Lecture 17 Flashcards

1
Q

True or False: Vesicular transport is Bidirectional

A

True

it is technically both directional and bidirectional (retrieval pathways are what makes it bidirectional)

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2
Q

What determines where a vesicle will end up and how it gets there?

A

the composition of it’s membrane and molecular markers on the surface of that membrane AND complementary receptors on the target membrane.

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3
Q

describe the location of the coat on coated proteins

A

on the cytosolic side of the membrane

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4
Q

What are the 2 major functions of the coat on coated vesicles?

A

Concentrates selected proteins for transport

Molds the vesicle to form a basket-like lattice (gives shape to the membrane)

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5
Q

The coat is _____ when the vesicle reaches the target membrane

A

discarded

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6
Q

What is the function of COPI?

A

mediates transport from the golgi cisternae

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7
Q

What is the function of COPII?

A

Mediates transport from the ER

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8
Q

What is the function of Clathrin-coated vesicles?

A

mediates transport from the golgi and from the plasma membrane

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9
Q

Describe the structure of a clathrin subunit and give the term that describes the structure they form.

A

3 large and 3 small polypeptide chains that come together to form a “3 legged structure” called the

Triskeleton

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10
Q

where are triskeleton’s found, and describe their structure in geometric terms.

A

Found on the cytosolic side of the membrane

basket-like structure of hexagons and pentagons that form coated pits

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11
Q

in clathrin coated vesicles, what forms the second layer between the clathrin cage and the membrane-bound cargo receptors?

A

adaptor proteins

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12
Q

Assembly of a protein molecule coat induces what effect on the membrane?

A

curvature

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13
Q

what type of recuitment of membrane and cargo molecules occurs in a vesicle?

A

selective

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14
Q

what are cargo receptors bound to?

A

cargo molecules on one end and adaptor proteins(which will be attached to a clathrin subunit) on the other

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15
Q

What family of molecules plays a major role in coat assembly, vesicle formation, and protein trafficking?

A

Phosphoinositides (PI)

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16
Q

What do different organelles have in order to facilitate interconversion?

A

unique sets of PI kinases and Phosphatases

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17
Q

What is the purpose of Phosphatidylinositol?

A

interconversion occurs to change it between various phosphoinisitides to control the recruitment and binding of adaptor proteins for the specific needs of that organelle/domain.

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18
Q

Define what interconversion is

A

rapid cycles of phosphorylation and dephosphorylation at the 3’, 4’, and 5’ positions of phosphoinositides to form various derivatives.

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19
Q

What part of Phosphoinositides is recognized by proteins?

A

the head group (inositol to be exact) that serves as a “signature”

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20
Q

What are BAR domains?

A

proteins with “coiled coils” that bend membranes

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21
Q

How do BAR domains bend membranes?

A

they have a positively charged inner surface that interacts with the negatively charged lipid head groups of the membrane (bends it)

22
Q

What removes clathrin coats from vesicles? how does this process happen?

A

Dynamin removes clathrin coats by first forming a ring around a clathrin bud.

The PIP2 binding domain and GTPase domain help “pinch” the membrane together

Dynamin recruits other proteins to “distort the lipid bilayer” and the vesicle looses it’s coat.

23
Q

Once dynamin recruits other proteins to distort the lipid bilayer, how are the adaptor proteins unbound?

A

PIP2 is degraded once the vesicle looses it’s clathrin coat and that weakens the binding of adaptor proteins.

24
Q

what protein physically peels off the clathrin coat?

