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lecture 4

Total questions: 40

Worksheet time: 20mins

Name
Class
Date
1.

Protein sorting refers to:

a)

Protein degradation in lysosomes

b)

Directing proteins to their correct cellular locations

c)

Synthesis of proteins on ribosomes

d)

Modification of proteins by glycosylation

2.

Signal sequences are usually located:

a)

At the N-terminus

b)

At the C-terminus

c)

Always in the middle of the protein

d)

Only on enzymes

3.

Which organelle is the major site for initial protein glycosylation?

a)

Nucleus

b)

Endoplasmic reticulum (ER)

c)

Golgi apparatus

d)

Lysosome

4.

Which proteins typically remain in the cytoplasm?

a)

Hormones

b)

Structural proteins (e.g., cytoskeletal)

c)

Secretory proteins

d)

Receptor proteins

5.

Proteins destined for secretion are synthesized on:

a)

Free ribosomes

b)

ER-bound ribosomes

c)

Mitochondrial ribosomes

d)

Nuclear ribosomes

6.

Proteins enter the nucleus via:

a)

Vesicular transport

b)

Nuclear pores

c)

Protein translocators

d)

Endocytosis

7.

Energy for nuclear import is provided by:

a)

ATP hydrolysis

b)

GTP hydrolysis

c)

NADH oxidation

d)

Proton gradient

8.

Proteins entering mitochondria must:

a)

Be fully folded

b)

Remain unfolded during translocation

c)

Be glycosylated

d)

Be degraded and resynthesized

9.

Chaperone proteins inside mitochondria and chloroplasts:

a)

Degrade proteins

b)

Help pull proteins across membranes and refold them

c)

Remove signal sequences

d)

Block protein import

10.

Proteins entering peroxisomes:

a)

Must be unfolded

b)

Can enter folded from cytosol

c)

Require vesicles only

d)

Are degraded on entry

11.

Proteins enter the ER:

a)

After being fully synthesized in cytosol

b)

While being synthesized (co-translational import)

c)

Only when folded

d)

Only via vesicles

12.

Soluble ER proteins end up in the:

a)

ER lumen

b)

ER membrane

c)

Cytosol

d)

Lysosome

13.

Transmembrane proteins are inserted into the ER membrane by:

a)

Hydrophobic signal sequences

b)

Glycosylation

c)

Chaperone proteins

d)

SNAREs

14.

Which organelle modifies oligosaccharides and sorts proteins for secretion or lysosomes?

a)

Nucleus

b)

ER

c)

Golgi apparatus

d)

Peroxisome

15.

Exit from the ER is controlled by:

a)

pH gradient

b)

Protein quality control (chaperones, unfolded protein response)

c)

ATP synthase

d)

Random diffusion

16.

Vesicle budding is driven by:

a)

SNARE proteins

b)

Protein coats (e.g., clathrin)

c)

Proton pumps

d)

Ion channels

17.

The role of clathrin is to:

a)

Hydrolyze ATP

b)

Shape the membrane into a vesicle bud

c)

Glycosylate proteins

d)

Degrade proteins

18.

Vesicle docking specificity is determined by:

a)

Chaperones

b)

SNARE and tethering proteins

c)

Porins

d)

Glycolipids

19.

SNARE proteins catalyze:

a)

Protein folding

b)

Membrane fusion

c)

ATP hydrolysis

d)

Glycosylation

20.

Vesicular transport ensures:

a)

Random movement of proteins

b)

Constant, specific protein flow between organelles

c)

Protein degradation

d)

Nuclear import

21.

Proteins secreted outside the cell follow which pathway?

a)

ER → Golgi → vesicle → plasma membrane

b)

Cytosol → nucleus → plasma membrane

c)

Lysosome → vesicle → plasma membrane

d)

Peroxisome → Golgi → membrane

22.

Which covalent modification occurs in the ER but not in the cytosol?

a)

Disulfide bond formation

b)

Phosphorylation

c)

Acetylation

d)

Methylation

23.

The unfolded protein response is triggered by:

a)

Overexpression of receptors

b)

Accumulation of misfolded proteins in ER

c)

Loss of SNAREs

d)

Lysosome rupture

24.

Proteins destined for lysosomes are tagged with:

a)

O-linked glycosylation

b)

Mannose-6-phosphate

c)

Phosphate group on serine

d)

Disulfide bonds

25.

Endocytosed macromolecules are first delivered to:

a)

Nucleus

b)

Lysosome

c)

Endosome

d)

ER

26.

Phagocytosis involves vesicles of size:

a)

>250 nm

b)

20 nm

c)

500 µm

d)

<150

27.

Which cells specialize in phagocytosis?

a)

Epithelial cells

b)

Macrophages

c)

Muscle cells

d)

Fibroblasts

28.

Pinocytosis is often carried out by:

a)

Clathrin-coated vesicles

b)

Lysosomes

c)

Nuclear pores

d)

Mitochondria

29.

Receptor-mediated endocytosis ensures:

a)

Random uptake

b)

Selective uptake of molecules

c)

Protein degradation

d)

Vesicle fusion with ER

30.

Low pH in endosomes facilitates:

a)

ATP production

b)

Dissociation of receptor–ligand complexes

c)

Vesicle budding

d)

Protein synthesis

31.

Lysosomes maintain acidity using:

a)

Proton pumps (V-type ATPases)

b)

Na⁺/K⁺ pump

c)

Ca²⁺ channels

d)

SNARE proteins

32.

Lysosomes degrade:

a)

Proteins

b)

Nucleic acids

c)

Lipids

d)

All of the above

33.

Macrophages ingest old RBCs using:

a)

Autophagy

b)

Phagocytosis

c)

Pinocytosis

d)

Exocytosis

34.

The main sorting station for endocytosed material is the:

a)

ER

b)

Early endosome

c)

Golgi

d)

Lysosome

35.

Defects in lysosomal enzymes often lead to:

a)

Cancer

b)

Storage diseases (e.g., Tay-Sachs)

c)

Protein overexpression

d)

Golgi expansion

36.

Proteins entering the nucleus require:

a)

Nuclear localization signal (NLS)

b)

ER signal sequence

c)

Mannose-6-phosphate

d)

Clathrin coat

37.

Proteins that misfold and fail ER quality control are degraded by:

a)

Lysosomes

b)

Proteasomes after retro-translocation

c)

Peroxisomes

d)

Endosomes

38.

A defect in SNARE proteins would primarily impair:

a)

Protein folding

b)

Vesicle docking and fusion

c)

ATP synthesis

d)

Protein glycosylation

39.

Which pathway delivers extracellular proteins to lysosomes?

a)

Autophagy

b)

Endocytosis

c)

Proteasome pathway

d)

ER quality control

40.

The major function of vesicular transport is to:

a)

Randomize protein distribution

b)

Maintain organelle identity and protein flow

c)

Provide ATP

d)

Synthesize signal sequences

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