MCBG 11 Flashcards

1
Q

Protein sorting. Which organelles use the ER to get their proteins?

A

Lysosomes

ER

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2
Q

Which organelles get their proteins from free cytosolic ribosomes?

A

Nucleus
Mitochondria
Peroxisomes

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3
Q

What is required for protein sorting?

A

Signal
Receptor
Translocational machinery
Energy

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4
Q

How do protein get to the ER?

A

mRNA (specific translocational sequence) and a ribosome in the cytoplasm get bound by a SRP (signal recognition particle) where it is transported to the ER

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5
Q

How is PDI (an ER resident protein) retained

in the ER and not secreted?

A

The golgi body has retrograde secretions back to the ER

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6
Q

What is the signal used to get golgi vesicles back to the ER (WHERE IS IS FOUND SPECIFICALLY)

A

KDEL on the C-terminus

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7
Q

What does the signal for retrograde transportation back to the ER bind to?

A

KDEL receptor which forms a vesicle with a COPI coat

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8
Q

Whats the signal in lysosome import?

A

Mannose-6-phosphate

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9
Q

Lysosome import. What happens for to the signal so it know where its going?

A

In Golgi M6P binds to

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10
Q

Whats the mitochondrial signal called? WHERE IS IS FOUND SPECIFICALLY

A

MTS Mitochondrial targeting signal

N-terminus

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11
Q

Whats MTS?

A

Mitochondrial targeting signal

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12
Q

What are the additional proteins needed in MITO import?

A

Chaperone proteins

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13
Q

MITO. Energy?

A

Yes. Transporters

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14
Q

Nuclear transport. What is the signal?

A

NLS. Nuclear localising signal

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15
Q

What are the additional proteins needed in Nuclear import?

A

Importin

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16
Q

Describe how the nuclear protein in imported?

A

PP chain binds to importin (alpha and beta) this transports it into the cell via a nuclear pore. RanGTP binds to Importin, displaces the protein and is transported out of the cell. GTP->GDP causes ran to be recycled back to the nucleas

17
Q

What are the two ways of Short term regulation of enzyme activity

A
  1. Substrate and product concentration
  2. Change in enzyme conformation
    (A)llosteric. Allosteric regulation
    (B)onds. Covalent modification
    (C)leavage. Proteolytic cleavage
18
Q

What are the two ways of LONG TERM REGULATION of enzyme activity

A
  1. Change in rate of protein synthesis

2. Change in rate of protein degradation

19
Q

What is Phosphofructokinase?

A

allosterically regulated and sets the pace of glycolysis.

20
Q

What activates Phosphofructokinase? What regulation is this?

A

AMP, fructose-2,6-
bisphosphate
Allosteric

21
Q

What deactivates Phosphofructokinase?

What regulation is this?

A

ATP, citrate, H+

Allosteric

22
Q

What is haemophilia?

A

mostly inherited genetic disorder that impairs the body’s ability to make blood clots. X-linked recessive disorders

23
Q

What are the two types of haemophilia?

A

There are two main types of haemophilia: haemophilia A, which occurs due to not enough clotting factor VIII, and haemophilia B, which occurs due to not enough clotting factor IX.

24
Q

Why is protein phosphorylation so effective? 3/5

A
  • Adds 2 negative charges
  • A phosphoryl group can make H-bonds
  • Allow for amplification effects
  • Rate of phosphorylation/dephosphorylation can be adjusted
  • Links energy status of the cell to metabolism through ATP
25
Q

define the term zymogen

A

inactive substance which is converted into an enzyme when activated by another enzyme

26
Q

Coagulation cascade. Whats the intrinsic pathway?

A
XII
XI
IX +VIII
X + V
II THROMBIN
I FIBRIN
27
Q

Coagulation cascade. Whats the extrinsic pathway?

A
III (Tissue factor)
VII
X
II
I
28
Q

How does the Coagulation cascade get activated?

A

By the extrinsic pathway (SPARK)
At a epithelial break, platelets and Tissue factors form at the blood clot. This activates the extrinisic cascade forming thrombin which activates the intrinsic pathway (WORK HORSE)

29
Q

Whats a thrombosis

A

The formation of a solid mass of blood within the circulatory system of a living body

30
Q

What factors get activated by thrombin?

A

All odd numbers (kinda)

(2) 5 7 (X9X)8 11 13

31
Q

What does XIII do?

A

Connects the fibrin strands with cross strands

32
Q

What inactivates the coagulation cascade? 2

A
Thrombin forms 
plasmin (breaks down crosslinks)
Stimulates antithrombrin ( inhibits thrombin and Factor X