Week 4 lectures Flashcards

1
Q

What is a phosphatidyl lipid

A

A glycerol backbone with 2 ester bonds to fatty acid chains and 1 ester bond to a phosphate group which binds to a polar head group which can vary

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2
Q

Which Phosphatidyl lipid is charged

A

Phosphatidylserine

All of them have charged parts of the head group but they cancel out overall except phosphatidylserine

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2
Q

Name the 3 phosphatidyl lipids and their head groups

A

phosphatidylenthanolanime - ethanol amine head group
Phosphatidylserine - serine head group
Phosphatidylcholine - choline head group

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2
Q

How are sphingosine lipids different to phosphatidyl lipids

A

Instead of the 3 carbon with 3 hydroxyl groups (glycerol), sphingosine has 3 carbon structure with 2 hydroxyl groups and 1 amine. 1 hydroxyl group and 1 amine group are used to bond to the fatty acid chains and 1 hydroxyl group is used to bond to the phosphate

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3
Q

which group which is added to sphingosine based lipids causes them to be negatively charged

A

sialic acid

sialic acid is a sugar group which can be added to sphingosine based lipids (glycosylated)

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4
Q

Structure of cholesterol

A

Has a polar head group which consists of a singular hydroxyl group

A 4 membered ring structure which is highly rigid, and a short flexible aliphatic side chain.

much smaller and more rigid than the other lipid groupsn

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5
Q

What are the 3 key lipid types

A

Phosphatidyl lipids- phosphatidylenthanolanime, Phosphatidylserine, Phosphatidylcholine

Sphingosine-based lipids and glycolipids

cholesterol

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6
Q

What are the 4 types of motion found in a lipid bilayer

A

Flextion (pretty useless)
rotation (pretty useless)
lateral diffusion
flip-flop

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7
Q

How can changes in the lipid bilayer cause changes in the fluidity of the membrane

A

The closer and the more regular the packing of the tails the more viscous and less fluid the membrane will be

this is dependant on the length of the tails - shorter tails are packed less tightly.
number of double bonds- more double bonds means packed less tightly

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8
Q

What is the effect of cholesterol on membrane fluidity and why

A

No effect. tighter packing close to the head group is counteracted by less order away from the head group

It does effect the permeability of the membrane

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9
Q

Different ways a protein can associate with the membrane

A

QUESTION ASKED ON PADLET CHECK FOR ANSWER

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10
Q

How is the movement of a membrane proteins limited

A

Movement of membrane proteins are limited by the cortical cytoskeleton, Proteins largely move within one membrane domain but can move between domains

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11
Q

How are proteins on the basal and apical sections of epithelial cells kept apart

A

there are very tight junctions towards the apical side of the cell, this tight junction means that proteins from the apical side cannot move to the basal side maintaining the polarity of epithidiel cells

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12
Q

What are the roles of the cytoskeleton

A

Structural integrity
Shape and movement of cell
Subcellular organisation of the cell

cytoskeleton is a highly dynamic assembly

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13
Q

How does the structure of the cytoskeleton allow for dynamic behaviour

A

Its composed of fibres that are build from individual proteins. Allowing monomers to be added and removed as needed.
they can be added and removed form either end.

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14
Q

What are the 3 types of filaments

A

Intermediate filaments
Microtubules
Actin filaments

15
Q

What is the basic unit of a microtubule

A

A heterodimer of tubulin (alpha and beta subunits)

16
Q

How is a microtubule structured

A

Made form heterodimers of tubulin and formed around an inner hollow core

Thickest of all filaments
Have plus and minus ends

17
Q

What is the difference between the plus and minus ends of a microtubule

A

Minus end has an alpha subunit on the end
plus end has a beta subunit
Minus end is anchored into the MTOC or centrosome

18
Q

How do microtubules grow/shrink

A

Tubluin can bind to GTP. When they are in the GTP bound state this promotes the addition of further monomers. tubulin is also a GTPases and slowly converts GTP into GDP.
The end of the polymer can be severed of exposing the GDP bound tubulin which promotes the rapid removal of the monomers