A

HSP 70 chaperone protein and it uses ATP to do this

25
What are Rab protiens and what do they do?
Rab proteins are monomeric GTPases that play a central role in the specificity of vesicular transport
26
Compare and contrast the inactive and active forms of Rab protein. where are these found?
Inactive: Rab in the GDP-bound form ; found in the cytosol (soluble form) Active: Rab in the GTP-bound form ; found in the membrane
27
What are Rab effectors and where are they found?
motor proteins/tethering proteins that the active form of Rab binds to in the target membrane
28
(Rab Proteins) | name the sub-cellular location of Rab1
ER and Golgi
29
(Rab Proteins) | name the sub-cellular location of Rab3A
Synaptic vesicles and secretory vesicles
30
(Rab Proteins) | name the sub-cellular location of Rab5
Early endosomes, the plasma membrane, and in clathrin-coated vesicles.
31
What is the general function of snares? what are the 2 types?
they catalyze the fusion of vesicles with membranes v-SNAREs and t-SNAREs
32
explain the locations of vSNAREs and tSNARES and how they interact
v: vesicle membrane t: target membrane they wrap around each other to lock 2 membranes together
33
what is the first step of docking and the first step of fusion?
docking: the rab effector binds to RabGTP fusion: the trans-SNARE complex is formed
34
define the Rab5 domain on an endosome membrane
a "soft spot" of phosphorylated PI's, filamentous tethering protiens, and Rab effector proteins in the membrane where the vesicle can be more easily received into the cell
35
describe how Rab5 domains are formed
Rab5-GEF adds a phosphate to create Rab-GTP (from Rab-GDP) Rab5-GTP activates the PI 3-kinase which creates PI(3)P (on the membrane) PI(3)P creation recruits more Rab5-GEF, whose repeated activity form the Rab5 domain
36
describe how a trans-SNARE complex is dissociated
NSF (activated by an accessory protein) hydrolyzes ATP to untangle the transSNARE complex
37
what are newly synthesized proteins packaged into? where do these vesicles originate?
COPII coated transport vesicles they bud off the ER
38
What role to exit signals have in the formation of transport vesicles from the ER?
they are recognized by receptors on the COPII (this is what keeps the process selective)
39
What happens to incompletely folded/mislfoded proteins that enter the ER?
they are retained in the ER by binding to BiP or calnexin then they are degraded
40
compare and contrast homotypic and hetertypic vesicle fusion. What does this result in?
homo: describes vesicles from the same compartment hetero: describesV's from a different compartment these form vesicular tubular structures
41
what is crucial to the process of vesicle fusion? where re these found?
vSNAREs and tSNAREs both vesicles contribute both of these to the process
42
how to vesicular tubular clusters migrate around the cell?
they use motor proteins to crawl along microtubules
43
retrieval transport vesicles use what type of coat, and what is their origin/destination?
COPI coat moving from cis Golgi back to the ER
44
What does the retrieval pathway depend on? give 2 examples of these
ER retrieval signals at the C terminus ``` KKXX (in the ER) KDEL sequence (in soluble proteins) ```
45
what is the main difference between KKXX and KDEL ER retrieval signals?
KKXX interacts with COPI directly while soluble proteins require a KDEL receptor to be packaged into COPI vesicles
46
list and describe the 2 faces of the Golgi
Cis: network of fused vesicular tubular clusters arriving from the ER (proteins/lipids enter here) Trans: region that allows the exit of secretory vesicles (part of secretory pathway)
47
what lies between the cis and trans faces of the golgi?
the medial cisterna of the golgi
48
Describe the cisternal maturation model that describes the golgi apparatus.
Says that the cis matures into the medial, and then those mature into the trans
49
Describe the vesicular transport model that describes the golgi apparatus.
States that these 3 portions of the golgi are static and their vesicles are replenished as they are used
50
Where can rab-GTP be found? what about Rab-GDP?
Rab-GTP: on the vesicle with the cargo in it Rab-GDP: bound to the GDI?
51
True or false: during docking, the Rab-GTP interacts with the membrane of the target cell before the SNAREs can interact with one another. explain why
False: Rab-GTP interacts with the Rab effector (a tethering protein that extends out from the target cell's membrane) THEN the V and T SNARES can interact and form the transSNARE complex