chapter 12 Flashcards

(37 cards)

1
Q

The endomembrane system

A

movement of lipids and proteins between organelles (called trafficking) must be tightly regulated

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2
Q

Components of the endomembrane system

A

Golgi, ER (rough and smooth), lysosomes, endosomes, peroxisomes

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3
Q

Rough endoplasmic reticulum

A

is characterized by ribosomes on the cytsolic side of the membrane

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4
Q

A subdomain of rough ER, the ___ ___ (TEs), play a role in the formation of transition vesicles that shuttle lipids and proteins from the ER to the Golgi complex

A

transitional elements

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5
Q

Smooth ER

A

lacks ribosomes and has other roles in the cell involving the processing and storage of nonproteins

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6
Q

Rough ER membranes form (structure)

A

large flattened sheets

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7
Q

Smooth ER membranes form (structure)

A

tubular

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8
Q

Rough Er is the site for…(4 things)

A
  • The initial steps of additoon of carbohydrates of glycoproteins
  • The folding of polypeptides
  • assembly of multimeric proteins
  • proteins that are incorrectly folded, modified, or assembled are recognized and exported for degration
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9
Q

Smooth ER is involved in (4 things)

A

drug detoxification, carbohydrate metabolism, calcium storage, and steroid biosynthesis

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10
Q

Transition elements of rough Er and smooth ER…

A

resemble one another

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11
Q

Are the rough ER and smooth ER separate organelles?

A

NO, material can travel between the rough and smooth ER without the aid of vesicles

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12
Q

Cells involved in the biosynthesis of secretory proteins, such as liver cells and cells producing digestive enzymes, tend to have very prominent ____networks. On the other hand, cells producing steroid hormones, such as in the testis or ovary, contain extensive networks of ___.

A

rough ER ; smooth ER

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13
Q

What does it mean by “Newly synthesized proteins enter the endomembrane system cotranslationally”?

A

They are inserted through a pore complex in the ER membrane into the rough ER lumen as the polypeptide is synthesized by the ER-bound ribosome.

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14
Q

The ER is also a site for quality control, where proteins improperly modified, folded, or assembled are exported from the ER for degradation by cytosolic ____ instead of moving on to the Golgi apparatus.

A

proteasomes

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15
Q

Drug detoxification often involves enzyme-catalyzed _____ because the addition of hydroxyl groups to hydrophobic drugs makes them more soluble and easier to excrete from the body.

A

hydroxylation

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16
Q

Hydroxylation of organic acceptor molecules is typically catalyzed by a member of the _____ family of proteins.

A

cytochrome P-450

17
Q

hepatocytes

18
Q

The Smooth ER plays a central role in the biosynthesis of

19
Q

What are the few exceptions to smooth er making membranes?

A

mitochondria synthesize phosphatidylethanolamine, peroxisomes synthesize cholesterol, chloroplasts contain enzymes for chloroplast specific lipids

20
Q

The golgi apparatus is a series of flattened membrane bounded ___

21
Q

a series of cisternae (3-8) is called

22
Q

Anterograde

A

movement of material from the ER through the Golgi apparatus toward the plasma membrane

23
Q

Retrograde

A

flow of vesicles from Golgi cisternae back toward the ER

24
Q

CGN (cis)

A

compartment closest to the ER, a network of flattened, membrane bounded tubules
Vesicles containing newly synthesized lipids and proteins from the ER continuously arrive at the CGN, where they fuse with CGN membranes

25
TGN (trans)
Proteins and lipids leave the golgi in transport vesicles that continuously bud from the tips of TGN cisternae
26
Glycosylation
the addition of carbohydrate side chains to specific amino acid residues of proteins, forming glycoproteins
27
N-linked glycosylation
involved the addition of a specific oligosaccharide unit to the nitrogen atom on the terminal amino group of certain asparagine residues
28
O linked glycosylation
involves addition of an oligosaccharide to the oxygen atom on the hydroxyl group on serine
29
The most abundant chaperone in the ER lumen is
BiP
30
How does BiP work?
BiP is a helper protein in the ER that keeps new proteins from sticking together the wrong way. When a new protein starts to form, BiP grabs onto the sticky (hydrophobic) parts so they don’t clump up with other proteins. BiP then lets go for a moment, using energy from ATP, to give the protein a chance to fold properly. If the protein folds the right way, those sticky parts get tucked inside and BiP doesn't need to grab on again. But if the protein still isn’t folded right, BiP grabs it again and tries the process over. This cycle helps proteins fold correctly so they can work properly in the cell.
31
protein disulfide isomerase
an enzyme present in the ER lumen that catalyzes the formation and breakage of disulfide bonds between cysteine residues
32
Unfolded protein response (UPR)
uses sensor molecules in the ER membrane to detect misfolded proteins. These sensors activate signaling pathways that shut down the synthesis of most proteins while enhancinh the production of those required for protein folding and degradation
33
ER associated degradation (ERAD)
recognizes misfolded or unassembled proteins and exports, or "retrotranslocates" tjem back acorss the ER membrane to the cytosol where they are degraded by proteasomes
34
The initial steps of N-glycosylation take place on the
cytosolic surface of the ER membrane
35
Later steps of glycosylation take place in the
ER lumen
36
All carbohydrate side chains initially have a common ___ ___ consisting of two unites of N-acetylglucosamine, nine mannose units and three glucose units
core oligosaccharide
37