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38 notecards = 10 pages (4 cards per page)

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Protein Degradation iRAT

front 1

Why is protein degradation important?

back 1

It allows the cell to have a constant supply of amino acids and prevents the accumulation of abnormal proteins.

front 2

Short-lived proteins with a half-life with seconds and minutes are degraded by what pathway?

back 2

Cytosolic ATP dependent pathway

front 3

Cytosolic ATP dependent pathway is mediated by-

back 3

the proteosome

front 4

What is the function of the proteosome?

back 4

carries out hydrolytic cleavage

front 5

What degrades proteins with long half lives?

back 5

Lysosomes

front 6

What pathways can degrade proteins?

back 6

Cytosolic ATP dependent and Lysosomal

front 7

What is a lysosome?

back 7

membrane-enclosed organelle that contain the digestive enzymes: lipases, nucleases and proteases.

front 8

What is the function of a lysosome?

back 8

the digestive system of the cell, breaks down waste materials, cellular debris, and foreign particles in the cell using digestive enzymes

front 9

What is the term for the cellular process that breaks down and recycles olf, damaged, or abnormal cell parts?

back 9

Autophagy

front 10

What is the process of autophagy?

back 10

a process where vesicles called autophagosomes engulf small amounts of cytoplasm or specific organelles using the endoplasmic reticulum

front 11

what occurs when vesicles fuse with lysosomes?

back 11

the release of the lysosomal hydrolytic enzymes causing degradation of macromolecules

front 12

LC3-I and LC3-II does what for autophagosomes

back 12

decides and regulates

front 13

When you have more LC3-II you will have more

back 13

autophagosomes

front 14

What is a autolysosome?

back 14

a compartment that is created when an autophagosome fuses with a lysosome

front 15

Lysosomes can selectivley degrade-

back 15

cytosolic proteins

front 16

The target proteins of lysosomes are usallly proteins with

back 16

long half lives

front 17

The function of dispensible proteins is -

back 17

to be sacrifies to make amino acids and energy to support basic metabolic reactions

front 18

The ATP dependent pathway involves the protein ______________

back 18

ubiquitin (highly conserved protein containing 76 amino acids)

front 19

What is the function of ubiquitin in the ATP dependent pathway?

back 19

it tags proteins that are destined for destruction via. a covalent attatchment

front 20

What are the mechanisms for recognition?

back 20

Half-life of proteins, recogition of phsophorylated substrates, recogition of ancillary porteins bound to the substrate, recogition of mutated abnormal protein.

front 21

The half-life of proteins correlates with what?

back 21

amino-terminal residue

front 22

Proteins with N-terminal Met, Ser, Ala, Thr, Val, or Gly have half lives greater than?

back 22

20 hours

front 23

Proteins with the N-terminal Phe, Leu, Asp, Lys, or Arg have half-lives of ?

back 23

3 mins or less.

front 24

Proteins rich in Pro (P), Glu (E), Ser (S), and Thr (T) are more ____________ degraded than other proteins

back 24

rapidly

front 25

Ubiquitin is ____________ linked to proteins through the ATP dependent pathway involving enzymes ___ , ____ , ____.

back 25

covalently, E1, E2, E3

front 26

Ubiquitination of proteins results in what?

back 26

the linking the carboxy-terminal glycine residue in ubiquitin to a lysine residue in the protein to be degraded

front 27

What is the function of the E1 enzyme?

back 27

acitivates ubiquitin, to bind to it

front 28

What is the function of the E2 enzyme?

back 28

conjugates ubiquitin

front 29

The function of E3 enzyme?

back 29

ubitquitin ligase, promotes the transfer of ubiquitin from E2 to the lysine residue of the protein recognized by the E3 as being slated for degradation.

front 30

What is the 26S proteosome?

back 30

a large complex of proteins that structurally resembles a large cylinder that is covered on both ends.

front 31

What is the central 20S core particle?

back 31

is a barrel shaped formed of 4 rings, outer rings formed of 7 alpha rings and inner rings formed of 7 beta rings

front 32

What part of the proteosome is this?

back 32

The central 20S core particle

front 33

What part(s) of the proteosome is this?

back 33

The 19S regulatory particle caps

front 34

Why are the 19S regulatory caps important?

back 34

they are important for recogition and binding of polyubiquinated proteins, removal of ubiquitin, unfolding of protein substrate, and translocation into the central core

front 35

How many ubiquitin are needed to be recoginzed by proteosome?

back 35

a minimum of 4

front 36

Degradation of proteins in the proteosomes are faciliated by ________ and hydrolyzed by ________

back 36

19S particles, central 20S core

front 37

What is bortezomib?

back 37

the 1st therapeutic proteosome inhibitor to be tested in humans.

front 38

What is the function of bortezomib?

back 38

a peptide that binds in the catalytic site of the 26S proteosome and inhibits the degradtionof proteins