Unit 4 Flashcards

1
Q

What is the function of Ran GTPase in nuclear transport?

A

Regulates the binding and release of cargo proteins during import/export through nuclear pores.

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2
Q

What vesicle type moves proteins from the ER to the Golgi?

A

COPII vesicles.

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3
Q

What happens to proteins with a KDEL sequence?

A

They are retrieved back to the ER from the Golgi via COPI vesicles.

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4
Q

What types of bonds stabilize protein structures in the ER?

A

Disulfide bonds.

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5
Q

What is the role of the Unfolded Protein Response (UPR)?

A

Helps reduce ER stress by halting protein translation, degrading misfolded proteins, and increasing chaperone production.

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6
Q

What is the difference between one-pass and multi-pass membrane proteins?

A

One-pass proteins use a single stop-transfer sequence, while multi-pass proteins have multiple start and stop-transfer sequences.

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7
Q

How does glycosylation affect proteins?

A

It stabilizes proteins, aids in cell-cell communication, and determines protein destination.

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8
Q

What is autophagy?

A

A cellular process for degrading damaged organelles or proteins.

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9
Q

What triggers regulated exocytosis?

A

External signals, such as hormones or neurotransmitters.

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10
Q

What is the purpose of proteasomes?

A

They degrade misfolded or damaged proteins tagged with ubiquitin.

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11
Q

what is protein sorting

A

the process by which proteins are directed to specific locations within or outside the cell, this is guided by signal sequences

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12
Q

What are signal sequences

A

short stretches of AA that direct proteins to their appropriate cellular components

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13
Q

Free Ribosomes

A

Free ribosomes are located in the cytosol, they synthesize proteins that function in the cytosol, mitochondria, chloroplasts, nucleus, and peroxisomes

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14
Q

what are polyribosomes

A

cluster of free ribosomes translating the same mRNA simultaneously

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15
Q

Membrane Bound Ribosomes

A

ribosomes that are embedded in the ER, they synthesize proteins that are destined for secretion, incorporation into the plasma membrane or lysosomes

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16
Q

what proteins are made in membrane bound ribosomes

A

transmembrane, integral membrane proteins, soluble proteins for secretion, soluble proteins that will remain inside the ER, Golgi, or lysosomes

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17
Q

proteins from membrane bound ribosomes travel though vesicles in the order of

A

vesicles to golgi to surface (proteins in plasma membrane) or to be secreted
or
vesicles to golgi to lysosomes

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18
Q

Nuclear Transport of proteins

A

proteins that contain nuclear localization signals (NLS) are recognized by nuclear import receptors, the nuclear envelope allows transport through nuclear pore complexes

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19
Q

Role of RAN in Protein transport

A

Ran is a GTPase that provides energy for the import and export of proteins across the nuclear envelope by facilitating cargo binding and release though nuclear pores

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20
Q

Steps of RAN usage (steps of how proteins enter the nucleus)

A

must have NLS, the NLS signal is recognized by receptor in cytoplasm called importin, the receptor picks up the nuclear protein in the cytosol and directs it to the nuclear pore, importin grabs onto the repeated AA sequences at the rim of the pore making a passage way pulling the proteins though
once inside the nuclear envelope, the protein encounters RAN, RAN GTP binds to receptor causing it to release cargo, importin carrying the GTP is transported back through pore and hydrolyzed back to GDP to start process over

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21
Q

mitochondrial transport

A

proteins containing targeting signals that direct them to the mitochondrial surface, where they are translocated across the membrane

22
Q

peroxisomal transport

A

proteins are imported post translationally guided by peroxisomal targeting signals

23
Q

endomembrane system

A

group of organelles including the ER, Golgi, lysosomes, and vesicles involved in transport and processing of all proteins destined for secretion or lysosomal use

