Protein Synthesis in Nervous System Flashcards

(29 cards)

1
Q

What 3 main proteins do AA sequence for?

A

Cytosolic proteins
Nuclear/mitochondrial proteins
Membrane proteins

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2
Q

What are cytosolic proteins folded by?

A

Chaperones

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3
Q

What is N-acylation?

A

Transfer of an acyl group to the N terminus
Allows for better interaction with membrane proteins eg. G proteins

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4
Q

What is isoprenylation?

A

Thioacylation of a C-terminal cysteine
Helps proteins cycle between membrane and cytosol

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5
Q

What is phosphorylation?

A

Phosphorylation of hydroxyl group of Ser, Thr or Tyr residues
Can change enzymatic or interactive properties

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6
Q

What is ubiquitination?

A

Addition of ubiquitin to lysine residues in an aa sequence

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7
Q

What 3 enzymes are required for tagging?

A

Ubiquitination activating (E1)
Conjugating (E2)
Ligase (E3)

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8
Q

What does ubiquitin tagging a protein do?

A

Tags a protein for processing/degradation by the proteasome
Important for synaptogenesis and long term memory

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9
Q

What do nuclear proteins contain?

A

Nuclear localization signal (NLS)

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10
Q

What does the NLS do?

A

Target nuclear protein entry into the nucleus in an energy-dependent reaction

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11
Q

Which proteins need active import to pass through nuclear pores?

A

proteins < 10nm

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12
Q

When do mitochondrial proteins reach native conformation?

A

After import into target organelle

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13
Q

What is the mitochondrial signal sequence?

A

20-80 aa basic helix with hydrophilic (+) residues on one side and hydrophobic (-) residues on the other

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14
Q

What happens if the membrane protein doesn’t contain hydrophobic sequences?

A

Co-translational transfer continues until C terminus is transferred across membrane
Becomes free protein in lumen

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15
Q

What happens if the membrane protein does contain hydrophobic sequences?

A

Undergo co-translational transfer until ‘stop transfer’ sequence is reached
Forms integral membrane proteins

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16
Q

What are disulfide linkages?

A

(Cys-S-S-Cys)
Define teritary structure
Doesn’t occur in cytosol

17
Q

What is N-linked glycosylation?

A

Addition of a polysaccharide chain to amino groups of asparagine residues
Diversifies conformation and function of proteins

18
Q

How are proteins transported through the golgi apparatus?

A

Via transport vesicles

19
Q

What are the two protein coats?

A

COP1 and COP11

20
Q

how do ER vesicles enter the trans-golgi network (TGN)?

A

Arrive at cis side of the golgi
fuse with membranes of golgi cisternae
deliver contents into golgi complex
move to trans side

21
Q

What modifications do proteins undergo as they reach trans side?

A

N-linked and O-linked glycosylation
Phosphorylation
Sulfation

22
Q

What do these trans modifications cause?

A

Increase hydrophobicity of the protein - makes them more resistant to protein degradation

23
Q

How do plasma proteins leave TGN?

A

Constitutive secretion - vesicles continually secreted in a non-regulated manner

24
Q

How do neurohormones leave TGN?

A

Regulated secretion - concentrated into large dense-core vesicles and targeted to axons

25
How do synaptic proteins leave TGN?
unknown some - transported along neuronal cytoskeleton others - synthesized and assembled at synapse
26
What is required for chemotrophic response?
Local protein translation
27
What is localised mRNA actively trafficked by?
RNA binding proteins (RBPs)
28
What do RBPs form complexes with?
RNA granules
29
What do RBPs complexes allow for?
mRNA to be redistributed to the synapse along microtubule molecular motors