Protein Trafficking Flashcards

1
Q

What are the three domains of the endoplasmic reticulum and their functions?

A

Smooth ER - lipid metabolsim

Rough ER - protein synthesis

ERGIC - vesicles exit to golgi

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What are two destination pathways for proteins?

A

Cytosolic pathway

Secretory pathway

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What are two ways proteins get into the ER?

A

Co-translational translocation

Post-translational translocation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What is the role of the signal recognition particle?

A

SRP binds the signal sequence, halting translation.

Also binds the SRP receptor on the RER

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

What is the function of the translocon?

A

To allow proteins to be translated into the ER and insert transmembrane portions into the membrane

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What is the role of Hsp70 and Hsp40?

A

Maintains the protein in an unfolded state so that it can be transported to the ER.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

What is the role of Sec62/63?

A

Recognizes the signal sequence of a completed polypeptide and causes translocon to open

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

What is the function of BiP?

A

Internal chaperone that acts as a molecular ratchet to drive translocation into the ER.

ATP-dependent

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

How does a transmembrane portion enter the membrane?

A

Exits the translocon laterally after it is translated.

Multiple domains mediated by SRP

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What four protein processing mechanisms occur in the ER?

A
  • BiP mediates folding
  • Protein disulfide isomerase
  • N-linked glycosylation
  • GPI anchors
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

What are two types of export signals that trigger export from the ER to the golgi?

A
  • Di-acidic or di-hydrophobic AA signals in the cytosolic domain
  • GPI anchors
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

What is the ERES

A

Specialized region of the ER where proteins and phospholipids are exported.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

How are proteins transported between the ER and golgi?

A

Proteins in the lumen of one organelle are packaged into budding transport vesicles, then released to the lumen of the recipient organelle

topology is maintained

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

What is the default pathway?

A

Pathway by which unmarked proteins in the ER can be packaged and transported to the golgi

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

What is the ERGIC?

A

ER-Golgi Intermediate complex

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

What is the role of the Golgi Apparatus?

A
  • Process and sort proteins coming from ER
  • Transport to endosomes, lysosomes, PM, or secretion
  • most glycolipids and sphingomyelin are synthesized here
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

What are the four regions of the Golgi and their functions?

A

Cis - receives molecules from the ERGIC

Medial and trans - modifications

Trans-Golgi network - sorting and distribution

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

What occurs to N-linked oligosaccharides

A
  • Mannoses are replaced with NAG, galactoses, and sialic acids
  • Fucose is added to origin NAG
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

How are the N-linked oligosaccharides of lysosomal proteins modified?

A

Mannose phosphorylation

Recognized by a mannose-6-phosphate receptor in the trans Golgi Netowrk

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

What is O-linked Glycosylation?

A

Carbohydrate addition ot serine and threonine in the Golge

21
Q

What happens to proteins that are destined to stay in the Golgi?

A

They are associated with the membrane and contain signals that prevent packaging and transport

22
Q

What are the three routes that transport from the Golgi to the cell surface can occur?

A
  • Direct transport
  • Recycling endosomes
  • Regulated secretory pathways
23
Q

What is regulated release and what types of molecules are regulated this way?

A

Contents are stored in granules until signals direct their fusion with the PM

Hormones and neurotransmitters

24
Q

What is the function of COPII-coated vesicles?

A

Carry proteins forward from the ER–>ERGIC–>Golgi

25
Q

What is the function of COPI-coated vesicles?

A

Bud from ERGIC or Golgi and carry their cargo backwards to earlier compartments

26
Q

What is the function of clatherin-coated vesicles?

A

transport in both directions between the trans Golgi network, endosomes, lysosomes, and PM

27
Q

What is the KDEL sequence?

A

Tags ER-resident soluble proteins for return to the ER by COPI vesicles

28
Q

What is the role of Mannose 6-phosphate?

A

Tags soluble lysosomal enzymes and secreted lysosomal enzymes for transport to lysosomes via Clatherin coated vesicles

29
Q

What are ARF1 and Sar1?

A

Small GTP-binding proteins that regulate the formation of coated vesicles

30
Q

How are clatherin-coated vesicles formed?

A
  • GEF activates ARF1
  • ARF binds an adaptor protein
  • The adaptor protein binds the cargo
  • Clatherin binds to the adaptor protein
31
Q

What mediates interaction between transport vesicles and target membranes?

A

Tethering factors

Rab proteins (small-GTP binding porteins)

32
Q

What three things drive membrane fusion?

A

vSNARES

tSNARES

Dynamin

33
Q

How do vesicles dock?

A

Active Rab proteins bind membrane tethering factors

Tethering factors bind coat proteins and the coat is removed.

34
Q

How do vesicles fuse?

A

The membranes are pulled together and fused via vSNARES and tSNARES interacting

35
Q

What is the mechanism of vSNARE and tSNARE interaction?

A

SNARE proteins have a central coiled-coil domain

Responsible for zipping the two SNARES together

36
Q

What are lysosomes?

A

membrane-enclosed organelles containing enzymes to break down all types of biological polymers

37
Q

What are lysosomal storage diseases?

A

Diseases that result from mutations in lysosomal enzymes

undegraded material accumulates in the lysosomes

38
Q

Most lysosomal enzymes are…?

A

Acid Hydrolases active at pH 5

39
Q

What is the significance of lysosomal enzymes only being active at pH 5?

A

Prevents cell contents digestion if the lysosome membrane breaks down

40
Q

How does material for digestion get into the cell?

A

Endocytosis

41
Q

How are lysosomes formed?

A

When transport vesicles fuse with a late endosome

42
Q

What two pathways intersect at endosomes?

A

Secretory and endocytic pathways

43
Q

What is the function of early endosomes?

A

Fuse with endocytic vesicles from PM

Separate molecules for recycling from molecules destined for degradation in lysosomes

44
Q

What is the function of recycling endosomes?

A

Serve as a site for molecules that are to be transported back to the plasma membrane

45
Q

What is the function of late endosomes?

A

Carry molecules to be degraded by lysosomes

46
Q

What happens during the maturation of late endosomes?

A

Transport vesicles carrying acid hydrolases fuse with late endosomes, forming lysosomes

47
Q

What are phagolysosomes?

A

Specialized lysosomes in phagocytic cells

48
Q

What is autophagy?

A

Digestion of the cell’s own components

49
Q

What normal roles does autophagy play?

A

Nutrient starvation - reutilized nonessential cellular components

Apoptosis