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BMS242 Cell and Molecular > L18 - Receptor Tyrosine Kinases > Flashcards

L18 - Receptor Tyrosine Kinases Flashcards

1
Q

How many families of RTKs

A

16 families

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2
Q

Ligands can be of what two broad calss

A

Hi or lo affinity

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3
Q

What is the structure of the EC domain of the RTK

A

These vary greatly

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4
Q

What activity to the IC domain of the RTK have

A

Kinase activity

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5
Q

How many TMD of the RTK

What is the strcutre, what is the question this produces

A

1

Lacks structure

Question: How is the ligand binding transduced to the inside of the cell

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6
Q

RTK ligand has the abiliy to …

What can this do

A

DImerise and facillitates receptor dimerisation

May also reorient existing receptor oligomers

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7
Q

Describe what happens to the RTK once the ligand is bound

A

Kinase domains phosphorylate each other

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8
Q

Desribe the effects (3) once the kinase domains have phosphorylated each other

A

Increases the activity of the kinase
Stabilises the receptor in the active state
Casues the kinase to phosphorylate other tyrosines in the receptor to create a docking site

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9
Q

Tools for RTK analysis exploit …

A

Dimerisation

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10
Q

Describe how a dominatn geative RTK would be produced

A

Using genetic engineering to make DNA encoding a receptor which is MUTATED IN THE KINASE DOMAIN

Expressed at high levels and poisons the endogenous receptor

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11
Q

How is a constiuently active RTK produced

A

Use genetic engineering to make an RTK lacking the homodimerisation domain

DNA expressed at normal levels and is ligand independent

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12
Q

What are HSPGS

A

Multifunctional extracellular matrix components

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13
Q

Describe the types of protein core in HSPGs (3)

A

Transmembrane
Tethered
Secreted

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14
Q

What happens to the sugars on HSPGs

A

They can be moified

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15
Q

What is one of the most common modifcations on the HSPG sugar

A

Sulphation

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16
Q

What does modificaiton of the HSPG sugar result in

A

Results in a code that creates binding sites for specific proteins

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17
Q

What is a protein which commonly binds to HSPG

A

FGF2

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18
Q

Example of a secreted HSPG

A

Perlecan

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19
Q

Example of a tethered HSPG

A

Glypican

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20
Q

Example of a transmembrane HSPG

A

Syndecan

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21
Q

What occurs when FGF binds to its receptors

A

FGF and its receptor form a complex with HSPGs

FGF first forms oligomers of HSPGs

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22
Q

How does the activated receptor transduce the signal

A

Activated receptor recruits other proteins to the membrane

These protiens bind to phosphotyrosines

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23
Q

RTK have two binding sites - name them

A

Binding site for phosphotyrosine

Binding site for amino acid side chain

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24
Q

The SH2 domain in the RTK recongises which sequence

A

Phosphtyrosine - glutamic acid - glutamic acid - isoleucine

25
Q

What 2 branches are there in the RTK pathway

A

RAS

PI3 kinase

26
Q

What 3 proteins can bind to the PDGF receptor

A

PI3 kinase

GTPase activating protein (GAP)

Phospholipase C-gamma

27
Q

PI3 kinase and PLC-gamma are part of which pathway

A

Inositol lipid pathway

28
Q

What is the GTpase activating protein part of which pathway

A

RAS/MAP kinase pathway

29
Q

What are some of the family members of the Ras family

A

H-RAS K-RAS N-RAS
Rheb
Rep1

30
Q

Functions of H-Ras K-Ras and N-Ras

A

Relays signals from RTKs

31
Q

Functions of Rheb

A

Activates mTOR to stmulate cell growth

32
Q

function of Rep1

A

Activated by a cAMP dependent GEF

Influences cell adhesion by activating integrins

33
Q

Family members of Rho

A

Rho Rac cdc42

34
Q

functions of rho rac and cdc42

A

Relay signals from surface receptors to the cyotskeleton and elsewhere

35
Q

What binds causing the coupling of the receptor to inactive ras

A

GRB2 and Sos(GEF)

36
Q

What is the effect of GRB2 and Sos(GEF) bidning

A

Couples the receptor to inactive ras

37
Q

What does Sos promote

What type of molecule is it

A

Promotes dissociation of GDP from Ras

GEF (gunaine nucelotide exhcnage factor)

38
Q

What occurs after GDP has dissociated

A

GTP binds to Ras

Sos dissociates from the now active Ras

39
Q

Describe the MAP kinase pathway which is downstream of the activated Ras

A

GTP-Ras activates MAP-KKK
MAP-KKK –> MAP-KK (phosohrylation consuming ATP)
MAP-KK –> MAP-K (phosohrylation consuming ATP)
MAP-K can then phosphorylate target proteins

40
Q

What are the two targets for MAP-K what does phosphorylation at each cause

A

protein - changes protein activity

Gene regulatory proteins - changes in gene expression

41
Q

MAP-K pathways is an example of a __________

What are the properites of this

A

Cascade

Rapid and transient response

42
Q

What occurs at each stage of the MAP pathway

A

Amplificaiton

43
Q

What methods may be used to study signalling

A

Visualisation or detection of interations
Chemical inhibitors
Misexpression or overexpression
Genetic methods

44
Q

what types of visualisation methods may be used to study signalling

A 
Biochemical methods (columns
Fret (in vivo)
45
Q

Descruve why grey scale camera are used for flouresecence microscopy

A

Colour cameras are not as sensitive

46
Q

What do dichroic mirrors relfect

A

Shorter wavelengths

47
Q

What is the light source used in flourescence microscopy

A

Laser or a mercury lamp

48
Q

What are the exictation and emission wavelengths of Blue flourescent protein ECFP

A

Exitate at 410 nm

emmit at 480 nm

49
Q

Descirbe the structure of a fluroescent fusion protein

A

Protein - peptide linker and flourophore

50
Q

Blue flouresecnet protein

EXCITE COLOUR _______
EMITT COLOUR _______

A

violet

Blue

51
Q

Green flouresecnet protein

EXCITE COLOUR _______
EMITT COLOUR _______

A

Blue

Green

52
Q

In Fret if there is no interaction what will be seen why will this happen

A

Violet light excites the BFP (blue) causes emission of blue light
No GFP present so all observed is the blue light

53
Q

In FRET if there is an interaction describe what will be seen, why does this happen

A

Violet light excites the BFP - emission of blue light which then excites the GFP causing emssion of green light
Green light is detect

54
Q

What does FRET stand for

A

Forster resonance energy transfer

55
Q

Describe how FRET may be used for protein and substrate

A

BFP - protein
GFP - substrate

If interaction between protein and sunstarate green light will be seen

56
Q

Describe how FRET may be used for a ligand

A

BFP and GFP either side of the ligand binding site
If ligand binds these domains will be brought closer together
If ligand binds - FRET

57
Q

Descibe how FRET may be used for a sensory domain

A

BFP - sensory doamin - substrate - GFP

If substrate binds to sensory domain then BFP and GFP brought closer together and FRET

58
Q

Describe how FRET may be used with a proteease

A

GFP and BFP connected with a peptide linker
If cleavage occurs there will be no FRET
FRET will only occur if there is a link between the BFP and the GFP

59
Q

What type of afifnity do HSPGs have for RTKs

A

Low affinity

BMS242 Cell and Molecular (26 decks)

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