Lecture 4: Receptor Tyrosine Kinases and Insulin Signaling
Module 8: Topic 4 – Receptor Tyrosine Kinases
Introduction
- Discussing receptor tyrosine kinases, focusing on the insulin receptor as a second class.
- Relation of insulin receptor to diabetes and its importance in glucose regulation.
Insulin Receptor Overview
- Function of Insulin Receptor: Controls glucose uptake in the bloodstream.
- Normal Range of Glucose: Approximately 5 millimolar necessary in the blood for various cellular functions.
- Diabetes: Type 1 and Type 2 diabetes are characterized by ineffective insulin signaling leading to glucose accumulation in the blood, which is harmful.
Insulin Receptor Structure
- Dimer Formation: Insulin receptor forms a dimeric structure (two units).
- Hormone Binding Sensitivity: Requires only one insulin molecule to bind to one of the receptors, effectively turning off hormone binding to the other dimer, enhancing signaling sensitivity.
- Receptor Composition: Alpha and Beta Chains
- Structure: Composed of an alpha2 beta2 complex with disulfide bonds (similar to antibodies).
- **Extracellular Domains:
- L1 Domain:** Leucine-rich domain.
- Cysteine-rich Domain:
- Second L1 Domain: Another leucine-rich domain.
- Cytoplasmic Domain: Contains multiple tyrosine residues that require phosphorylation for function.
Signaling Pathway of Insulin Receptor
- Tyrosine Phosphorylation: Phosphorylated tyrosines act as docking sites for adapter proteins.
- **Activation Mechanism:
- Phosphorylation Process:** Insulin binds to the receptor, activates the receptor through phosphorylation, which is facilitated by ATP.
Pathways Regulated by Insulin
- Two primary pathways following activation:
- **Glucose Regulation Pathway:
- Insulin Receptor Substrate (IRS-1):** Key player in directing the signaling towards glucose regulation.
- **Growth Regulation Pathway:
- SHC Protein:** Directs signaling towards growth processes, particularly in development.
Specific Interactions
- IRS Protein (IRS-1): Targets glucose pathways.
- SHC Protein: Targets growth regulation pathways.
- Binding Mechanism: Requires specific nearby components in the receptor for effective interaction (e.g., phosphotyrosine binding domains).
Key Proteins in the Signaling Pathway
- SH2 Domain: Present in both IRS-1 and SHC proteins, facilitates binding to phosphotyrosines.
- SH2 Domain of GRAB2 Protein: An intermediary that connects signaling processes but does not directly interact with the insulin receptor.
- **Binding Specificity:
- IRS-1:** Recognizes phosphotyrosines adjacent to alanine.
- SHC:** Binds to phosphotyrosines adjacent to specific amino acids like glutamate.
PI3-kinase Activation and Function
- PI3-Kinase: Major player following IRS-1 recruitment.
- Structure: Composed of p85 (regulatory) and p110 (catalytic) subunits.
- Conversion Process:
- Converts PIP2 (phosphatidylinositol 4,5-bisphosphate) to PIP3 (phosphatidylinositol 3,4,5-trisphosphate).
- Mechanism: PIP3 formation involves phosphorylation of the 3-position on the sugar, highlighting its importance for signaling.
- Activates downstream phosphoproteins including AKT.
Downstream Effects of PIP3
- Role of PIP3: Acts as a docking site for proteins like PDK1 and AKT, facilitating their recruitment and subsequent signaling events.
- PDK1 Function: Phosphorylates AKT, activating it for downstream signaling involved in glucose metabolism.
- Insulin Signaling Outcomes: Multiple steps lead to effective glucose regulation and other downstream biological effects.
Summary of Signaling Mechanisms
- Ensure understanding of each step sequentially, especially how insulin signaling leads to glucose regulation and the importance of protein interactions in signaling pathways.
- Implications for diabetes and metabolic regulation highlighted, alongside the mechanisms that ensure precise physiological response to insulin.
Conclusion
- Emphasize the complexity and interconnectedness of these pathways, illustrating the importance of these receptors in health and disease management, specifically regarding diabetes and metabolic syndrome.