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Cancer Y2 > Invasion - Regulation of Cell Migration > Flashcards

Invasion - Regulation of Cell Migration Flashcards

1
Q

: Most human tumours are derived from X tissues

A

Epithelial

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2
Q

2 types of cell migration?

A
  • Individual cell migration

- Collective cell migration- group of cells which maintain cell-cell contacts

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3
Q

What is needed uniquely for collective cell migration regarding cell adhesion

A
  • Cadherins and gap junctions are needed for collective migration
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4
Q

Examples of times cells need to move? (3)

A

organogenesis and morphogenesis, or in wound healing

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5
Q

What are the usual stimuli for cell movement (2)

A

growth factors or chemoattractants

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6
Q

How does the morphology of a cell change when they are stimulated to migrate

A

retraction at the back of the cell and protrusions appear at the front- this helps the cell to move efficiently

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7
Q

What stop cells moving and guides them in the right direction

A

Contact inhibition

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8
Q

What specialized structures allow efficient movement (3)

A

focal adhesions, lamellae, filopodium

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9
Q

What are focal adhesions

A

Points where the cell can hook on to ECM proteins

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10
Q

Points where the cell can hook on to ECM proteins are known as …

A

focal adhesions

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11
Q

What protein facilitates hooking of the cell to ECM proteins

A

Integrins

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12
Q

What ends at the point of focal adhesions

A

Actin filaments

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13
Q

Tracks of actin filaments end at …

A

focal adhesions

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14
Q

What are integrins

A

are transmembrane protein dimers with a short cytoplasmic tail with docking sites for cytoskeletal proteins

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15
Q

What are filopodia (consist of (2)… shape…)

A

Finger-like protrusions rich in actin filaments (and vinculin)

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16
Q

What do filopodia do

A
  • They allow cells to sense their environment and coordinate their movement
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17
Q

What are lamellipodia (consist of … shape…)

A

Sheet-like protrusions rich in actin filaments

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18
Q

What do lamellipodia do (how do they facilitate movement)

A
  • Sheets project to the front and then ruffle back to allow the cell to move
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19
Q

2 types of motility? (regarding cause of movement)

A

MOTILITY can be HAPOPTATIC (random) or CHEMOTATIC (has purpose e.g. responding to growth factor etc.)

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20
Q

4 stages of cell movement?

A
  1. Extension
  2. Adhesion
  3. Translocation
  4. De-adhesion
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21
Q

2 types of actin

A

G and F actin

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22
Q

Difference between G and F actin

A
  • G actin (small and soluble) and F actin which is polymerized G actin. F actin is also polar
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23
Q

What is the polymerised filamentous form of actin known as

A

F actin

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24
Q

Filaments are X (have different structures in one end compared to the other)

A

Polarised

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25
Q

organisation of F actin in filopodium?

A

Bundles of parallel filaments

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26
Q

organisation of F actin in stress fibres?

A

antiparallel contractile structures

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27
Q

organisation of F actin in lamellipodium?

A

Branched and cross linked filaments

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28
Q

What three structures can actin filaments form

A

Lamellipodium, filopodium and stress fibres

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29
Q

What is the rate limiting step in the organisation of the cytoskeleton

A

Nucleation

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30
Q

What does nucleation of actin achieve

A

formation of trimers to initiate polymerization

31
Q

What proteins are need for nucleation? what complex does this form

A
  • Arp2 and Arp3 form ARP complexes
32
Q

How does ARP complex interact with actin (which end does it bind to)

A
  • These bind to actin monomers and will be bound at the –ve end of the filament when it has formed
33
Q

What proteins facilitate elongation of filaments

A
  • Prolifin
34
Q

What does prolifin do (which end)

A
  • Prolifin is a protein that binds to actin monomers (G-actin) and brings them to the actin filament to the +ve end to elongate it
35
Q

What does thymosin do

A
  • Thymosin is a protein that binds to actin monomers but doesn’t bring them to the actin filament -> Inhibit the polymerization process
36
Q

What do sequestering protein beta4thymosin and ADF/cofilin do

A
  • Sequestering proteins called beta4-thymosin and ADF/cofilin bind to monomers but do not inhibit polymerization
37
Q

