Class 12 - Transport From ER Through Golgi (PRETTY GOOD) Flashcards

1
Q

ER exit site

A

Specialized regions of ER where COPII-coated transport vesicles destined for Golgi bud off.

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2
Q

Exit signal

A

Present in ER transmembrane proteins to be recruited into vesicles. Recognized by adapter proteins of inner COPII coat.

Soluble cargo proteins in ER lumen also have exit signals, recognized by transmembrane proteins, which serve as cargo receptors.

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3
Q

Homotypic fusion + 3 steps

A

The fusion of vesicle membranes from the same compartment.

  1. NSF protein pries apart SNAREs.
  2. Matching t and v-SNAREs on vesicles interact and force them together
  3. Vesicles fuse, creating vesicular tubular clusters
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4
Q

Heterotypic fusion

A

Vesicle fusion between membranes of different compartments.

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5
Q

Vesicular tubular cluster

A

Structures formed when ER-derived vesicles fuse with one another. Function as transport containers that bring materials from ER to Golgi.

Bud off transport vesicles of their own - COPI-coated. Function as retrieval pathway, carrying proteins back to ER (escapees, receptors, SNAREs).

Move toward Golgi by means of motor proteins which walk along microtubules.

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6
Q

Retrieval pathway

A

Between ER and Golgi: Done by COPI-coated vesicles which bud off from vesicular tubular clusters, carrying proteins back to ER.

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7
Q

ER retrieval signal

A

Present in ER-residing proteins and bind to COPI coats, allowing their transport back to ER after escaping.

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8
Q

KKXX sequence

A

An ER retrieval signal found at the C-terminus of ER membrane proteins (SNAREs, cargo receptors).

Allows them to enter the retrieval pathway back to ER.

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9
Q

KDEL sequence

A

ER retrieval signal found in soluble ER resident proteins, such as BiP, at C-terminus.

Bind in Golgi - lower pH - and release in ER.

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10
Q

KDEL receptor

A

Multipass transmembrane protein. Binds to KDEL sequence and packages any protein displaying it into COPI-coated retrograde transport vesicles (part of retrieval pathway).

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11
Q

Cis face

A

The entry face of the Golgi.

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12
Q

Trans face

A

The exit face of the Golgi.

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13
Q

Cis Golgi network (CGN)

A

Collection of fused vesicular tubular clusters arriving from ER.

Proteins which don’t belong sent back to ER.

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14
Q

Trans Golgi network (TGN)

A

Proteind are sorted and exported to lysosome, secretory vesicles, or plasma membrane.

Proteins not to be exported are returned to earlier compartment.

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15
Q

Cis cisternae

A

First Golgi processing compartment.

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16
Q

Medial cisternae

A

Second Golgi processing compartment.

17
Q

Trans cisternae

A

Final Golgi processing compartment, where glycosylation is completed.

Lumen of this is continuous with the TGN.

18
Q

Vesicle transport mechanism

A

Golgi cisternae are static compartments. Movements of cargo accomplished by forward-moving transport vesicles
(COPI), budding from one cisterna and fusing with the next.

19
Q

Cisternal maturation mechanism

A

Golgi is dynamic structure. Entire cisternae move through the stack. Vesicular tubular clusters from ER become cis-Golgi network, which mature to become medial and trans. Resident Golgi enzymes transported backwards as cisterna mature. Trans-cisterna disappears as vesicles bud off.

20
Q

GRASPs

A

Golgi matrix proteins called Golgi reassembly and stacking proteins. Form a scaffold between adjacent cisternae, giving Golgi stack structural integrity.

21
Q

Golgins

A

Golgi matrix proteins which form long tethers, composing a forest of tentacles that extend from the surface of the Golgi stack.

May contain binding sites for different Rab proteins; Initially select which part of Golgi stack transport vesicles engage with

22
Q

Golgi apparatus

A

Functions: Carbohydrate synthesis, makes all cell’s polysaccharides, sorting/dispatching station for ER products.

Structure: CGN and TGN sandwiching the cis, medial, and trans cisterna.

All resident proteins are membrane bound.

23
Q

Glycosylation in the Golgi

A

Takes place at membrane, in cis, medial, and trans cisternae.

Benefits:
1. Mark progression of protein folding for chaperones.
2. Participate in sorting in trans Golgi network
3. Keep other molecules at a distance—resistant to digestion or pathogens.
4. Cell-cell recognition
5. Signaling (Notch)

24
Q

Components of COPII vesicle (5)

A
  1. Cargo from ER
  2. Cargo receptors
  3. Sar1 (GTPase)
  4. Coat proteins
  5. v-SNAREs
25
Q

2 ways to leave ER in COPII-coated vesicles

A
  1. Selective - ER exit signal
  2. Default - No ER exit signal
26
Q

How do cells respond to protein folding issues?

A

They make an excess of proteins to ensure enough fold up properly

27
Q

Reasons for glycosylation in Golgi

A

Protein folding, protein sorting, resistance to proteases, protection of cell, cell-cell recognition or adhesion, antigenic properties, regulatory roles