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EOM 1 - Test 2 > Delidow - ER, Golgi, and Trafficking > Flashcards

Delidow - ER, Golgi, and Trafficking Flashcards

1
Q

What covers the rough ER?

A

Ribosomes

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2
Q

ERGIC

A

Vesicles exit to the Golgi apparatus

E.R. Golgi Intermediate Complex

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3
Q

What type of network is the endoplasmic reticulum (ER)?

A

Continuous Membrane Network

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4
Q

What is the structure of Golgi?

A

Stacked and polarized cisternae

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5
Q

Does the way a protein “faces” change as processing through secretory organelles?

A

No, topology of the secretory pathway is conserved

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6
Q

When is entry direction of protein determined?

A

Translation

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7
Q

Where are the ribosomes found which translate proteins destined for the secretory pathway?

A

Membrane bound ribosome

or Free Ribosomes

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8
Q

How to proteins get into the ER?

A

Co-translational translocation (during)

Post-translational translocation (after)

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9
Q

Co-translational Translocation

A

Proteins synthesized on membrane-bound ribosomes enter the ER during translation

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10
Q

Post-translational translocation

A

Protesins translated on free ribosomes move into the ER after translation

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11
Q

Wat is the first step in co-translational translocation?

Next?

A

Signal Recognition Particle (SRP) binds signal sequence, arresting translation

Complex binds to SRP Receptor on RER mebrane, SRP released

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12
Q

Once the SRP disociated, when occurs next during co-translational translocation?

What is the fate of the signal sequence?

A

Ribosome binds translocon, signal sequence enters channel and translocon opens.

Translation resumes, polypeptide chains translocated across membrane

Signal sequence cleaved by signal peptidase and released into ER

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13
Q

Post-translational translocation

What drives the protein in the ER?

A

Protein translated by free ribosome, Hsp 40/70 maintain protein unfolded.

Signal sequence recognized, protein inserted through translocon.

BiP coats proteins, and drives proper folding (molecular ratcheting)

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14
Q

How does the translation of integral membrane proteins occur?

A

Translated on membrane bound ribosomes located on translocon

Signal peptidase translates internal until transmembrane sequence hits.

Ribosome finishes translating outside, ribosome bounces

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15
Q

What changes in a translocon following translocation of integral membrane proteins?

A

Conformational change of “arm” swinging shut the translocon

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16
Q

What mediates transmembrane insertion and direction of C/N terminus?

A

Internal Signal Sequence

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17
Q

BiP

A

Chaperone to aid in folding the polypeptide in the ER

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18
Q

Protein Disulfide Isomerase

A

Facilitates disulfide bonds after protein properly folded

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19
Q

N-linked Glocosylation

A

Oligosaccharide synthesized on a lipid carrier, preventing protein aggregation in ER

  • Sorting signals
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20
Q

GPI Anchors

A

Glycolipids assembled in the ER membrane, and added to C-terminus

(lipidatipon)

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21
Q

What function as ecport signals to move proteins from ER to Golgi?

A

Peptide Signals, di-acidic or di-hydrophbic AA signals in cytosol domain

GPI Anchors function as export signals

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22
Q

ERES

A

Specialized region of the ER where proteins and phspholipids bud to go to Golgi

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23
Q

What type of special signal does BiP have? What does this indicate about movement within the secretory system?

A

KDEL=needs to come back home

Movement is a two-way street

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24
Q

What do proteins targeted for export have to mark them?

A

Peptide and carbohydrate signals

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25
Q

How can unmarked proteins in the ER be transported to the Golgi?

A

Default pathway

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26
Q

What major processes occur at the Golgi?

What two major molecule classes are synthesized in the Golgi?

A

Proetins coming from ER are processed and sorted for transport to endosomes, lysosomes, plasma membrane, or secretion

Glycolipids, Sphingomyelin

27
Q

What Golgi compartment receives molecules from the ERGIC?

A

cis

28
Q

What Golgi complex(s) are most of the work done?

A

Medial and Trans

29
Q

What is the Golgi sorting and distrubiution center?

A

trans-Golgi Network

30
Q

What are the two theories for protein movement in the Golgi?

A

Stable Cisternae , Cisternal maturation Model

31
Q

What major modification occurs in the Golgi?

A

Carbohydrate portions of glycoproteins

N-linked oligosaccharides are modified

32
Q

What modifications are made to N-Linked Oligo’s in the Golgi?

What does this drive?

