publication . Article . 2014

The SH2 Domain Regulates c-Abl Kinase Activation by a Cyclin-Like Mechanism and Remodulation of the Hinge Motion

Giulio Superti-Furga; Francesco Luigi Gervasio; Ludovico Sutto; Maria Górna; Antonio Sánchez Torralba;
Open Access English
  • Published: 09 Oct 2014
  • Country: United Kingdom
Abstract
Author Summary The Abl kinase is a key player in many crucial cellular processes. It is also an important anti-cancer drug target, because a mutation leading to the fusion protein Bcr-Abl is the main cause for chronic myeloid leukemia (CML). Abl inhibitors are currently the only pharmaceutical treatment for CML. There are two main difficulties associated with the development of kinase inhibitors: the high similarity between active sites of different kinases, which makes selectivity a challenge, and mutations leading to resistance, which make it mandatory to search for alternative drugs. One important factor controlling Abl is the interplay between the catalytic ...
Subjects
free text keywords: Research Article, Biology and Life Sciences, Biophysics, Biophysical Simulations, Cell Biology, Molecular Cell Biology, Computational Biology, Molecular Biology, Biology (General), QH301-705.5, Ecology, Modelling and Simulation, Computational Theory and Mathematics, Genetics, Ecology, Evolution, Behavior and Systematics, Cellular and Molecular Neuroscience
Funded by
EC| PRACE-2IP
Project
PRACE-2IP
PRACE - Second Implementation Phase Project
  • Funder: European Commission (EC)
  • Project Code: 283493
  • Funding stream: FP7 | SP4 | INFRA
54 references, page 1 of 4

1. Daley GQ, van Etten RA, Baltimore D (1990) Induction of chronic myelogenous leukemia in mice by the P210bcr/abl gene of the Philadelphia chromosome. Science 247: 824-830.

2. Nowell PC, Hungerford DA (1960) A Minute Chromosome In Human Chronic Granulocytic Leukemia. Science 132: 1497. Available: http://www.sciencemag. org/content/132/3438/1488.extract.

3. Rowley JD (1973) Letter: A new consistent chromosomal abnormality in chronic myelogenous leukaemia identified by quinacrine fluorescence and Giemsa staining. Nature 243: 290-293. [OpenAIRE]

4. Hantschel O, Superti-Furga G (2004) Regulation of the c-Abl and BcrAbl Tyrosine Kinases. Nat Rev Mol Cell Biol 5: 33-44. doi:10.1038/nrm 1280. [OpenAIRE]

5. Grebien F, Hantschel O, Wojcik J, Kaupe I, Kovacic B, et al. (2011) Targeting the SH2-kinase interface in Bcr-Abl inhibits leukemogenesis. Cell 147: 306-319. doi:10.1016/j.cell.2011.08.046. [OpenAIRE]

6. Gonfloni S, Williams JC, Hattula K, Weijland A, Wierenga RK, et al. (1997) The role of the linker between the SH2 domain and catalytic domain in the regulation and function of Src. EMBO J 16: 7261-7271. doi:10.1093/emboj/ 16.24.7261. [OpenAIRE]

7. Hantschel O, Nagar B, Guettler S, Kretzschmar J, Dorey K, et al. (2003) A myristoyl/phosphotyrosine switch regulates c-Abl. Cell 112: 845-857. [OpenAIRE]

8. Gonfloni S, Frischknecht F, Way M, Superti-Furga G (1999) Leucine 255 of Src couples intramolecular interactions to inhibition of catalysis. Nat Struct Biol 6: 760-764. doi:10.1038/11537. [OpenAIRE]

9. Druker BJ, Tamura S, Buchdunger E, Ohno S, Segal GM, et al. (1996) Effects of a selective inhibitor of the Abl tyrosine kinase on the growth of Bcr-Abl positive cells. Nat Med 2: 561-566. [OpenAIRE]

10. Hunter T (2009) Tyrosine phosphorylation: thirty years and counting. Curr Opin Cell Biol 21: 140-146. doi:10.1016/j.ceb.2009.01.028.

11. Sicheri F, Kuriyan J (1997) Structures of Src-family tyrosine kinases. Curr Opin Struct Biol 7: 777-785. doi:10.1016/S0959-440X(97)80146-7.

12. Xu W, Doshi A, Lei M, Eck MJ, Harrison SC (1999) Crystal structures of c-Src reveal features of its autoinhibitory mechanism. Mol Cell 3: 629-638.

13. Gonfloni S, Weijland A, Kretzschmar J, Superti-Furga G (2000) Crosstalk between the catalytic and regulatory domains allows bidirectional regulation of Src. Nat Struct Biol 7: 281-286. doi:10.1038/74041. [OpenAIRE]

14. Xu W, Harrison SC, Eck MJ (1997) Three-dimensional structure of the tyrosine kinase c-Src. Nature 385: 595-602. doi:10.1038/385595a0.

