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1. Introduction
2. Oncogenic transformation by v-Src
3. SH2 domains of cytoplasmic tyrosine kinases
4. Interaction between tyrosine kinase receptors
5. Signaling through regulated protein interactions
6. Interaction domains in cellular regulation
7. Features of interaction domains
8. Design of SH2 domain signaling proteins
9. SH2 binding sites on the beta-PDGF receptor
10. Specific SH2 phosphopeptide interaction
11. SH2 domain selectivity
12. SH2 domain specificity (1)
13. SH2 domain specificity (2)
14. WT and mutant SH2 domain structure
15. Recognition motifs in signal transduction
16. SH3 domains have a modular structure
17. SH3 domain versatility
18. Signaling from the T cell antigen receptor
19. The Gads SH2/SH3 adaptor links LAT to SLP-76
20. Mode of peptide recognition by Gad SH3-C
21. Interaction domains are adaptable
22. Mechanisms of interaction surfaces for signaling
23. Functions of interaction domains (1)
24. Physiological functions of interaction domains
25. Functions of interaction domains (2)
26. Interactions regulated by Ser/Thr phosphorylation
27. Phosphorylation and ubiquitin ligase complex (1)
28. Phosphorylation and ubiquitin ligase complex (2)
29. Cdc4 WD40 domain
30. Mechanism of Sic1 degradation
31. Activation of S-phase CDK
32. 14-3-3 proteins bind sites as dimers
33. Regulation of protein function by 14-3-3 binding
34. Functional 14-3-3 binding
35. Physiological functions of interaction domains (1)
36. Adaptors couple receptors to intracellular targets
37. Signaling pathway through an adaptor protein
38. PTB domain proteins serve as scaffolds
39. Different receptors use signaling adaptors
40. Physiological functions of interaction domains (2)
41. Re-iterated use of interaction domains
42. Physiological functions of interaction domains (3)
43. Interaction domains control Src function
44. Interaction domains can be combined
45. The Abl SH3 domain
46. Rewiring cellular signaling by pathogenic proteins
47. Nck adaptors in cytoskeletal regulation
48. Enteropathogenic E.Coli (EPEC)
49. EPEC manipulates the cell cytoskeleton via Nck
50. Nck1 and Nck2 in pedestal formation
51. Oncogenic rewiring
52. Rewiring using chimaric adaptor proteins
53. Therapeutic possibilities of protein interactions
54. Conclusion

Topics Covered

• Mechanisms through which protein interactions modules, such as the SH2 domain, mediate the activation of specific signaling pathways by normal and oncogenic tyrosine kinases
• The biological functions and biochemical properties of interaction domains including their roles in controlling protein localization, in recognition of post-translational modifications, in forming multi-protein complexes, and in regulating enzymatic function
• The versatility of interaction domains, their potential utility in the evolution of new signaling pathways, and their exploitation by pathogenic proteins to rewire cellular behavior

Links

Series:

• Protein Phosphorylation
• Signal Transduction via Protein Tyrosine Kinase Receptors

Categories:

• Biochemistry
• Cell Biology

Talk Citation

Pawson, T. (2010, December 14). Modular protein-protein interactions provide a general mechanism to organize dynamic cellular systems [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved April 15, 2025, from https://doi.org/10.69645/GVBD1102.
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Publication History

• Published on December 14, 2010
• Archived on May 31, 2018

Financial Disclosures

• Prof. Tony Pawson has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.