27
Signalling via Enzyme-Linked Receptors
Learning Targets
- How signalling via enzyme-linked receptors work, focusing on Receptor Tyrosine Kinases (RTKs).
- How is the receptor activated?
- How is RTK signalling organized?
- RTK signalling induces widespread effects.
- Example: signalling via insulin receptors.
- Role of growth factor receptors and how they work.
- MAP kinases cascade activation.
- Role of GTP binding in signalling.
- How growth factor signalling becomes deregulated in cancer.
- Key concept: Receptor tyrosine kinase signalling plays an essential role in the regulation of cell growth and survival, and is targeted for cancer treatment.
Case Study
- A patient, Mrs. Jones, has a lump on her breast and undergoes a biopsy.
- The breast specialist suggests immediate treatment with Herceptin (Trastuzumab).
- Why? How does this drug work?
Enzyme-Linked Receptors
- Receptors are activated through ligand binding, such as growth factors and cytokines.
- Ligand binding induces conformational changes in the receptor.
- Change in receptor structure activates an intrinsic enzyme activity associated with the receptor or promotes the binding and activation of an enzyme.
- Enzymatic activation begins the signal transduction process.
Receptor Tyrosine Kinases (RTKs)
- Major class of enzyme-linked cell surface receptors.
- Have intrinsic tyrosine (Tyr) kinase activity.
- Activated RTKs phosphorylate themselves on Tyr amino acids!
- Contain:
- An extracellular ligand-binding domain.
- One transmembrane domain per protein subunit.
- An intracellular protein tyrosine kinase domain.
- Family of about 60 human genes.
RTKs and Cell Growth/Survival
- RTKs typically transmit signals that promote cell growth and survival.
- Activated by a large variety of secreted tissue cell-specific growth factors and hormones like insulin.
Mechanisms of Activation of RTKs
- For many receptor tyrosine kinases, ligand binding causes receptor subunits to dimerize and become activated.
- Leads to autophosphorylation of Tyr residues within the kinase domain in the cytosolic tail of RTK.
- Tyr phosphorylation outside the kinase domain creates high-affinity docking sites for the binding of intracellular signalling proteins in the target cell.
- Signalling proteins become activated due to docking or Tyr phosphorylation.
Multiple Signals Generated by RTKs
- RTK activation triggers the transient assembly of a large intracellular signalling complex.
- This allows broadcasting multiple signals along multiple pathways to many destinations in the cell.
- Distinct RTKs bind different combinations of signalling proteins, thereby inducing different responses.
- Once cross-phosphorylated, the cytoplasmic tails of RTKs serve as docking platforms for various intracellular proteins involved in signal transduction.
Example: Insulin Signalling
- After a meal, insulin stimulates uptake of glucose, amino acids & free fatty acids from blood.
- Promotes synthesis & storage of carbohydrates, proteins, and lipids.
- Binding of insulin to receptor promotes Tyr autophosphorylation of the receptor.
- Leads to Tyr phosphorylation of specific proteins called insulin receptor substrates (e.g., IRS-1).
- Phosphorylated IRS serve as multisite docking proteins for various effector molecules, enlarging the size of the signalling complex.
Insulin's Effects
- Insulin initiates a wide variety of growth and metabolic effects.
- Activation of several signalling cascades leading to widespread effects (tissue-specific).
- Rapid effects: e.g., glucose uptake, activation and inhibition of enzymes.
- Long-lasting effects: e.g., protein synthesis (metabolic enzymes), cell growth.
Growth Factor Signalling and Cancer
- Normal tissues carefully control the production and release of growth-promoting signals that instruct entry into and progression through the cell growth and division cycle.
- This ensures homeostasis of cell size, number, and function.
Epidermal Growth Factor Receptor (EGFR)
- EGFR is a member of the HER family of 4 human epithelial receptors (EGFR or HER1, HER2, HER3, and HER4).
- Each is activated by specific ligands, except HER2 (no ligand required).
- Dimerization is required for activation.
- If the same receptor → homodimerization.
- If a different receptor → heterodimerization.
