CellSig10 - 18 Flashcards Preview

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Flashcards in CellSig10 - 18 Deck (18):
1

How many families of RTKs are there?

16

2

Characterise RTKs

EC domains vary greatly, IC have kinase activity, 1TM with a lack of structure

3

Outline canonical RTK activation

Ligand dimerises and facilitates the dimerisation of receptors > IC kinase domains phosphorylate each other > stabilisation, and creation of docking sites

4

How do we analyze RTK signalling?

Mutate one version - this poisons endogenous receptor, which interrupts function; create homodimerisation domain that forces constiuent activity

5

Characterise the role and structure of heparan sulphate proteoglycans

Protein core,polyanionic (negative), long heparan (sugar) chains, each sugar can be modified in different ways > possible 'code' that creates binding sites?

6

What broader family are HSPGs part of?

GAGs - Glycosoaminoglycans

7

What are HSPGs integral to?

FGF signalling - they first form oligomers with HSPGs

8

3 proteins that bind RTKs

PI3K, GAP, PLC-g

9

What often form between cysteines and what is their function?

Sulphide bridge - often hold EC proteins together

10

What transporter takes up glucose?

GLUT4 proteins

11

How are GLUT4 receptors involved in the insulin pathway?

They are held in IC vesicles that fuse immediately after insulin binding, causing a massive uptake of glucose from the bloodstream

12

What does insulin binding result in?

Autophosphrylation and ligand independence

13

What is IRS?

Insulin receptor substrate

14

What does IRS contain?

PTB - phosphotyrosine binding domain

15

What does IRS do?

Acts a docking site for many other proteins, such as GRB2 of the RAS pathway

16

What constitutes PI3K?

P85 and P110 (SH2 domain and kinase)

17

What does PI3K do in the insulin cascade?

Binds to IRS, phosphorylating PI4,5 and PI4 into PI3,4,5 and PI3,4, creating a binding site for PKB

18

What does PKB go on to do in the insulin cascade?

Phosphorylated and released, affecting numerous regulatory proteins