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Acetylation within the N- and C-Terminal Domains of Src Regulates Distinct Roles of STAT3-Mediated Tumorigenesis
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| Zeitschriftentitel: | Cancer Research |
|---|---|
| Personen und Körperschaften: | , , , , , , , , , , , , , |
| In: | Cancer Research, 78, 2018, 11, S. 2825-2838 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
American Association for Cancer Research (AACR)
|
| Schlagwörter: |
| author_facet |
Huang, Chao Zhang, Zhe Chen, Lihan Lee, Hank W. Ayrapetov, Marina K. Zhao, Ting C. Hao, Yimei Gao, Jinsong Yang, Chunzhang Mehta, Gautam U. Zhuang, Zhengping Zhang, Xiaoren Hu, Guohong Chin, Y. Eugene Huang, Chao Zhang, Zhe Chen, Lihan Lee, Hank W. Ayrapetov, Marina K. Zhao, Ting C. Hao, Yimei Gao, Jinsong Yang, Chunzhang Mehta, Gautam U. Zhuang, Zhengping Zhang, Xiaoren Hu, Guohong Chin, Y. Eugene |
|---|---|
| author |
Huang, Chao Zhang, Zhe Chen, Lihan Lee, Hank W. Ayrapetov, Marina K. Zhao, Ting C. Hao, Yimei Gao, Jinsong Yang, Chunzhang Mehta, Gautam U. Zhuang, Zhengping Zhang, Xiaoren Hu, Guohong Chin, Y. Eugene |
| spellingShingle |
Huang, Chao Zhang, Zhe Chen, Lihan Lee, Hank W. Ayrapetov, Marina K. Zhao, Ting C. Hao, Yimei Gao, Jinsong Yang, Chunzhang Mehta, Gautam U. Zhuang, Zhengping Zhang, Xiaoren Hu, Guohong Chin, Y. Eugene Cancer Research Acetylation within the N- and C-Terminal Domains of Src Regulates Distinct Roles of STAT3-Mediated Tumorigenesis Cancer Research Oncology |
| author_sort |
huang, chao |
| spelling |
Huang, Chao Zhang, Zhe Chen, Lihan Lee, Hank W. Ayrapetov, Marina K. Zhao, Ting C. Hao, Yimei Gao, Jinsong Yang, Chunzhang Mehta, Gautam U. Zhuang, Zhengping Zhang, Xiaoren Hu, Guohong Chin, Y. Eugene 0008-5472 1538-7445 American Association for Cancer Research (AACR) Cancer Research Oncology http://dx.doi.org/10.1158/0008-5472.can-17-2314 <jats:title>Abstract</jats:title> <jats:p>Posttranslational modifications of mammalian c-Src N-terminal and C-terminal domains regulate distinct functions. Myristoylation of G2 controls its cell membrane association and phosphorylation of Y419/Y527 controls its activation or inactivation, respectively. We provide evidence that Src–cell membrane association–dissociation and catalytic activation–inactivation are both regulated by acetylation. In EGF-treated cells, CREB binding protein (CBP) acetylates an N-terminal lysine cluster (K5, K7, and K9) of c-Src to promote dissociation from the cell membrane. CBP also acetylates the C-terminal K401, K423, and K427 of c-Src to activate intrinsic kinase activity for STAT3 recruitment and activation. N-terminal domain phosphorylation (Y14, Y45, and Y68) of STAT3 by c-Src activates transcriptionally active dimers of STAT3. Moreover, acetyl-Src translocates into nuclei, where it forms the Src-STAT3 enhanceosome for gene regulation and cancer cell proliferation. Thus, c-Src acetylation in the N-terminal and C-terminal domains play distinct roles in Src activity and regulation.</jats:p> <jats:p>Significance: CBP-mediated acetylation of lysine clusters in both the N-terminal and C-terminal regions of c-Src provides additional levels of control over STAT3 transcriptional activity. Cancer Res; 78(11); 2825–38. ©2018 AACR.</jats:p> Acetylation within the N- and C-Terminal Domains of Src Regulates Distinct Roles of STAT3-Mediated Tumorigenesis Cancer Research |
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10.1158/0008-5472.can-17-2314 |
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American Association for Cancer Research (AACR), 2018 |
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American Association for Cancer Research (AACR), 2018 |
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0008-5472 1538-7445 |
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| title |
Acetylation within the N- and C-Terminal Domains of Src Regulates Distinct Roles of STAT3-Mediated Tumorigenesis |
| title_unstemmed |
Acetylation within the N- and C-Terminal Domains of Src Regulates Distinct Roles of STAT3-Mediated Tumorigenesis |