24
Q

transport of proteins to the endomembranous system

A

proteins moving from ER onward through endomembrane system are transported though transport vesicles which become loaded w cargo proteins they pinch off from one organelle and travel to the next
protiens with ER signal sequences are directed to the ER where they begin the secretory pathway

25
Mechanism of transport of proteins to the RER
proteins enter the ER cotranslationally, insoluble proteins are either retained inside the ER or packaged for specific destinations
26
Where do soluble RER proteins end up?
in lumen of ER or secreted outside the cell
27
Soluble RER protein sequence signals
proteins made by ribosomes display ER signal signal sequences which is normally present at the N term of new protein ER sequence, recognized by signal recognition particles SRP present in cytoplasm protein synthesis stops, SRP locates SRP receptors on ER surface and binds to it, SRP released passing ribosomes to translocation channels in ER membranes
28
ER transport Mechanisms: membrane and transmembrane proteins
interact with ER membrane where their insertion and orientation are determined by stop transfer and signal anchor sequences: single pass or multipass
29
One pass membrane proteins
one membrane spanning sequence, N term signal sequence initiates transloction as it does for soluble protein stops translocating when protein being synthesized displays stop signal sequence
30
multipass membrane proteins
on internal rather han N terminus signal sequence is used to start protein transfer and signal will remain in protein never removed, moves back and forth across lipidbilayer
31
Protein Processing: Disulfide bonds and glycolsylation
disulfide bonds are formed between two cys AA, frmed by the oxidation of these two pairs catalyzed but disulfide isomerase that is inside the ER lumen, helps to stabilize proteins, enhance protein folding and function
32
Protein processing glycosylation
Proteins are converted to glycoproteins , N linked is the most common, begins in ER ends in Golgi, for O linked glycosylation it occurs only in golgi
33
Chaperones
proteins that assist in correct folding of other protiens
34
Proteasomes
Degrade misfolded or damaged proteins
35
Chaperone Malfunction
can cause diseases, proteins don't fold properly get clogs- cystic fibrosis: result from mis folding of the CFTR protein
36
What is the Unfolded Protein Response
UPR: is a cellular stress response related to the ER, it aims to restore normal ER function when ER is overwhelmed and cant check all proteins, sends more chaperone proteins
37
Type 2 diabetes and UPR
chronic excess sugar in the diet makes beta cells in the pancrease work in overdrive, as insulin secreting cells are called upon to produce more and more insulin they get overwhelmed and UPR gets activated but if not strong enough/ not enough UPR, trigger cell death
38
movement of vesicles from ER to Golgi
Vesicles transport proteins synthesized in the ER to Golgi for further processing
39
Function of Golgi in intracellular transport
golgi modifies proteins though glycosylation sorting them to various destinations
40
Two faces of the golgi and their function
proteins are futher modified and sorted in the golgi, the Cis face of the Golgi recieves vesicles from rough ER filled with new synthesized proteins trans face buds off transport vesicles filled with modified proteins destined from further modification
41
constitutive secretion
continuous process does not require signals
42
regulated exocytosis
stores proteins in vesicles and releases in response to signals
43
lysosomes
contain digestive enzymes - main digestive organism identified by mannose 6 phosphate tags , critical in cellular waste processing
44
lysosomal storage diseases
causes by enzyme deficiencies lead to accumulation of undigested substrates: Tay-Sachs disease
45
autophagy
cell recycling
46
macro autophagy
cell debris or damaged organelles get surrounded by membrane then forming autosome
47
micro autophagy
cytoplasmic components enter lysosome by invagination of lysosome membrane
48
chaperone mediated autophagy
some chaperones bind to unfolded or misfolded proteins which target then lysosomes, very specific
49
ER to Golgi Transport
COPII vesicles move protiens from ER to Golgi
50
Golgi to ER
COPI Vesicles move proteins from golgi back to ER
51
What ensures proper localization of ER to Golgi transport
KDEL retrieval signals
52
Mannose 6 phosphate Tag
directs enzymes to lysosomes