Protein Synthesis in Nervous System Flashcards

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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
Q

How do synaptic proteins leave TGN?

A

unknown
some - transported along neuronal cytoskeleton
others - synthesized and assembled at synapse

26
Q

What is required for chemotrophic response?

A

Local protein translation

27
Q

What is localised mRNA actively trafficked by?

A

RNA binding proteins (RBPs)

28
Q

What do RBPs form complexes with?

A

RNA granules

29
Q

What do RBPs complexes allow for?

A

mRNA to be redistributed to the synapse along microtubule molecular motors