protein sorting and intracellular traffic Flashcards

1
Q

Is the nuclear envelope continuous with the ER?

A

yes

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2
Q

What is the main difference of function of the SER and RER

A

RER: Protein synthesis
SER: Lipid synthesis

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3
Q

What does the SER do?

A

1) synthesis of lipids
2) Synthesis of steroid hormones
3) Storage and release of Ca2+
4) Detox

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4
Q

Give examples of where in the body has a dense volume of SER

A

Liver and adrenal cortex

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5
Q

Give an example of a protein made in the cytosol

A

AKT, synthesised by free ribosomes

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6
Q

What is the process of proteins being transported in the ER during protein synthesis called?

A

Co-translational translocation

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7
Q

How does a ribosome bind to the RER?

A

A signal sequence is synthesised in the ribosome through the mRNA, which allows it to attach to an SRP. The SRP then attaches to an SRP receptor in the rough ER membrane

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8
Q

What happens to the SRP once the ribosome has binded to the ER membrane?

A

It will detach from the ribosome, and disassociate from the SRP receptor

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9
Q

What is the process of a protein being released from the cell called?

A

Exocytosis

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10
Q

What is glycosilation of proteins and what does it do

A

The addition of a sugar to a protein
Acts as:
- Quality control
- Recognition
- Protection

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11
Q

Where does the sugar attach to the protein during glycosilation

A

On the asparagine side chain (C2H3NO)

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12
Q

In what direction is the protein read?

A

3’ -> 5’

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13
Q

What happens if a protein is correctly folded?

A

3 glucose are cleaved from the N-linked olgiosaccharide

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14
Q

What happens if a protein is uncorrectly folded?

A

Glucosyl transferase adds a single glucose back. Calnexin (membrane bound) then binds to the unfolded protein to prevent aggregation. From there glucosidase releases calnexin from protein to be reviewed and is let out of ER or will be refolded again

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15
Q

What happens to the protein if it is misfolded too many times?

A

Exits the ER through a protein translator complex, N linked olgiosaccharide is cleaved, and then moves through a proteasome to be degraded (in the cytosol)

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16
Q

What is the UPR?

A

The unfolded protein response is a response to the build up of misfolded proteins in the ER lumen.
1) inhibit protein synthesis
2) degrade all misfolded proteins
3) Increase transcription of chaperones (eg BiP, Calnexin and calreticulin)

17
Q

What happens if the UPR does not succeed in resolving the number of proteins?

A

Apoptosis :(

18
Q

What is the “pulse chase” experiment?

A

Originally created by George Emil Palade, it was an expiremtn that proved the theory of exocytosis

19
Q

How many pathways are there in the cell?

A

3, exocytosis, endocytosis and retrieval pathways

20
Q

Where do COPII coated vesicles come from?

A

The Endoplasmic reticulum

21
Q

Where do COP I coated vesicles come from?

A

The Golgi

22
Q

Where do clarithin coated vesicles come from?

A

From the plasma membrane
between Golgi and Endosomes

23
Q

What happens with the Rab-GTP in membrane fusion?

A

binds to a rab effector

24
Q

Once the Rab-GTP effector complex has been created? what happens next?

A

the v(esicle)-snare and t(arget)-snare create a complex. From there, the t(snare) disassociates from the vesicle and the vesicle forms with the target membrane

25
Q

What happens to Rab-GTP once the vesicle has formed up with the membrane?

A

Rab-GTP disassociates from vesicle and is reduced, Rab-GDP then binds to GDI to keep it inactive

26
Q

What side of the Golgi receives packages from the ER?

A

The cis face

27
Q

What side of the golgi sends packages onwards?

A

The trans face

28
Q

What is the function of the golgi

A

To further process the proteins and olgiosacharide chains