Unit 4: Endoplasmic Reticulum, Golgi Complex and Lysosomes - Practice Quiz

BTS118 — Cell Biology 60 Questions
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1 Which type of vesicle commonly carries proteins and lipids from the ER to the Golgi complex?

Export of proteins and lipids from the ER Easy
A. COPI-coated vesicle
B. Lysosomal vesicle
C. COPII-coated vesicle
D. Clathrin-coated vesicle

2 What is a major function of the endoplasmic reticulum in lipid transport?

Export of proteins and lipids from the ER Easy
A. Producing cellular ATP
B. Digesting membrane lipids
C. Storing genetic material
D. Synthesizing membrane lipids

3 Which feature distinguishes rough ER from smooth ER?

Structure and types of Endoplasmic reticulum Easy
A. A surrounding cell wall
B. DNA inside its lumen
C. A lack of membrane
D. Ribosomes on its surface

4 Which type of ER is especially involved in detoxification and lipid synthesis?

Structure and types of Endoplasmic reticulum Easy
A. Smooth ER
B. Nuclear ER
C. Rough ER
D. Golgi ER

5 The endoplasmic reticulum is best described as a:

Structure and types of Endoplasmic reticulum Easy
A. Membrane-bound network
B. Rigid cellular wall
C. Digestive enzyme crystal
D. Protein-free chromosome

6 What directs many newly synthesized proteins to the ER?

Targeting proteins to ER Easy
A. Signal sequence
B. Lipid droplet
C. Centromere
D. DNA promoter

7 Which particle recognizes an ER signal sequence on a newly forming protein?

Targeting proteins to ER Easy
A. Signal recognition particle
B. Ribosomal subunit
C. Lysosomal enzyme
D. Spliceosome

8 Proteins entering the ER are commonly synthesized by ribosomes attached to the:

Targeting proteins to ER Easy
A. Lysosome membrane
B. ER membrane
C. Golgi lumen
D. Mitochondrial matrix

9 What is one important function of molecular chaperones in the ER?

Protein folding and processing in ER Easy
A. Making ribosomal RNA
B. Helping proteins fold
C. Breaking down glucose
D. Copying DNA molecules

10 Which covalent bond can help stabilize the folded structure of a protein in the ER?

Protein folding and processing in ER Easy
A. Disulfide bond
B. Peptide bond
C. Glycosidic bond
D. Phosphodiester bond

11 What usually happens to a protein that fails to fold correctly in the ER?

Protein folding and processing in ER Easy
A. It is immediately secreted
B. It enters the nucleus freely
C. It becomes cellular DNA
D. It is retained or degraded

12 The Golgi complex is made up mainly of a stack of flattened membrane sacs called:

Organization of Golgi complex Easy
A. Cristae
B. Ribosomes
C. Cisternae
D. Peroxisomes

13 Which Golgi face receives transport vesicles from the ER?

Organization of Golgi complex Easy
A. Cis face
B. Basal face
C. Trans face
D. Lateral face

14 Which Golgi face is closest to the plasma membrane and sends materials toward their destinations?

Organization of Golgi complex Easy
A. Cis face
B. Trans face
C. Luminal face
D. Nuclear face

15 Glycosylation is the process of adding which type of molecule to a protein?

Protein glycosylation within Golgi Easy
A. DNA
B. Amino acid sequence
C. Sugar
D. Fatty acid only

16 What is one important result of protein glycosylation in the Golgi?

Protein glycosylation within Golgi Easy
A. Chromosome separation
B. ATP breakdown
C. Protein modification
D. DNA replication

17 The trans-Golgi network is mainly involved in:

Protein sorting and export from Golgi apparatus Easy
A. Producing ribosomes
B. Copying chromosomes
C. Digesting cytosol
D. Sorting cargo

18 Which destination can receive proteins packaged by the Golgi apparatus?

Protein sorting and export from Golgi apparatus Easy
A. Chromosome core
B. Nucleolus only
C. Cytosolic ribosome
D. Plasma membrane

19 Lysosomes contain enzymes that primarily function in:

Structure and function of lysosomes Easy
A. Intracellular digestion
B. Light absorption
C. DNA transcription
D. Protein synthesis

20 The interior of a lysosome is usually:

Structure and function of lysosomes Easy
A. Strongly alkaline
B. Neutral like cytosol
C. Filled with DNA
D. Acidic

21 A newly synthesized secretory protein leaves the rough ER in a transport vesicle. Which coat protein is most directly associated with vesicle formation for transport from the ER to the Golgi?

Export of proteins and lipids from the ER Medium
A. Clathrin
B. COPII
C. Caveolin
D. COPI

22 A pancreatic cell produces large amounts of digestive enzymes for secretion. Which ER specialization would be especially abundant in this cell?