Major Pathways Activated by EGFR
- MAPK/ERK cascade.
- PI-3 kinase / Akt pathway.
- JAK/STAT pathway.
- Lead to enhanced growth and survival.
Molecular Switches in Cell Signalling
- Two main molecular switch mechanisms to turn on or off proteins:
- Protein phosphorylation.
- GTP binding.
- Protein in an inactive state is bound to GDP.
- Exchange of GDP for GTP leads to protein activation.
- Two types of GTP-binding proteins:
- Large heterotrimeric G proteins: transduce signals from G-protein-coupled receptors.
- Small monomeric GTPases: transduce signals from enzyme-linked receptors.
GTP Binding as a Signalling Switch
- ON SWITCH:
- GDP is exchanged for GTP, resulting in protein activation.
- Exchange is promoted by GEF = Guanine nucleotide exchange factors.
- OFF SWITCH: Activation is short-lived!
- GTP binding proteins have intrinsic hydrolysing activity (GTPase activity).
- GTP hydrolysis leads to inactivation, thereby terminating signalling.
- GTPase-activating or GTPase-accelerating proteins called GAP increase the rate of GTP hydrolysis, accelerating inactivation.
MAP Kinase Activation Pathway
- RTK phosphorylation results in the recruitment of an adapter protein called Grb2 (growth factor receptor-bound protein 2).
- Grb2 recruits SOS, a GEF that promotes the exchange of GDP to GTP on Ras (small GTPase), leading to Ras activation.
- This leads to phosphorylation and activation of the kinase, Raf (or B-Raf) and initiation of sequential phosphorylation/activation steps of the MAPK cascade.
EGFR Signalling and Cancer
- RTKs can be constitutively activated by mutations that induce malignant cell transformation.
- Deregulation of signalling by EGFR or family members is a common feature in several human malignancies, including lung, breast, colorectal, prostate, and head and neck cancer.
- This makes them a target of an expanding class of anticancer therapies.
Hyperactivation of EGFR Signalling in Cancer
- Overexpression of EGFR, often due to gene amplification.
- Mutations in receptor and signaling proteins, leading to constitutive activation.
- Increased secretion of growth factors by tumor cells, which can stimulate EGFR (autocrine).
EGFR Signalling: A Therapeutic Target
- Anti-EGFR monoclonal antibodies inhibit ligand binding.
- Small-molecule EGFR tyrosine-kinase inhibitors inhibit TK activity.
- These block EGFR signalling to inhibit growth, tumour proliferation, and migration.
RTKs as Drug Targets
- Examples of drugs that act against tyrosine kinases:
- Small molecule drugs: Gleevec (imatinib), Iressa (gefitinib), Tarceva (erlotinib), Sutent (sunitinib), Sprycel (dasatinib), Tykerb (lapatinib).
- Monoclonal antibody drugs: Herceptin (trastuzumab), Erbitux (cetuximab), Avastin (bevacizumab).
Case Study: Herceptin
- Biopsy has shown invasive cancer cells.
- Genetic testing shows that the breast cancer is HER-2 (human epidermal growth factor receptor 2) positive.
- ~1 in 5 women with breast cancer are HER2+.
- Herceptin: Monoclonal antibody inhibits ligand-independent HER2 dimerization and thus inhibits activation of signalling.
RTK Inhibitors
- Examples: Trastuzumab, Gefitinib, Erlotinib, Cetuximab, Bevacizumab.
- Other inhibitors of the MAPK pathway:
- B-Raf inhibitors: Dabrafenib, Vemurafenib.
- Mek inhibitors: Refametinib, Selumetinib, Trametinib.
- Raf inhibitors: Regorafenib, Sorafenib.
Summary
- RTK signalling is a key driver of cell signalling and is often hijacked in cancer.
- Activated RTKs or downstream signalling proteins are targets for anti-cancer therapies.
- RTKs activate downstream pathways via phosphorylation or GTP binding.
- The MAPK pathway is an essential signalling cascade for cellular growth and survival, activated downstream of multiple RTKs, including EGFR/HER.