A

Mannoses are replaced w/ NAG, Galactoses, and Sialic Acids

FInal destination depends on “tags”

33
Q

What type of modification occurs to lysosomal proteins in the Golgi?

What recognizes these?

A

Mannose phosphorylation

Mannose-6-phosphate receptor (which transports them from the trans network)

34
Q

What is the destination of mannose-6-phosphate tagged proteins?

A

Lysosome

35
Q

What is O-linked glycosylation?

What does this form?

A

Carbohydrates added to Serine and Threonine

Proteoglyan

36
Q

What are the 3 ways transport from the Golgi to the Cell Surface occurs?

A
  1. Direct transport
  2. Recycling Endosomes
  3. Regulated secretory pathways
37
Q

Why must proteins be selectively packaged in the Golgi?

A

epithelial tissues are polarized and divided into two domains (apical/basolateral) which have specific proteins

38
Q

What is key to maintaining the fucntional organization in cells?

A

Selective Vesicular Transport

39
Q

What are transport vesicles from the ER coated with?

A

Cytostolic coat proteins

40
Q

COPII-Coated Vesicles

COPI-Coated Vesicles

Clathrin-Coated Vesicles

A

Carry proteins from the ER to the ERGIC and on to Golgi (forward)

Bud from ERGIC or Golgi and carry cargo back (backward)

Transport in both directions between the trans Golgi network, endosomes, lysosomes, and plasma membrane (Golgi and final f

estination)

41
Q

How are Mannose 6-Phosphate (M6P) signals coated?

Where are these destined for?

A

Clathrin

Lysosome

42
Q

What coat does KDEL use?

A

COP I

43
Q

What regulates coated vesicle foramtion?

How do they function?

A

Small GTP-binding proteins

GTP-binding recruits adaptor protein that mediate vesicle assembly by interacting with cargo and coat proteins

44
Q

What 5 things do vesicles need to form coat?

A
  1. Small G
  2. GEF
  3. Adaptor
  4. The Cargo
  5. The Coat
45
Q

What mediates interaction b/t transport vesicle and target membranes?

A

Tethering factors, Rab proteins

46
Q

What drives membrane fusion of vesicles?

A

vSNARES

tSNARES

Dynamin

47
Q

What can be said about G-proteins in relation to their targets?

A

They’re specific

48
Q

How does vesicle docking and fusion occur?

A

GTP-Rab (active) bind tethering factors

tethering factors bind coat proteins

SNAREs interact with eachother

Kind of like immune response w/selectin (weak), integrin (strong), and ICAM (sticky and strong)

49
Q

What is the role of SNAREs in vesical docking and fusion?

A

Membrane fusion of vesicle and target membrane

50
Q

What is the main structure of a SNARE, and why is this the case?

A

Central coiled-coil domain

Binds to others in “zipper” model, brings two membranes together

51
Q

Lysosomes

A

Membrane-enclosed organzelles w/enzymes to break down all types of biological polymers

52
Q

What do mutations in genes that encode lysosomes cause?

A

Lysosomal storage disease

53
Q

What are most lysosomal enzymes?

When are these activated?

What maintains this activity?

A

Acid Hydrolases (active at pH 5)

Proton pump

54
Q

How do lysosomes digest material?

A

Endocytosis

55
Q

What do endosomes represent?

A

Intersection between the secretory pathways and endocytic pathway

56
Q

What are three types of endosomes?

A
  1. Early Endosomes - separate recycling/destruction
  2. Recycling - passed to recyling endosomes, and back to plasma membrane
  3. Late - carry molecules to lysosome for destruction
57
Q

What is the fate for late endosomes?

How do they gain this function?

A

Lysosome

Transport vesicles carrying acid hydrolases from the trans-golgi network fuse with late endosomes

58
Q

Phagocytosis

A

Specialized cells that take up and degrage large particles

59
Q

Phagosomes

Phagolysosomes

A

Phagocytic vacuoles

Phagosome fused with lysosome

60
Q

Autophagy

Autophagosome

Example?

A

Internal cellular recycling system “self consumption”

Small area of cytoplasm or organelle enclosed in a vesicle which fuses with a lysosome and have its contents digested

Ex: Insect metamorphosis

61
Q

What is a role of autophagy in times of stress?

A

During nutrient starvation, autophagy degrades nonessential macromolecules for reutilization

62
Q

What impact does autophagy have with cancer?

A
  1. Cancer cells can utilize it to steal nutrients for their own evil plots
  2. Potential therapeutic avenue to defeat these jerks
63
Q
A

EOM 1 - Test 2 (18 decks)

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