| title_full |
Acetylation within the N- and C-Terminal Domains of Src Regulates Distinct Roles of STAT3-Mediated Tumorigenesis |
| title_fullStr |
Acetylation within the N- and C-Terminal Domains of Src Regulates Distinct Roles of STAT3-Mediated Tumorigenesis |
| title_full_unstemmed |
Acetylation within the N- and C-Terminal Domains of Src Regulates Distinct Roles of STAT3-Mediated Tumorigenesis |
| title_short |
Acetylation within the N- and C-Terminal Domains of Src Regulates Distinct Roles of STAT3-Mediated Tumorigenesis |
| title_sort |
acetylation within the n- and c-terminal domains of src regulates distinct roles of stat3-mediated tumorigenesis |
| topic |
Cancer Research Oncology |
| url |
http://dx.doi.org/10.1158/0008-5472.can-17-2314 |
| publishDate |
2018 |
| physical |
2825-2838 |
| description |
<jats:title>Abstract</jats:title>
<jats:p>Posttranslational modifications of mammalian c-Src N-terminal and C-terminal domains regulate distinct functions. Myristoylation of G2 controls its cell membrane association and phosphorylation of Y419/Y527 controls its activation or inactivation, respectively. We provide evidence that Src–cell membrane association–dissociation and catalytic activation–inactivation are both regulated by acetylation. In EGF-treated cells, CREB binding protein (CBP) acetylates an N-terminal lysine cluster (K5, K7, and K9) of c-Src to promote dissociation from the cell membrane. CBP also acetylates the C-terminal K401, K423, and K427 of c-Src to activate intrinsic kinase activity for STAT3 recruitment and activation. N-terminal domain phosphorylation (Y14, Y45, and Y68) of STAT3 by c-Src activates transcriptionally active dimers of STAT3. Moreover, acetyl-Src translocates into nuclei, where it forms the Src-STAT3 enhanceosome for gene regulation and cancer cell proliferation. Thus, c-Src acetylation in the N-terminal and C-terminal domains play distinct roles in Src activity and regulation.</jats:p>
<jats:p>Significance: CBP-mediated acetylation of lysine clusters in both the N-terminal and C-terminal regions of c-Src provides additional levels of control over STAT3 transcriptional activity. Cancer Res; 78(11); 2825–38. ©2018 AACR.</jats:p> |
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| author | Huang, Chao, Zhang, Zhe, Chen, Lihan, Lee, Hank W., Ayrapetov, Marina K., Zhao, Ting C., Hao, Yimei, Gao, Jinsong, Yang, Chunzhang, Mehta, Gautam U., Zhuang, Zhengping, Zhang, Xiaoren, Hu, Guohong, Chin, Y. Eugene |
| author_facet | Huang, Chao, Zhang, Zhe, Chen, Lihan, Lee, Hank W., Ayrapetov, Marina K., Zhao, Ting C., Hao, Yimei, Gao, Jinsong, Yang, Chunzhang, Mehta, Gautam U., Zhuang, Zhengping, Zhang, Xiaoren, Hu, Guohong, Chin, Y. Eugene, Huang, Chao, Zhang, Zhe, Chen, Lihan, Lee, Hank W., Ayrapetov, Marina K., Zhao, Ting C., Hao, Yimei, Gao, Jinsong, Yang, Chunzhang, Mehta, Gautam U., Zhuang, Zhengping, Zhang, Xiaoren, Hu, Guohong, Chin, Y. Eugene |
| author_sort | huang, chao |
| container_issue | 11 |
| container_start_page | 2825 |
| container_title | Cancer Research |
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| description | <jats:title>Abstract</jats:title> <jats:p>Posttranslational modifications of mammalian c-Src N-terminal and C-terminal domains regulate distinct functions. Myristoylation of G2 controls its cell membrane association and phosphorylation of Y419/Y527 controls its activation or inactivation, respectively. We provide evidence that Src–cell membrane association–dissociation and catalytic activation–inactivation are both regulated by acetylation. In EGF-treated cells, CREB binding protein (CBP) acetylates an N-terminal lysine cluster (K5, K7, and K9) of c-Src to promote dissociation from the cell membrane. CBP also acetylates the C-terminal K401, K423, and K427 of c-Src to activate intrinsic kinase activity for STAT3 recruitment and activation. N-terminal domain phosphorylation (Y14, Y45, and Y68) of STAT3 by c-Src activates transcriptionally active dimers of STAT3. Moreover, acetyl-Src translocates into nuclei, where it forms the Src-STAT3 enhanceosome for gene regulation and cancer cell proliferation. Thus, c-Src acetylation in the N-terminal and C-terminal domains play distinct roles in Src activity and regulation.</jats:p> <jats:p>Significance: CBP-mediated acetylation of lysine clusters in both the N-terminal and C-terminal regions of c-Src provides additional levels of control over STAT3 transcriptional activity. Cancer Res; 78(11); 2825–38. ©2018 AACR.</jats:p> |