What protein inhibits the elongation of actin filaments

A
  • Thymosin is a protein that binds to actin monomers but doesn’t bring them to the actin filament Inhibit the polymerization process
38
Q

What proteins sequester actin monomers

A
  • Sequestering proteins called 4-thymosin and ADF/cofilin bind to monomers but do not inhibit polymerization
39
Q

What do capping proteins do

A
  • Capping proteins regulate the elongation process of the filaments
40
Q

What is MoA of capping proteins

A
  • They bind to the end of the filament and prevent monomers binding
  • After a capping protein binds to one end, you get disassembly of some of the filament which causes shortening of the filament
41
Q

What capping proteins bind to the negative end of actin filaments (2)

A

 Tropomodulin

 Arp complex

42
Q

What capping proteins bid to the positive end of actin filaments (3)

A

 Cap Z
 Gelsolin
 Fragmin/severin

43
Q

What do severing proteins do

A

Regulates filament size

44
Q

What happens in unsevered population of actin filaments regarding growth

A
  • In un-severed populations, filaments grow and shrink relatively slowly
45
Q

What happens in severed population of actin filaments regarding growth

A
  • In severed populations, actin filaments grow and shrink more rapidly
46
Q

Example of severing proteins

A

Gelsolin, ADF/cofilin, fragmin/severin

47
Q

Bundles of parallel filaments describes the structure of …

A

Filopodia

48
Q

antiparallel contractile structures describes the structure of …

A

Stress fibres

49
Q

Branched and cross linked filaments describes the structure of …

A

Lamellipodia

50
Q

What does fascin do

A

Protein that bundles filaments at a particular distance

51
Q

What does FIMBRIN do

A

Does the same but at longer distance between filaments

52
Q

What does alpha-ACTININ do

A

Bundles

53
Q

What does SPECTRIN do

A

Cross-links filaments at particular angles

54
Q

What does FILAMIN do

A

Cross-links filaments at particular angles

55
Q

What does DYSTROPHIN do

A

Cross-links filaments at particular angles.

56
Q

Proteins that bundle?

A

FASCIN
FIMBRIN
-ACTININ

57
Q

Proteins that cross link?

A

SPECTRIN
FILAMIN
DYSTROPHIN

58
Q

Depending on the width of the gap between filaments, motor proteins can or cannot ……..

A

travel along the actin filaments

59
Q

What is responsible for branching in lamellae

A
  • Arp2 complex
60
Q

What angle does branching occur at

A

70 degree angles

61
Q

What is gel-sol transition and when does it take place and by what

A

When the cell needs to move, the membrane will need to flow- in gel form, the actin cytoskeleton is rigid, but in sol form, the filaments are severed to allow flow

62
Q

Which actin modifying processes are involved in filopodia formation

A

elongation
bundling
actin assembly

63
Q

Which actin modifying processes are involved in lamellae formation

A 
Assembly
Elongation
Capping
Branching
Severing
64
Q

Signalling mechanisms that regulate actin cytoskeleton

A
  1. Ion flux changes (i.e. intracellular calcium)
  2. Phosphoinositide signalling (phospholipid binding)
  3. Kinases/phosphatases (phosphorylation cytoskeletal proteins)
  4. Signalling cascades via small GTPases
65
Q

What GTPase subfamily regulates the actin cytoskeleton

A

Rho subfamily

66
Q

What 3 things activate the Rho subfamily

A

receptor tyrosine kinase, adhesion receptors (integrins cadherins) and signal transduction pathways

67
Q

Which small GTPase causes lamellipodia

A

Rac

68
Q

What do stress fibres do

A

Contractile fibres

69
Q

Which small GTPase causes filopodia

A

Cdc42

70
Q

Which small GTPase causes stress fibres

A

Rho

71
Q

What does activation of Cdc42 cause the formation of

A

Filopodia

72
Q

What does activation of Rho cause the formation of

A

Stress fibres

73
Q

What does activation of Rac cause the formation of

A

Lamellipodia

Cancer Y2 (15 decks)

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