W4 d1 and w3 day 2Bio421_5_ER protein trafficking

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47 Terms

1
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What are the two types of protein transport regarding the timing of protein transport to the endoplasmic reticulum (ER)?

Co-translational and post-translational protein transport.

2
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What is the role of the signal sequence in protein transport to the ER?

It directs the ribosome-RNA complex to the protein translocator during protein synthesis.

3
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Name one characteristic of the ER signal sequence.

It has a hydrophobic core region.

4
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What is the ultimate fate of water soluble proteins after translocating across the ER?

They may be secreted from the cell or stay in the ER or Golgi.

5
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What is the function of the Sec61 complex?

It serves as the ER translocator that forms a water-filled pore through the ER membrane.

6
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What happens to the signal peptide after protein synthesis is complete in the ER?

Signal peptidase cleaves the signal peptide, releasing the protein into the ER lumen.

7
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What defines single-pass transmembrane proteins during their translocation process?

They begin similarly to soluble ER proteins, but translation pauses until the ribosome is brought to the ER membrane.

8
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What defines multi-pass transmembrane proteins?

They have multiple transmembrane domains and contain multiple start and stop transfer signals.

9
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How can we predict the number of transmembrane domains in a protein?

By looking at the hydrophobic regions within the protein structure.

10
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What distinguishes N-terminal signal sequences from internal signal sequences in transmembrane protein targeting?

N-terminal signal sequences get cleaved by signal peptidase, but internal signal sequences do not.

11
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What are the two types of protein transport regarding the timing of protein transport to the endoplasmic reticulum (ER)?

Co-translational and post-translational protein transport.

12
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What is the role of the signal sequence in protein transport to the ER?

It directs the ribosome-RNA complex to the protein translocator during protein synthesis.

13
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Name one characteristic of the ER signal sequence.

It has a hydrophobic core region.

14
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What is the ultimate fate of water soluble proteins after translocating across the ER?

They may be secreted from the cell or stay in the ER or Golgi.

15
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What is the function of the Sec61 complex?

It serves as the ER translocator that forms a water-filled pore through the ER membrane.

16
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What happens to the signal peptide after protein synthesis is complete in the ER?

Signal peptidase cleaves the signal peptide, releasing the protein into the ER lumen.

17
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What defines single-pass transmembrane proteins during their translocation process?

They begin similarly to soluble ER proteins, but translation pauses until the ribosome is brought to the ER membrane.

18
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What defines multi-pass transmembrane proteins?

They have multiple transmembrane domains and contain multiple start and stop transfer signals.

19
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How can we predict the number of transmembrane domains in a protein?

By looking at the hydrophobic regions within the protein structure.

20
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What distinguishes N-terminal signal sequences from internal signal sequences in transmembrane protein targeting?

N-terminal signal sequences get cleaved by signal peptidase, but internal signal sequences do not.

21
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What is a signal peptide in protein transport?

A short peptide that tells the cell to direct the protein to the ER.

22
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What happens during co-translational translocation?

Proteins are translocated into the ER while they are still being synthesized by ribosomes.

23
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What dietary component can affect the composition of the signal sequence?

The amino acid composition can vary based on dietary intake.

24
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How do ribosomes know where to begin protein synthesis?

The ribosome recognizes the start codon of the mRNA.

25
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What is the significance of hydrophobic amino acids in signal sequences?

They help anchor the protein in the lipid bilayer of membranes.

26
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What is required to initiate the translocation of proteins across the ER membrane?

The ribosome must be recruited to the protein translocator.

27
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What role does the Golgi apparatus play after protein translocation?

It modifies, sorts, and packages proteins for secretion or delivery to other organelles.

28
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What defines the ER lumen?

The interior space of the endoplasmic reticulum where proteins are folded and modified.

29
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Why are signal sequences important for protein targeting?

They ensure proteins reach their correct destinations within the cell.

30
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What are ER-resident proteins?

Proteins that function within the endoplasmic reticulum and are retained there.

31
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How is protein maturation achieved in the ER?

Through proper folding and post-translational modifications such as glycosylation.

32
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What is the relationship between the signal sequence and the ribosome?

The signal sequence is recognized by the ribosome during the synthesis of proteins destined for the ER.

33
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What does post-translational modification include?

Chemical modifications made to proteins after they have been synthesized.

34
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What are the consequences of improper signal sequence recognition?

Proteins may be misdirected and fail to reach their intended compartments.

35
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What factor contributes to the stability of transmembrane proteins?

The presence of hydrophobic and charged residues in specific regions of the protein.

36
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Why are start and stop transfer signals important?

They control the orientation and number of times a protein crosses the membrane.

37
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What is the role of chaperone proteins in the ER?

They assist in the proper folding of newly synthesized proteins.

38
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What occurs during glycosylation in the ER?

Sugar molecules are added to proteins, which is crucial for protein stability and function.

39
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What triggers the export of proteins from the ER to the Golgi apparatus?

The presence of signals that mark proteins for transport.

40
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How does the hydrophobicity of a signal sequence influence its function?

More hydrophobic sequences tend to integrate better into the membrane.

41
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How do cells ensure that only properly folded proteins leave the ER?

By utilizing quality control mechanisms that eliminate misfolded proteins.

42
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What is a potential outcome of mutations in signal sequences?

They can lead to diseases due to improper protein localization.

43
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How does the endoplasmic reticulum contribute to cellular communication?

By assisting in the production of signaling proteins that can be secreted.

44
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What is the main difference between the rough and smooth ER?

Rough ER is studded with ribosomes, while smooth ER is involved in lipid synthesis and detoxification.

45
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What process allows proteins to pass through the ER membrane?

Translocation during protein synthesis and subsequent folding.

46
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What is the role of the nuclear signal sequence?

It directs proteins into the nucleus through nuclear pores.

47
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What happens to proteins that are misfolded in the ER?

They are typically targeted for degradation through the ER-associated degradation pathway.