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Printable Handouts
Navigable Slide Index
- Introduction
- Oncogenic transformation by v-Src
- SH2 domains of cytoplasmic tyrosine kinases
- Interaction between tyrosine kinase receptors
- Signaling through regulated protein interactions
- Interaction domains in cellular regulation
- Features of interaction domains
- Design of SH2 domain signaling proteins
- SH2 binding sites on the beta-PDGF receptor
- Specific SH2 phosphopeptide interaction
- SH2 domain selectivity
- SH2 domain specificity (1)
- SH2 domain specificity (2)
- WT and mutant SH2 domain structure
- Recognition motifs in signal transduction
- SH3 domains have a modular structure
- SH3 domain versatility
- Signaling from the T cell antigen receptor
- The Gads SH2/SH3 adaptor links LAT to SLP-76
- Mode of peptide recognition by Gad SH3-C
- Interaction domains are adaptable
- Mechanisms of interaction surfaces for signaling
- Functions of interaction domains (1)
- Physiological functions of interaction domains
- Functions of interaction domains (2)
- Interactions regulated by Ser/Thr phosphorylation
- Phosphorylation and ubiquitin ligase complex (1)
- Phosphorylation and ubiquitin ligase complex (2)
- Cdc4 WD40 domain
- Mechanism of Sic1 degradation
- Activation of S-phase CDK
- 14-3-3 proteins bind sites as dimers
- Regulation of protein function by 14-3-3 binding
- Functional 14-3-3 binding
- Physiological functions of interaction domains (1)
- Adaptors couple receptors to intracellular targets
- Signaling pathway through an adaptor protein
- PTB domain proteins serve as scaffolds
- Different receptors use signaling adaptors
- Physiological functions of interaction domains (2)
- Re-iterated use of interaction domains
- Physiological functions of interaction domains (3)
- Interaction domains control Src function
- Interaction domains can be combined
- The Abl SH3 domain
- Rewiring cellular signaling by pathogenic proteins
- Nck adaptors in cytoskeletal regulation
- Enteropathogenic E.Coli (EPEC)
- EPEC manipulates the cell cytoskeleton via Nck
- Nck1 and Nck2 in pedestal formation
- Oncogenic rewiring
- Rewiring using chimaric adaptor proteins
- Therapeutic possibilities of protein interactions
- 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
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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 October 4, 2024, from https://doi.org/10.69645/GVBD1102.Export Citation (RIS)
Publication History
Financial Disclosures
- Prof. Tony Pawson has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.
Modular protein-protein interactions provide a general mechanism to organize dynamic cellular systems
A selection of talks on Biochemistry
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