Any protein in the cytosol can dock on a receptor phosphotyrosine.
Circle one: True False
Why must a receptor tyrosine kinase pair up before it can signal?
- Binding alone switches one receptor on
- Pairing only cleans up extra receptors
- Single receptors are inactive; only the dimer can cross-phosphorylate
What does autophosphorylation build on the receptor?
- Docking sites for specific adaptor proteins
- Second messengers flooding the cytosol
- New ligands for neighbouring receptors
What does the phosphorylation cascade achieve?
- It slows the signal so the cell can rest
- It removes the need for any ligand at all
- It turns one active receptor into a flood of active kinases in the nucleus
How does RTK signalling differ from GPCR signalling?
- RTKs use G proteins while GPCRs phosphorylate themselves
- GPCRs use G proteins and messengers while RTKs dock adaptors directly
- Both use identical relays with different names
A mutant receptor dimerises without any ligand present. What happens?
- It signals nonstop, as if growth factor were always present
- It stays silent, since no ligand arrived
- It switches to G protein signalling instead
A drug covers the phosphotyrosine docks without touching pairing or phosphates. What fails?
- The cascade amplifies even more
- Dimerisation stops happening
- Adaptors cannot latch, so the cascade never starts
Theo says binding alone switches the receptor on and pairing just follows. What is wrong?
- He is right; pairing just tidies up afterwards
- Pairing is the switch; without it no cross-phosphorylation happens
- Binding never matters; receptors fire at random