role especially for the Src-mediated Tyr phosphorylation of CAP in cell spreading. © Fernow et al; licensee BioMed Central Ltd. 2009. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (
abstractGer	Background The c-Cbl-associated protein (CAP), also known as ponsin, localizes to focal adhesions and stress fibers and is involved in signaling events. Phosphorylation has been described for the other two members of the sorbin homology family, vinexin and ArgBP2, but no data exist about the putative phosphorylation of CAP. According to previous findings, CAP binds to tyrosine kinase c-Abl. However, it is not known if CAP is a substrate of c-Abl or other tyrosine kinases or if phosphorylation regulates its localization. Results We here show that CAP is Tyr phosphorylated by and interacts with both c-Abl and c-Src. One major phosphorylation site, Tyr360, and two minor contributors Tyr326 and Tyr632 were identified as Abl phosphorylation sites, whereas Src preferentially phosphorylates Tyr326 and Tyr360. Phosphorylation of CAP was not necessary for its localization to focal adhesions and stress fibers, but Tyr326Phe substitution alters the function of CAP during cell spreading. Conclusion This is the first demonstration of phosphorylation of CAP by any kinase. Our findings suggest that coordinated action of Src and Abl might regulate the function of CAP and reveal a functional role especially for the Src-mediated Tyr phosphorylation of CAP in cell spreading. © Fernow et al; licensee BioMed Central Ltd. 2009. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (
abstract_unstemmed	Background The c-Cbl-associated protein (CAP), also known as ponsin, localizes to focal adhesions and stress fibers and is involved in signaling events. Phosphorylation has been described for the other two members of the sorbin homology family, vinexin and ArgBP2, but no data exist about the putative phosphorylation of CAP. According to previous findings, CAP binds to tyrosine kinase c-Abl. However, it is not known if CAP is a substrate of c-Abl or other tyrosine kinases or if phosphorylation regulates its localization. Results We here show that CAP is Tyr phosphorylated by and interacts with both c-Abl and c-Src. One major phosphorylation site, Tyr360, and two minor contributors Tyr326 and Tyr632 were identified as Abl phosphorylation sites, whereas Src preferentially phosphorylates Tyr326 and Tyr360. Phosphorylation of CAP was not necessary for its localization to focal adhesions and stress fibers, but Tyr326Phe substitution alters the function of CAP during cell spreading. Conclusion This is the first demonstration of phosphorylation of CAP by any kinase. Our findings suggest that coordinated action of Src and Abl might regulate the function of CAP and reveal a functional role especially for the Src-mediated Tyr phosphorylation of CAP in cell spreading. © Fernow et al; licensee BioMed Central Ltd. 2009. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (
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title_short	Cbl-associated protein is tyrosine phosphorylated by c-Abl and c-Src kinases
url	https://dx.doi.org/10.1186/1471-2121-10-80
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author2	Tomasovic, Ana Siehoff-Icking, Ann Tikkanen, Ritva
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up_date	2024-07-03T23:32:06.692Z
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Cbl-associated protein is tyrosine phosphorylated by c-Abl and c-Src kinases

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Zugang & Verfügbarkeit

Vorhandene Bände

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