The addition and removal of GTP caps causes the growth and shrinkage

19
Q

What are motor proteins

A

Proteins which associate with and move along microtubules and actin. Binds to the proteins as well as the cargo and uses ATP to change conformations to move along the actin/microtubule

On microtubules they can move from the plus end to the minus end. On actin it can only move from - to + end

20
Q

Different types of mictrotubule motor proteins

A

Kinesins - Move cargo from minus end to plus end – away from MTOC

Dynesins - move cargo from plus end to minus end

21
Q

What are the functions of microtubules

A

Interphase:
Vesicular transport
Structural integrity
formation/support of specialised cell structures like cilium

Dividing cell:
chromosome segregation

22
Q

Name drugs that affect microtubules

A

Colchicine - destabilises microtubules, Anti inflammatory drug

Taxol- Stabilises microtubules - cancer drug

23
Q

Name the process by which actin polymerises and how it works

A

Nucleation - nucleation is a process in which you disfavor the assembly of a small number of identical building blocks (actin monomers here) into a complex, while the further addition of building blocks once this small complex is formed becomes favorable. The tipping point of the number of assembled building blocks where you can switch from disfavored to favored assembly varies for each complex, for actin filaments that is three actin monomers. This process achieves two conflicting objectives. You want to make spontaneous assembly of monomers inefficient so that protein complexes don’t form at random (1 to 3 assembled actin monomers). At the same time you want to make the generation of larger protein complexes efficient as it otherwise would be practically impossible to build complexes of hundreds to thousands of monomers (3 and more assembled actin monomers).

24
Q

How can nucleation of actin be overcome

A

Arp2/3 complex
this is a complex which uses other existing actin filaments to create more actin filament. It is a highly regulated complex and is only active and when a new actin filament needs to be formed. when its activated the backside of the complex binds to the pre existing actin filament. this making it a new site for actin growth.
The Arp2/3 complex contains to proteins, Arp2 and Arp 3 which are structurally similar to actin making it much easier for an actin filament to form.

this combination of multiple beached structures means that you form a sheet-like structure composed of actin filaments

25
Q

How can polymerisation of actin be sped up

A

A protein family called formins bind to the plus end and provide a location to effectively add new actin monomers - doesn’t overcome nucleation but speeds up the process of actin polymerisation generating very long actin structures which are point like unlike sheet like structures formed from Arp2/3 complexes

26
Q

Motor proteins and actin

A

Motor proteins associate with and move along actin filaments using hydrolysis of ATP as energy
The motor proteins associated with actin is called myosin and can move actin filaments against each other and protein complexes, commonly on the surface of vesicles.
myosins move from the - to + end only

27
Q

What are the roles of myosin-I and myosin-II

A

Myosin-I - 1 side of the protein binds to the F-actin and the cargo side binds to membrane- can be vesicle or plasma membrane
Myosin-II moves different actin filaments against each other - muscle function, muscles are just highly organised structures of actin and myosin filaments when you contract the myosin filament pulls together the actin filaments

28
Q

Name actin filament structure

A

Microvilli
contractile bundle
sheet-like and finger-like projections
contractile ring
Stabilisation of membrane cortex - cell membrane are very thin and fragile, actin filaments underpin the membrane providing strength and mechanical stability.

29
Q

What is change of cell shape in migration atory cells

A

Actin filament and dynamic of actin filaments

30
Q

What are intermediate filaments

A

Toughest and most durable cytoskeleton structures, provide mechanical stability to the cell and like the dynamic features of actin and myosin

31
Q

Where are intermediate filaments found

A

Nucleus - form the nuclear lamina which underlies and strengthens the nuclear envelope
cytoplasm- form a network throughout the cell and are liked to cell-cell junctions allowing them to provide mechanical strength across a large number of cell - very important fro epithelial cells.

32
Q

What are the intermediate filaments made of

A

Several different proteins
Need to know that intermediate filaments that make up the nuclear lamia are Lamins A,B and C

33
Q

DO VESICLES LECTURE

A