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BIOL 331 > Markers and Random Proteins > Flashcards

Markers and Random Proteins Flashcards

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

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?

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
Q

How does clathrin uncoat?

A

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
Q

When vesicles pinch off which sides of the leaflets are brought together?

A

The two non-cytosolic sides

27
Q

How does glycosylation work as a timer?

A

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
Q

What happens in each part of the Golgi?

A

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
Q

What is the difference between high mannose and complex sugars. What determines what happens?

A

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
Q

what are the 3 fates for proteins leaving golgi

A

secretory vesicles (regualted exocytosis)
direct to PM
lysosomes (if MP6)

31
Q

what is a marker for recycling endosomes and early endosomes

A

transferin (holds Fe)

32
Q

what is transcytosis?

A

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
Q

where do receptors go when they are done their job?

A

return to pm (without or with ligand)
ex: LDL-R and TFR+TF respectively
degraded ex: EGFR
trancytosed

34
Q

what change as endosomes mature?

A

Rabs PIPs and SNARES

35
Q

how are endosomes matured

A

V type ATPass lowers pH
intralumenal vesicles made to house receptors
TGN deliverd lysosomal proteins

36
Q

how are intralumenal vesicle made?

A

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
Q

t

A

h

38
Q

what is the endocytosis sorting station

A

early endosome

39
Q

where do things go from early endosome

A

lysosome or recycled to PM

40
Q

what are LDLs? How are they reglated by the cell?

A

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
Q

how do LDLRs join clathrin coated pit?

A

diffuse across membrane till they see AP2 in a forming clathrin pit

42
Q

what happens to LDL and LDLR after endocytosis

A

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
Q

what kind of endocytosis makes big vesicles

A

phago

44
Q

how do protozoa and euks used phago

A

proto: to eat
euk: to eat dead cells and invaders

45
Q

what determines phago size

A

what it ate

46
Q

what happens to things lysosome cant digest

A

become residual bodies that can be exocytosed

47
Q

how does phago work

A

something binds receptors and then pseudopod extension forms

48
Q

what is macropinocytosis

A

pinkcytosis triggered by receptors to form actun ruffles that make large fluid filled sacs. INC bulk fluid uptake x10

49
Q

what is pinkcytosis

A

constitutive cell drinking that used short lived clathrin coated pits OR caveolae

50
Q

what is I cell disease

A

mannose never phosphorylated in CGN so no MP6 and thus no acid hysrolases in lysosomes

51
Q

where does mannose 6 P come from

A

add phosphorylated glucnac then cleave off the glucna so only phosphate on mannose

52
Q

when do retromers assemble

A

cystoplamic tails of cargo receptors avalible
curved bilayer avalible
PI(3)P maker avalible

retromer stabilizes curvature after binding

53
Q

what happens if m6p proteins are secreted on accident

A

M6PRs catch them with receptro mediated endocytosis

54
Q

when do M6PRs bind and unbind

A

bind at 6.5 ph
unbind at 6

55
Q

what vesicles carry mp6rs (coat type)

A

clathrin

56
Q

what is autophagy

A

engulfing cytosol to get things in the cell too big for proteosome degradation system ex: dead organells

57
Q

how are lysosomes made

A

late endosome fuses with preexisting lysosome

BIOL 331 (12 decks)

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