15. Sicheri F, Moarefi I, Kuriyan J (1997) Crystal structure of the Src family tyrosine kinase Hck. Nature 385: 602-609. doi:10.1038/385602a0. [OpenAIRE]

54 references, page 1 of 4
Abstract
Author Summary The Abl kinase is a key player in many crucial cellular processes. It is also an important anti-cancer drug target, because a mutation leading to the fusion protein Bcr-Abl is the main cause for chronic myeloid leukemia (CML). Abl inhibitors are currently the only pharmaceutical treatment for CML. There are two main difficulties associated with the development of kinase inhibitors: the high similarity between active sites of different kinases, which makes selectivity a challenge, and mutations leading to resistance, which make it mandatory to search for alternative drugs. One important factor controlling Abl is the interplay between the catalytic ...
Subjects
free text keywords: Research Article, Biology and Life Sciences, Biophysics, Biophysical Simulations, Cell Biology, Molecular Cell Biology, Computational Biology, Molecular Biology, Biology (General), QH301-705.5, Ecology, Modelling and Simulation, Computational Theory and Mathematics, Genetics, Ecology, Evolution, Behavior and Systematics, Cellular and Molecular Neuroscience
Funded by
EC| PRACE-2IP
Project
PRACE-2IP
PRACE - Second Implementation Phase Project
  • Funder: European Commission (EC)
  • Project Code: 283493
  • Funding stream: FP7 | SP4 | INFRA
54 references, page 1 of 4

1. Daley GQ, van Etten RA, Baltimore D (1990) Induction of chronic myelogenous leukemia in mice by the P210bcr/abl gene of the Philadelphia chromosome. Science 247: 824-830.

2. Nowell PC, Hungerford DA (1960) A Minute Chromosome In Human Chronic Granulocytic Leukemia. Science 132: 1497. Available: http://www.sciencemag. org/content/132/3438/1488.extract.

3. Rowley JD (1973) Letter: A new consistent chromosomal abnormality in chronic myelogenous leukaemia identified by quinacrine fluorescence and Giemsa staining. Nature 243: 290-293. [OpenAIRE]

4. Hantschel O, Superti-Furga G (2004) Regulation of the c-Abl and BcrAbl Tyrosine Kinases. Nat Rev Mol Cell Biol 5: 33-44. doi:10.1038/nrm 1280. [OpenAIRE]

5. Grebien F, Hantschel O, Wojcik J, Kaupe I, Kovacic B, et al. (2011) Targeting the SH2-kinase interface in Bcr-Abl inhibits leukemogenesis. Cell 147: 306-319. doi:10.1016/j.cell.2011.08.046. [OpenAIRE]

6. Gonfloni S, Williams JC, Hattula K, Weijland A, Wierenga RK, et al. (1997) The role of the linker between the SH2 domain and catalytic domain in the regulation and function of Src. EMBO J 16: 7261-7271. doi:10.1093/emboj/ 16.24.7261. [OpenAIRE]

7. Hantschel O, Nagar B, Guettler S, Kretzschmar J, Dorey K, et al. (2003) A myristoyl/phosphotyrosine switch regulates c-Abl. Cell 112: 845-857. [OpenAIRE]

8. Gonfloni S, Frischknecht F, Way M, Superti-Furga G (1999) Leucine 255 of Src couples intramolecular interactions to inhibition of catalysis. Nat Struct Biol 6: 760-764. doi:10.1038/11537. [OpenAIRE]

9. Druker BJ, Tamura S, Buchdunger E, Ohno S, Segal GM, et al. (1996) Effects of a selective inhibitor of the Abl tyrosine kinase on the growth of Bcr-Abl positive cells. Nat Med 2: 561-566. [OpenAIRE]

10. Hunter T (2009) Tyrosine phosphorylation: thirty years and counting. Curr Opin Cell Biol 21: 140-146. doi:10.1016/j.ceb.2009.01.028.

11. Sicheri F, Kuriyan J (1997) Structures of Src-family tyrosine kinases. Curr Opin Struct Biol 7: 777-785. doi:10.1016/S0959-440X(97)80146-7.

12. Xu W, Doshi A, Lei M, Eck MJ, Harrison SC (1999) Crystal structures of c-Src reveal features of its autoinhibitory mechanism. Mol Cell 3: 629-638.

13. Gonfloni S, Weijland A, Kretzschmar J, Superti-Furga G (2000) Crosstalk between the catalytic and regulatory domains allows bidirectional regulation of Src. Nat Struct Biol 7: 281-286. doi:10.1038/74041. [OpenAIRE]

14. Xu W, Harrison SC, Eck MJ (1997) Three-dimensional structure of the tyrosine kinase c-Src. Nature 385: 595-602. doi:10.1038/385595a0.

15. Sicheri F, Moarefi I, Kuriyan J (1997) Crystal structure of the Src family tyrosine kinase Hck. Nature 385: 602-609. doi:10.1038/385602a0. [OpenAIRE]

54 references, page 1 of 4
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