5: RTK signaling

Question 1

RTk signaling?

Answer 1

ligand -induced dimerization → signal proteins bind to ligands → ligand dimerizatien → trans autophosphorylation ( activated after 3 phosphors bind)

Question 2

Activation of the EGF receptor kinase?

Answer 2

Absence of ligand : in activated monomer, binding of EGF results in conformational change that promotes dimerizal ion of the external domains.
Orients the internal kinase domains into an asymmetrical dimer in Which kinase domain (activator) pushes against the receiver, thereby causing + activating conformational change in reciever.→ phosphorylates multiple tyrosine’s in the C_terminal tails of both receivers

Question 3

What does GEF do?

Answer 3

remove GDP

Question 4

what does GAP do?

Answer 4

removess phosphate molecule

Question 5

what recognize the SH2 and PT B domains?

Answer 5

phosphor proteins

Question 6

Where does SH3 bind?

Answer 6

to folded part of proteins

Question 7

what does the PH domain do?

Answer 7

recognize PIP3 ( ph domain is close to the plasma membrane

Question 8

feature of Grb2 (adapter protein)?

Answer 8

2x SH3 domains and 1 SH2 domain

Question 9

for what does the scaffold protein have spots?

Answer 9

Raf / MEK / ERK

Question 10

what is the Conserved RAS - ERK pathway

Answer 10

MAPkkk (RAF) → MAPKk (MEK) → MAPK (ERK)
MAP → Mitosos activating protein

Question 11

What happens if Bad is unfosfory lated?

Answer 11

holds apoptosis inhibitory proteins in an inactivated state

Question 12

what happens when Bad is phosphorylated?

Answer 12

releases the inhibitory protein that can block apoptosis and thereby promote cell survival