Structure and types of Endoplasmic reticulum Medium
A. Peroxisomal membranes
B. Rough ER cisternae
C. Smooth ER tubules
D. Lysosomal vesicles

23 What would most likely happen if the signal recognition particle could not bind the signal sequence of a nascent secretory protein?

Targeting proteins to ER Medium
A. The protein would remain in the cytosol
B. The protein would enter the ER because all ribosomes are membrane-bound
C. The protein would be sent directly to lysosomes
D. The protein would enter the nucleus

24 A mutation prevents formation of disulfide bonds in a protein that normally functions in the extracellular environment. Which ER process is directly impaired?

Protein folding and processing in ER Medium
A. Lipid beta-oxidation
B. Disulfide bond formation
C. mRNA transcription
D. Peptide bond formation

25 A transport vesicle carrying a newly synthesized lysosomal enzyme arrives at the Golgi. Which Golgi region should it reach first?

Organization of Golgi complex Medium
A. Medial cisterna
B. Cis-Golgi network
C. Trans-Golgi network
D. Secretory granule

26 A glycoprotein receives carbohydrate modifications as it moves from the cis face toward the trans face of the Golgi. What does this illustrate?

Protein glycosylation within Golgi Medium
A. Compartment-specific processing within Golgi cisternae
B. DNA-directed assembly at the plasma membrane
C. Random modification throughout the cytosol
D. Complete carbohydrate removal in the ER

27 A lysosomal hydrolase lacks its normal mannose-6-phosphate tag. Which outcome is most likely?

Protein sorting and export from Golgi apparatus Medium
A. It will automatically return to the ER
B. It will be sorted efficiently into lysosomes
C. It will be inserted into mitochondrial DNA
D. It may be secreted outside the cell

28 Why can lysosomal enzymes digest cellular materials without normally digesting the cytosol?

Structure and function of lysosomes Medium
A. Lysosomal enzymes function only in the nucleus
B. Lysosomes maintain an acidic lumen
C. Lysosomes lack hydrolytic enzymes
D. The cytosol contains no proteins

29 During autophagy, a damaged mitochondrion is enclosed in a double-membrane autophagosome. What must happen next for its contents to be degraded?

Lysosomes role in autophagy and phagocytosis Medium
A. Attachment to a ribosome
B. Fusion with a lysosome
C. Export through a COPII vesicle
D. Fusion with the nucleus

30 A cell treated with a drug that blocks COPII function accumulates newly synthesized secretory proteins in the ER. Which process is directly blocked?

Export of proteins and lipids from the ER Medium
A. Plasma membrane endocytosis
B. Golgi-to-ER retrieval
C. ER-to-Golgi transport
D. Endosome-to-lysosome fusion

31 A liver cell increases its ability to detoxify lipid-soluble drugs. Which cellular change would most directly support this function?

Structure and types of Endoplasmic reticulum Medium
A. Expansion of smooth ER
B. Reduction of mitochondrial cristae
C. Loss of Golgi cisternae
D. Expansion of nucleoli

32 A membrane protein contains a hydrophobic stop-transfer sequence. What is the usual consequence during ER targeting?

Targeting proteins to ER Medium
A. The sequence halts translocation and anchors the protein
B. The sequence causes immediate secretion without Golgi transport
C. The sequence marks the protein for cytosolic degradation
D. The sequence directs the protein into the nucleus

33 A misfolded ER protein is repeatedly recognized by chaperones and eventually degraded in the cytosol. Which pathway is involved?

Protein folding and processing in ER Medium
A. ER-associated degradation
B. Glycolysis
C. Phagosome maturation
D. Ribosomal recycling

34 If vesicles moving from the trans-Golgi network were prevented from budding, which event would be most directly affected?

Organization of Golgi complex Medium
A. Replication of mitochondrial DNA
B. Initiation of protein translation
C. Formation of ER signal sequences
D. Sorting cargo to final destinations

35 A Golgi enzyme is experimentally relocated from the medial cisterna to the trans-Golgi network. What is the most likely effect?

Protein glycosylation within Golgi Medium
A. Its substrates will bypass all membrane compartments
B. Its substrates may receive modifications at an altered stage
C. Its protein sequence will be rewritten by ribosomes
D. Its catalytic activity must shift to the cytosol

36 A membrane protein destined for the plasma membrane is transported from the trans-Golgi network in a secretory vesicle. What is required for delivery to the cell surface?

