9/2/14 - Intracellular Compartments Flashcards

1
Q

What is the function of the endosome?

A

Acts as a sorting center or “checkpoint” between the cell membrane and the lysosome. Some molecules are processed and sent to the lysosome for destruction, and others are recycled.

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2
Q

Which organelle functions in the oxidation of fatty acids and some metabolic intermediates?

A

Peroxisome

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3
Q

Which organelle is responsible for the breakdown of most biomolecules?

A

Lysosome

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4
Q

What is the purpose of the Golgi apparatus?

A

To process and sort various molecules, especially those destined to be secreted by the cell.

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5
Q

What are some functions of the endoplasmic reticulum?

A

It has several functions, including protein synthesis and protein transport. It is also the site of lipid biogenesis and calcium storage.

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6
Q

What is the difference between a signal peptide and a signal patch?

A

A signal peptide is normally a sequence at the N-terminal, a signal patch is usually a combination of internal amino acid sequences that contribute to the folding of a protein.

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7
Q

What is the purpose of signal peptides and signal patches?

A

These “tag” proteins and allow cellular machinery to direct them to the appropriate compartment.

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8
Q

What features of signal peptides and signal patches direct proteins to specific compartments?

A

Amino acid sequence and folded structure.

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9
Q

Signal peptides with a hydrophobic center are typically directed to which organelle?

A

Endoplasmic reticulum

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10
Q

Signal peptides that are amphipathic alpha helices are typically directed to which organelle?

A

Mitochondria

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11
Q

What protein helps regulate transport of macromolecules through the nuclear pore?

A

Ran

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12
Q

What effect does protein size have on nuclear uptake?

A

Larger proteins require nuclear import signals or they will not pass through the pore.

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13
Q

Describe how Ran facilitates the transport of proteins across nuclear pores.

A

RanGEF (guanine nucleotide exchange factor) phosphorylates Ran-GDP to form Ran-GTP inside the nucleus. The Ran-GTP gradient across the nuclear membrane powers transport of proteins across the nuclear pore. In the cytosol, RanGAP converts Ran-GTP to Ran-GDP before being transported back into the nucleus in GDP form.

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14
Q

How does the function of Ran-GTP differ between nuclear export and nuclear import?

A
  1. Nuclear import: Ran-GTP stimulates dissociation of cargo from the import receptor.
  2. Nuclear export: Ran-GTP stimulates the association of cargo with the export receptor.
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15
Q

How can the regulation of nuclear import lead to changes in gene expression?

A

Transcription factors have to enter the nucleus before they can activate gene expression. A disruption in nuclear import could alter gene expression depending on which TFs were affected.

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16
Q

What are the four main structural elements of the mitochondrion?

A
  1. Outer membrane
  2. Intermembrane space
  3. Inner membrane
  4. Matrix space
17
Q

Which membrane complex facilitates transport of proteins through the outer mitochondrial membrane?

A

TOM (translocase of outer membrane)

18
Q

Which membrane complex facilitates transport of proteins into the mitochondrial matrix?

A

TIM23 (translocase of inner membrane)

19
Q

What role do cytosolic chaperone proteins play in mitochondrial protein import?

A

Cytosolic Hsp70 bind to unfolded cargo proteins and “push” them through the mitochondrial membranes when powered by ATP hydrolysis.

20
Q

How are transported proteins re-folded once inside the mitochondria? (2 related proteins)

A
  1. Chaperone Hsp70 stabilizes unfolded regions of a protein while the rest of the protein folds up.
  2. Chaperone Hsp60 forms a cage around the unfolded protein which protects it while it re-folds.
21
Q

True/False: Peroxisomes perform most oxidation reactions within the cell.

A

False. Mitochondia perform the most oxidation reactions.

22
Q

How are peroxisomes differentiated from mitochondria in EM imaging?

A

Peroxisomes lack inner cristae (inner folds of the mitochondrion) and have a dense core.

23
Q

What is the main function of the rough ER?

A

Contains many ribosomes, therefore involved in protein synthesis.

24
Q

Proteins translated on the ER typically end up in which two locations?

A

Membrane or secreted from the cell.

25
Q

What feature of proteins directs them through the ER?

A

Signal peptides.

26
Q

What are the main steps in co-translational transport?

A
  1. SRP identifies a signal peptide and transports transcript to an ER membrane-bound ribosome.
  2. ER ribosome continues translation, and now the protein product is transported into the ER lumen instead of the cytosol.
27
Q

How are multipass membrane proteins able to be inserted into the ER membrane?

A

They contain multiple stop/start transfer sequences.

28
Q

What is an important 7-transmembrane protein in cell signalling?

A

G-protein coupled receptor

29
Q

Describe, in general terms, how proteins are glycosylated in the lumen of the ER.

A

Sugars are added to asparagine residues (mostly) of ER proteins by enzymes.

30
Q

What are some functions of protein glycosylation?

A
  1. To control ER protein folding
  2. To protect ER proteins from degradation
  3. To operate as a part of a sorting signal
31
Q

How does a cell respond to overwhelming protein levels within the ER?

A

Sensor molecules recognize over-abundance of proteins and activate to form a ribonuclease. Ribonuclease splices some mRNA to create a TF which promotes more chaperone expression. Higher chaperone levels allow ER to keep up with high levels of protein folding.