A. Cell Signaling (Part 2) Flashcards
transmembrane proteins with their ligand-binding
domain on the outer surface
signaling through enzyme-coupled receptor
the phosphorylation of tyrosine side chains creates
phosphotyrosine docking sites
cytosolic domain has intrinsic enzyme activity or associates directly with enzyme
signaling through enzyme-coupled receptor
how does EGT receptor kinase domain activates?
promoting conformational change
how does dimerizing happen?
bring the two cytoplasmic kinase domains together and promoting activation
cytosolic domain has intrinsic enzyme activity or associates directly with
enzyme
dimerization brings the kinase domains close to each other in an
orientation that allows them to phosphorylate each other on specific tyrosines
insulin receptor
most common class of the enzyme-coupled receptors
receptor tyrosine kinase
the binding of the signal protein to
the ligand-binding domain on the
extracellular side of the receptor
activates the tyrosine kinase
domain on the _ _
cytosolic side
How does the binding of ligand activate the kinase domain in intracellular?
ligand binding causes the receptors to dimerize
what happens if signaling proteins binds to a particular phosphorylated site?
phosphorylated on
tyrosines and become activated
families of
monomeric GTPases
Ras superfamily
Phosphorylation of kinase domains of RTK creates
high-affinity docking sites for intracellular signaling proteins
the kinase is not activated by phosphorylation but by conformational changes
epidermal growth factor (EGF)
What does kinase domains of RTK dimer phosphorylates?
multiple additional sites of cytosolic parts of receptors
serves as a switch to trigger the assembly of an intracellular
signaling complex
receptor phosphorylation