Protein sorting and export from Golgi apparatus Medium
A. Re-entry into the mitochondrial matrix
B. Degradation by lysosomal hydrolases
C. Direct passage through the nuclear pore
D. Vesicle docking and membrane fusion

37 A mutation disrupts the lysosomal proton pump. Which result is most likely?

Structure and function of lysosomes Medium
A. Increased ER targeting of cytosolic proteins
B. Higher lysosomal pH and reduced hydrolase activity
C. Lower lysosomal pH and faster protein synthesis
D. Enhanced DNA replication inside lysosomes

38 A macrophage engulfs a bacterium into a phagosome. Which event enables enzymatic destruction of the bacterium?

Lysosomes role in autophagy and phagocytosis Medium
A. Fusion of the phagosome with ribosomes
B. Release of the bacterium into the cytosol
C. Fusion of the phagosome with lysosomes
D. Transport of the bacterium into the ER lumen

39 A lipid synthesized on the cytosolic leaflet of the ER membrane becomes distributed to both leaflets. Which process best explains this redistribution?

Export of proteins and lipids from the ER Medium
A. Translation by free ribosomes
B. Mannose phosphorylation
C. Proteasomal cleavage
D. Action of lipid translocators

40 A soluble ER resident protein is accidentally transported to the Golgi. Which feature can help retrieve it back to the ER?

Targeting proteins to ER Medium
A. A mannose-6-phosphate signal
B. A mitochondrial targeting peptide
C. A nuclear localization signal
D. A C-terminal retrieval signal

41 A secretory protein has an N-terminal signal peptide that is cleaved during translocation. A mutation prevents SRP from binding the signal peptide but does not alter the translocon. What is the most likely immediate consequence?

Targeting proteins to ER Hard
A. The protein enters the ER but cannot be glycosylated
B. The protein is inserted into the mitochondrial inner membrane
C. The protein enters the nucleus instead of the ER
D. The protein remains in the cytosol and is likely degraded

42 A membrane protein contains an internal hydrophobic signal-anchor sequence whose positively charged residues are more abundant on its N-terminal side. Which topology is most likely produced by the positive-inside rule?

Targeting proteins to ER Hard
A. N terminus in the cytosol and C terminus in the ER lumen
B. Both termini in the ER lumen with a cytosolic loop
C. N terminus in the ER lumen and C terminus in the cytosol
D. Both termini in the cytosol with a luminal loop

43 A cell expresses a mutant cargo receptor that binds soluble ER proteins but cannot interact with COPII coat components. Which defect is expected?

Export of proteins and lipids from the ER Hard
A. Premature cleavage of signal peptides in the ER lumen
B. Accumulation of COPI vesicles at the trans-Golgi network
C. Selective failure of cargo concentration into ER exit sites
D. Global loss of lysosomal acidification

44 Which alteration would most directly impair anterograde ER-to-Golgi transport while preserving the ability of COPI vesicles to retrieve escaped ER-resident proteins?

Export of proteins and lipids from the ER Hard
A. Inhibition of luminal protein disulfide isomerase
B. Mutation of a KDEL receptor
C. Inhibition of Sar1 GTP loading
D. Loss of a cytosolic KKXX retrieval motif

45 A steroid-producing cell is experimentally induced to increase synthesis of membrane phospholipids and detoxification enzymes but not secreted proteins. Which structural adaptation is most likely?

Structure and types of Endoplasmic reticulum Hard
A. Expansion of smooth ER tubules with increased membrane surface
B. Expansion of Golgi cisternae with reduced ER contact sites
C. Expansion of rough ER cisternae with more bound ribosomes
D. Expansion of lysosomal compartments with lower luminal pH

46 Why can rough ER and smooth ER be considered functionally continuous despite their different microscopic appearances?

Structure and types of Endoplasmic reticulum Hard
A. They are separate organelles joined only by COPII vesicles
B. They exchange proteins exclusively through lysosomal degradation
C. They contain identical enzymes but differ only in luminal pH
D. They share a continuous membrane and lumen but differ in ribosome association

47 A secretory protein repeatedly exposes hydrophobic regions and fails to achieve its native conformation. Which response most directly links this defect to ER quality control?

Protein folding and processing in ER Hard
A. Conversion of the protein into a cytosolic transcription factor
B. Direct transport to lysosomes through clathrin-coated vesicles
C. Immediate secretion through constitutive exocytosis
D. Increased binding by chaperones followed by possible ER-associated degradation

48 A mutation eliminates the ER retrieval sequence of a soluble chaperone but leaves its folding activity intact. What is the most likely cellular effect?

Protein folding and processing in ER Hard
A. The chaperone becomes a transmembrane receptor
B. The chaperone accumulates in the nucleus
C. The chaperone is targeted directly to the lysosome from the ER
D. The chaperone is secreted after escaping to the Golgi

49 A cell is treated with a drug that blocks formation of disulfide bonds in the ER but does not inhibit peptide-bond synthesis. Which class of protein is most selectively affected?

