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BIOL 331 > Markers and Random Proteins > Flashcards

Markers and Random Proteins Flashcards

(57 cards)

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1
Q

Sec 61 (marker for?)

A

rER

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2
Q

BIP

A

Chaperone in the ER lumen that loves unfolded proteins.

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3
Q

Overlap of transferrin and Opioid receptors

A

Early endosome

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4
Q

EGFR

A

Late Endosome

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5
Q

Acid Hydrolases (ex: phosphatase)

A

Lysosome

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6
Q

Atg9

A

Autophagy

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7
Q

PI(3)P

A

Endosomes

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8
Q

Sec 61

A

4 of them + associated proteins make the ER translocator

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9
Q

Sec 62/63

A

Associated with ER translocator. They recruit BIP which helps with post-translational translocation

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10
Q

PDI

A

Binds proteins to be retrotranslocated to break their bad disulphide bonds

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11
Q

PERK

A

UPR response (upregualate and activate chaperones, promote protein degradation, stop protein synthesis)

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12
Q

ATF6

A

UPR response (upregualate and activate chaperones, promote protein degradation, stop protein synthesis)

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13
Q

IRE1

A

UPR response (upregualate and activate chaperones, promote protein degradation, stop protein synthesis)

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14
Q

Dynamin

A

Wraps around neck of budding vesicle and then hydrolyses GTP to constict. May also recruit lipid modding enzymes to help with fusion

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15
Q

AP5

A

Involved in endosomal vesicular transport

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16
Q

Rab7

A

On retromer coats (bring MP6-R back to TGN)

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17
Q

ARF

A

Form COPI coat + golgi made clathrin coat

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18
Q

Sar1

A

Form COPII coat. Once activated, an ampiphillic alpha helix pops out and inserts into cytosolic leaflet. Then, it recruits coat-forming proteins.

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19
Q

Sec 23/24

A

Gather the cargo for COPII coats

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20
Q

Sec 13/31

A

Form the COPII outer shell

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21
Q

GDI

A

Binds inactive Rab to make it soluble in the cytosol.

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22
Q

GlcNAc

A

N-Acytylglucosamine

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23
Q

Calreticulum + Calnexin

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A

Calcium activated lectins that bind sugars on proteins in the ER with only one glucose.

They help them associate with lectins chaperones that reduce cys residues, prevent aggregation and keep them from leaving the ER.

24
Q

How is COPII dissembled?

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A

Coat recruitment GTPases are always working towards hydrolyzing Sar 1 to make its tail pop out thus, vesicle only forms when it can outrun this.
HOWEVER
After vesicle formation, the coat is very strong without Sar 1 and will only dissemble after being phosphorylated by kinases on the target.

COPI however will just undo soon after pinching off.

25
How does clathrin uncoat?
PIP phosphatase was packaged in and it depletes the PIP that binds the adaptor. Auxilin activates the ATPase activity of Hsp70 chaperones which use that energy to peel off the coat. Mechs in place to ensure this doesn't happen until the vesicle is done being made.
26
When vesicles pinch off which sides of the leaflets are brought together?
The two non-cytosolic sides
27
How does glycosylation work as a timer?
2 glucoses immediately cut off so calreticulum and calnexin bind. Cycle of unbinding and binding them until proper folding as last glucose removed and put back on. During this, mannose is being trimmed and eventually will be recognized by retrotranslocator lectins. Thus must fold b4 time runs out.
28
What happens in each part of the Golgi?
CGN: sorting phosphorylation of lysosomal protein oligosacs CC: Mannose removal MC: Mannose removal + GluNAc added TC: Sialic acid + Gal + NANA added TGN: Sorting + sulfation of carbs and tyrosine residues + add gal + add sialic acid
29
What is the difference between high mannose and complex sugars. What determines what happens?
HM: nothing added after initial trim Complex: add stuff after intiail trim *Depends on where the sugars are in the protein and how accessible they are. to enzymes.
30
what are the 3 fates for proteins leaving golgi
secretory vesicles (regualted exocytosis) direct to PM lysosomes (if MP6)
31
what is a marker for recycling endosomes and early endosomes
transferin (holds Fe)
32
what is transcytosis?
movement from one side of membrane to another (endocytosis to early endosome to recycling endosome to PM) ex: in babies binding to cargo receptor depends on the pH of each side of the epithelial cell
33
where do receptors go when they are done their job?
return to pm (without or with ligand) ex: LDL-R and TFR+TF respectively degraded ex: EGFR trancytosed
34
what change as endosomes mature?
Rabs PIPs and SNARES
35
how are endosomes matured
V type ATPass lowers pH intralumenal vesicles made to house receptors TGN deliverd lysosomal proteins
36
how are intralumenal vesicle made?
patches of endosomal membrane invaginate into lumen and pinch off to form a multivesicular body. this happens when multiple ubiquitin tags bind the cytosolic sodd of a cargo capture protein (or membrane cargo) . then ESCRT proteins bind ubiquitin and PIPs and decide to defrom the membrane to make an internal vesicle.
37
t
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38
what is the endocytosis sorting station
early endosome
39
where do things go from early endosome
lysosome or recycled to PM
40
what are LDLs? How are they reglated by the cell?
BIG molecules that bring cholesterol into the cell. cells make more LDLR when they are low on cholesterol and they turn off its synthesis (along with cholesterol synthesis) when levels are high
41
how do LDLRs join clathrin coated pit?
diffuse across membrane till they see AP2 in a forming clathrin pit
42
what happens to LDL and LDLR after endocytosis
break up in early endosome due to lower pH LDL goes to lysosome and cholesterol ester is hydrolyxed to free the chloesterol cholesterol used to make new membranes LDLR recycled to PM
43
what kind of endocytosis makes big vesicles
phago
44
how do protozoa and euks used phago
proto: to eat euk: to eat dead cells and invaders
45
what determines phago size
what it ate
46
what happens to things lysosome cant digest
become residual bodies that can be exocytosed
47
how does phago work
something binds receptors and then pseudopod extension forms
48
what is macropinocytosis
pinkcytosis triggered by receptors to form actun ruffles that make large fluid filled sacs. INC bulk fluid uptake x10
49
what is pinkcytosis
constitutive cell drinking that used short lived clathrin coated pits OR caveolae
50
what is I cell disease
mannose never phosphorylated in CGN so no MP6 and thus no acid hysrolases in lysosomes
51
where does mannose 6 P come from
add phosphorylated glucnac then cleave off the glucna so only phosphate on mannose
52
when do retromers assemble
cystoplamic tails of cargo receptors avalible curved bilayer avalible PI(3)P maker avalible retromer stabilizes curvature after binding
53
what happens if m6p proteins are secreted on accident
M6PRs catch them with receptro mediated endocytosis
54
when do M6PRs bind and unbind
bind at 6.5 ph unbind at 6
55
what vesicles carry mp6rs (coat type)
clathrin
56
what is autophagy
engulfing cytosol to get things in the cell too big for proteosome degradation system ex: dead organells
57
how are lysosomes made
late endosome fuses with preexisting lysosome

BIOL 331 (12 decks)

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