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1
Q

Proteins that get secreted have a secretion signal that is located at what ?

A

The N-termini

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2
Q

What do we do as soon as protein starts to emerge and then where does it go ?

A

We stop making proteins and then everything will go to the ER if it contains a secretion signal

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3
Q

What is the secretion signal that has emerged from a ribosome bound by ?

A

SRP

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4
Q

What is the first job of SRP is responsible for ?

A

Halting translation

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5
Q

What is the second job that SRP is responsible for ?

A

It binds to the SRP receptor

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6
Q

What is a translocon ?

A

A channel in the ER membrane

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7
Q

Where does the secretion signal sequence always get stuck ?

A

The translocon

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8
Q

Where does translation drive a polypeptide that has a secretion signal sequence to go ?

A

Drive it to go to the ER lumen (Through the translocon)

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9
Q

Where is the signal peptidase anchored ?

A

The translocon

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10
Q

The secretion signal sequence that is anchored in the translocon is cleaved by what ?

A

Cleaved by Signal peptidase

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11
Q

Where is the protein released after is has been cleaved by the signal peptidase ?

A

The ER Lumen

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12
Q

Why do we call a protein a Transmembrane Protein ?

A

Transmembrane proteins cross the membrane

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13
Q

Where does a stop transfer sequence always get stuck ?

A

In the translocon

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14
Q

What does the Stop Transfer Sequence do ?

A

As the name suggests, it stops proteins through the translocon (cannot be cleaved)

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15
Q

What is a Multi Pass transmembrane protein ?

A

A protein that goes through the membrane a multiple number of times

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16
Q

What must happen to proteins in order for them to do their job correctly ?

A

They must be folded correctly

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17
Q

Are proteins in the translocon folded or are they in the form of a line ?

A

Form of a line

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18
Q

Is the ER lumen the same as the cytoplasm or is it different ?

A

It is different because there can be different environments

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19
Q

What does the ER have that helps proteins fold correctly ?

A

The ER has specific enzymes that help folding which are called chaperone

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20
Q

What type of environment does the ER have ?

A

It has an oxidizing environment

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21
Q

What type of environment does cytoplasm have ?

A

A reducing environment

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22
Q

What are disulfide bonds ?

A

Bonds that are between sulfurs

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23
Q

What do all proteins that end up in the ER become ?

A

They become glycosylated

24
Q

What do sugars act as ?

A

They act as shipping labels and inspection labels

25
Q

Why is it important that sugars act as shipping labels ?

A

So we know where a protein is eventually going to go

26
Q

What do some proteins also require be added to them

A

Some will need lipids because it they be in the membrane

27
Q

How is quality control in the ER maintained ?

A

We use a protein called Calreticulin and folding sensors

28
Q

What does Calriticulum do ?

A

Helps things fold correctly

29
Q

What does the folding sensor do ?

A

Gives the green light a protein is ready to be sent. If not it will be sent back to be remolded correctly. Sometimes if a protein is too messed up to be refolded it will disregard the protein entirely.

30
Q

What do we keep on stand by if a protein is not folded correctly ?

A

Chaperones

31
Q

What is most likely the issue that is happening if all the sudden we have a gene that is consistently sending out bad proteins ?

A

A mutated gene

32
Q

How much help do proteins need in order to do their job ?

A

Not a lot, but some help here and there

33
Q

What does sequester mean ?

A

Keeping chaperones seperated until they are needed.

34
Q

Is the stop transfer sequence bounded by SRP ?

A
35
Q

What must occur for a protein to get out of the translocon and into the ER Lumen ?

A

It must be cleaved

36
Q

What do we modify in the ER and what might some of them end up with ? What do they always have ?

A

We modify proteins in the ER. WIll sometimes end up with a lipid, but will always have a sugar

37
Q

What will the protein attach to if it has a lipid ?

A

The membrane

38
Q

What do sugars act as ?

A

Shopping label and inspection label

39
Q

WHat do proteins have to do in order to work correctly ?

A

Must fold correctly

40
Q

What is the addition of sugars called ?

A

Glycosylation

41
Q

What are the results that happen when quality crontrol in the ER is happening ?

A
  1. It’s ready to go
  2. It’s not ready to go
  3. It’s so bad that we send it ubiquination ?
42
Q

What is the response that happens when we have a mutated gene ?

A

TO shut down

43
Q

What is a more nuclear option when there is a mutation ?

A

Program cell death. Basically killing ourselves

44
Q

Why do we have a smooth ER ?

A
  1. It is essentially responsible for making our phospholipids
  2. Makes all the membranes in the cells
45
Q

Where are phospholipids made ?

A

The cytosolic face of the ER

46
Q

What must happen if we only make phospholipids on one side of the ER ?

A

We have to make it on both sides so we move some of them to the other side

47
Q

What is an example of a protein that should stay in the ER ?

A

Calreticulin

48
Q

What will a protein have if it is meant to be in the ER ?

A

It will have an ER retention sequence.

49
Q

What is the place called where we sort proteins ?

A

ERGIC (ER-Golgi-Intermediate Complex)

50
Q

What is the ER-GIC ?

A

A recycling facility for proteins

51
Q

WHat is similar between a secretion signal sequence and a stop signal sequence.

A

They both get stick translocon

52
Q

What is different between a Stop signal sequence and a secretion signal sequence

A

Stop can be cleaved and signal can. SRP isn’t bounded to the stop and srp is bounded to the secretion

53
Q

What must occur for a protein to get out of the translocon and into the ER membrane

A

It must move laterally out of the translocon

54
Q

How do we flip phoslipiids from one side of the er membrane to the other.

A

The enzyme flipase

55
Q

Er retention sequence means ?

A

A certain sequnce of amino acids