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| imprint | American Association for Cancer Research (AACR), 2018 |
| imprint_str_mv | American Association for Cancer Research (AACR), 2018 |
| institution | DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229 |
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| spelling | Huang, Chao Zhang, Zhe Chen, Lihan Lee, Hank W. Ayrapetov, Marina K. Zhao, Ting C. Hao, Yimei Gao, Jinsong Yang, Chunzhang Mehta, Gautam U. Zhuang, Zhengping Zhang, Xiaoren Hu, Guohong Chin, Y. Eugene 0008-5472 1538-7445 American Association for Cancer Research (AACR) Cancer Research Oncology http://dx.doi.org/10.1158/0008-5472.can-17-2314 <jats:title>Abstract</jats:title> <jats:p>Posttranslational modifications of mammalian c-Src N-terminal and C-terminal domains regulate distinct functions. Myristoylation of G2 controls its cell membrane association and phosphorylation of Y419/Y527 controls its activation or inactivation, respectively. We provide evidence that Src–cell membrane association–dissociation and catalytic activation–inactivation are both regulated by acetylation. In EGF-treated cells, CREB binding protein (CBP) acetylates an N-terminal lysine cluster (K5, K7, and K9) of c-Src to promote dissociation from the cell membrane. CBP also acetylates the C-terminal K401, K423, and K427 of c-Src to activate intrinsic kinase activity for STAT3 recruitment and activation. N-terminal domain phosphorylation (Y14, Y45, and Y68) of STAT3 by c-Src activates transcriptionally active dimers of STAT3. Moreover, acetyl-Src translocates into nuclei, where it forms the Src-STAT3 enhanceosome for gene regulation and cancer cell proliferation. Thus, c-Src acetylation in the N-terminal and C-terminal domains play distinct roles in Src activity and regulation.</jats:p> <jats:p>Significance: CBP-mediated acetylation of lysine clusters in both the N-terminal and C-terminal regions of c-Src provides additional levels of control over STAT3 transcriptional activity. Cancer Res; 78(11); 2825–38. ©2018 AACR.</jats:p> Acetylation within the N- and C-Terminal Domains of Src Regulates Distinct Roles of STAT3-Mediated Tumorigenesis Cancer Research |
| spellingShingle | Huang, Chao, Zhang, Zhe, Chen, Lihan, Lee, Hank W., Ayrapetov, Marina K., Zhao, Ting C., Hao, Yimei, Gao, Jinsong, Yang, Chunzhang, Mehta, Gautam U., Zhuang, Zhengping, Zhang, Xiaoren, Hu, Guohong, Chin, Y. Eugene, Cancer Research, Acetylation within the N- and C-Terminal Domains of Src Regulates Distinct Roles of STAT3-Mediated Tumorigenesis, Cancer Research, Oncology |
| title | Acetylation within the N- and C-Terminal Domains of Src Regulates Distinct Roles of STAT3-Mediated Tumorigenesis |
| title_full | Acetylation within the N- and C-Terminal Domains of Src Regulates Distinct Roles of STAT3-Mediated Tumorigenesis |
| title_fullStr | Acetylation within the N- and C-Terminal Domains of Src Regulates Distinct Roles of STAT3-Mediated Tumorigenesis |
| title_full_unstemmed | Acetylation within the N- and C-Terminal Domains of Src Regulates Distinct Roles of STAT3-Mediated Tumorigenesis |
| title_short | Acetylation within the N- and C-Terminal Domains of Src Regulates Distinct Roles of STAT3-Mediated Tumorigenesis |
| title_sort | acetylation within the n- and c-terminal domains of src regulates distinct roles of stat3-mediated tumorigenesis |
| title_unstemmed | Acetylation within the N- and C-Terminal Domains of Src Regulates Distinct Roles of STAT3-Mediated Tumorigenesis |
| topic | Cancer Research, Oncology |
| url | http://dx.doi.org/10.1158/0008-5472.can-17-2314 |