Protein folding and processing in ER Hard
A. Nuclear proteins imported after complete cytosolic synthesis
B. Mitochondrial matrix proteins synthesized on free ribosomes
C. Cytosolic enzymes lacking cysteine residues
D. Secretory proteins whose native structures require disulfide bonds

50 A Golgi-resident enzyme is found predominantly in the cis-Golgi, while another is found predominantly in the trans-Golgi. Which model best explains this distribution?

Organization of Golgi complex Hard
A. Random diffusion through a single continuous Golgi lumen
B. Permanent vesicular separation of all Golgi cisternae
C. Cisternal maturation combined with selective retrieval of resident enzymes
D. Synthesis of each enzyme by ribosomes attached to its cisterna

51 If COPI-dependent retrograde traffic between Golgi cisternae is strongly reduced, which outcome is most likely before widespread organelle disorganization?

Organization of Golgi complex Hard
A. Failure of ribosomes to bind the rough ER
B. Loss of all COPII vesicle budding from the ER
C. Mislocalization of resident Golgi enzymes toward later compartments
D. Immediate fusion of lysosomes with the plasma membrane

52 A glycoprotein reaches the Golgi with a high-mannose N-linked oligosaccharide. Which processing sequence is most plausible?

Protein glycosylation within Golgi Hard
A. Direct conversion of the oligosaccharide into a peptide bond
B. Mannose trimming followed by addition of sugars in ordered Golgi compartments
C. Addition of all terminal sugars before the protein enters the ER
D. Complete removal of the oligosaccharide followed by cytosolic resynthesis

53 A lysosomal hydrolase is synthesized normally but lacks mannose-6-phosphate on its N-linked oligosaccharides. Which defect is most likely?

Protein glycosylation within Golgi Hard
A. Insertion of the hydrolase into the mitochondrial membrane
B. Retention of the hydrolase in the cytosol by a ubiquitin ligase
C. Secretion of the hydrolase and reduced delivery to lysosomes
D. Failure of signal peptide removal in the ER

54 A mutation removes a luminal cysteine from a Golgi glycosyltransferase but leaves its catalytic residues intact. Why could glycosylation still be defective?

Protein glycosylation within Golgi Hard
A. The enzyme is redirected automatically to the nucleus
B. The mutation prevents all nucleotide-sugar synthesis in mitochondria
C. The enzyme may fail to fold or remain stable in the Golgi lumen
D. The enzyme can no longer bind cytosolic ribosomes

55 A soluble lysosomal enzyme binds its sorting receptor in the trans-Golgi network. What event normally promotes release of the enzyme from the receptor after delivery?

Protein sorting and export from Golgi apparatus Hard
A. Acidification of the endosomal lumen
B. Phosphorylation of the ribosome
C. Reduction of disulfide bonds by cytosolic thioredoxin
D. Alkalinization of the ER lumen

56 A membrane protein destined for the plasma membrane contains a cytosolic sorting motif that recruits clathrin adaptors at the trans-Golgi network. What is the most likely consequence of mutating this motif?

Protein sorting and export from Golgi apparatus Hard
A. The protein becomes soluble because its transmembrane domain is removed
B. The protein remains in the ER because translation stops
C. The protein may enter an incorrect post-Golgi pathway
D. The protein loses every luminal N-linked glycan in the ER

57 A lysosomal membrane protein is synthesized with a cytosolic tail that contains a tyrosine-based sorting signal. What is the primary significance of this signal?

Structure and function of lysosomes Hard
A. It targets the protein to clathrin-dependent transport from the trans-Golgi network
B. It causes the protein to be secreted through constitutive exocytosis
C. It prevents transmembrane insertion during ER translation
D. It directs the protein into the mitochondrial matrix

58 A mutation reduces activity of the lysosomal V-type proton ATPase but does not alter lysosomal membrane permeability. Which change is expected first?

Structure and function of lysosomes Hard
A. Higher lysosomal pH and reduced activity of acid hydrolases
B. Immediate loss of all lysosomal membrane proteins
C. Lower lysosomal pH and increased proteolysis
D. Increased cytosolic ribosome assembly

59 During macroautophagy, inhibition of lysosomal fusion with autophagosomes would most directly cause which phenotype?

Lysosomes role in autophagy and phagocytosis Hard
A. Accelerated breakdown of cytosolic proteins by proteasomes
B. Accumulation of autophagosomes containing undegraded material
C. Reduced formation of isolation membranes but normal degradation
D. Increased export of damaged mitochondria through COPII vesicles

60 A macrophage internalizes bacteria into phagosomes, but a defect prevents phagosome–lysosome fusion. Which result is most likely?

Lysosomes role in autophagy and phagocytosis Hard
A. Conversion of phagosomes into COPII-coated ER vesicles
B. Persistence of intact bacteria and impaired antigen processing
C. Failure of bacterial uptake at the plasma membrane
D. Enhanced bacterial degradation within isolated phagosomes