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- The Discovery of Protein Phosphorylation
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1. Phosphorylase and the origin of reversible protein phosphorylation
- Prof. Edmond Fischer
- Protein Kinase Cascades
- The Modulation of Protein Function by Phosphorylation
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4. Two is the key to 14-3-3: dimeric mechanical signaling devices
- Prof. Carol MacKintosh
- Protein Phosphatases
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5. Structure and mechanisms of protein phosphatases
- Prof. David Barford
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6. Protein tyrosine phosphatases
- Prof. Jack Dixon
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7. The regulation of MAP kinase signalling by dual-specificity protein phosphatases
- Prof. Steve M. Keyse
- The Structures of Protein Kinases
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9. Protein kinase structure, function and regulation
- Prof. Susan Taylor
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10. The structural basis for the modulation of protein function by protein phosphorylation
- Prof. Dame Louise N. Johnson
- Biological Systems that are Regulated by Reversible Phosphorylation
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11. Protein phosphorylation and the control of protein synthesis
- Prof. Christopher Proud
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13. Roles of AMPK in energy homeostasis and nutrient sensing
- Prof. Grahame Hardie
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14. Serine kinases and T lymphocyte biology
- Prof. Doreen Cantrell
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15. The interplay between protein phosphorylation and ubiquitylation in the NF-κB pathway
- Prof. Zhijian 'James' Chen
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16. SMAD phosphorylation and the TGF-beta pathway
- Prof. Joan Massagué
- Protein Kinases and Human Disease
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17. Function and regulation of the PDK1 kinase
- Prof. Dario Alessi
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18. LKB1 pathway and its role in cancer
- Prof. Dario Alessi
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19. WNK1 pathway and its role in regulating hypertension
- Prof. Dario Alessi
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20. The hyperphosphorylation of tau and Alzheimer's disease
- Prof. Michel Goedert
- Protein Kinases as Targets for the Development of Anti-Cancer Drugs
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21. PI3K/AKT signaling in cancer
- Prof. Neal Rosen
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22. RAS and RAF signaling in melanoma: biology and therapies
- Prof. Richard Marais
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23. The mTOR kinase as a target for anti-cancer drugs
- Prof. David Sabatini
- Archived Lectures *These may not cover the latest advances in the field
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25. AMP-activated protein kinase: regulating cellular and whole body energy balance
- Prof. Grahame Hardie
Printable Handouts
Navigable Slide Index
- Introduction
- The 14-3-3 dimer
- Plants photosynthesise
- 14-3-3 inhibits nitrate reductase
- Mutated nitrate reductase and NO levels
- Other functions of 14-3-3
- Plant and human 14-3-3s are identical
- Human and plant 14-3-3-binding proteins
- 14-3-3 dimers as mechanical devices
- 14-3-3 alter tyrosine hydroxylase conformation
- A 14-3-3 clamp masks DNA binding in FOXO4
- A 14-3-3 may clip flanking regions
- 14-3-3 may act as an adapter of two proteins
- Phosphorylated 14-3-3-binding sites
- Many kinases phosphorylate 14-3-3 binding sites
- IGF1/PI3 and 14-3-3-binding site phosphorilation
- 14-3-3 capture and release with isotope labelling
- Overlapping substrates of PKB/Akt and p90RSK
- Patterns in 14-3-3-binding phosphoproteome (1)
- Patterns in 14-3-3-binding phosphoproteome (2)
- Function of 14-3-3 in glucose uptake in muscles
- 14-3-3 binding sites in AS160 and TBC1D1
- Yin-Yang regulation of TBC1D1 and AS160
- Regulating glucose trafficking in different tissues
- 14-3-3 as digital logic gate
- 14-3-3 dimer as logic gate or coincidence detector
- Hypothesis: 14-3-3 dimer as evolutionary device
- Summary
- Thanks to....
Topics Covered
- 14-3-3s dock onto specific sites phosphorylated by AGC and CAMK kinases
- 14-3-3s have hundreds of phosphoprotein partners
- 14-3-3 dimers as mechanical levers and clamps, and 'coincidence detectors'
- Cellular regulation of the 14-3-3-binding phosphoproteome
- Case studies including plant leaf responses to darkness and human cell responses to insulin
Talk Citation
MacKintosh, C. (2010, November 30). Two is the key to 14-3-3: dimeric mechanical signaling devices [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved January 15, 2025, from https://doi.org/10.69645/QXLU4092.Export Citation (RIS)
Publication History
Financial Disclosures
- Prof. Carol MacKintosh has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.