Multiple-Choice Questions PDF

Multiple-Choice Questions 1. What is the first step in the coat assembly process? A) Scission B) Uncoating C) Initiation of coat assembly D) Tethering 2. Which component is responsible for recruiting coat components to the donor compartment? A) SNAREs B) Phosphoinositides...

Multiple-Choice Questions 1. What is the first step in the coat assembly process? A) Scission B) Uncoating C) Initiation of coat assembly D) Tethering 2. Which component is responsible for recruiting coat components to the donor compartment? A) SNAREs B) Phosphoinositides C) GTPase D) Rab proteins 3. During which step does the membrane curvature increase? A) Tethering B) Budding C) Uncoating D) Docking 4. What occurs during the scission step? A) The coat proteins are recycled B) The vesicle loses its coat C) The neck between the vesicle and donor compartment is severed D) The cargo is concentrated 5. What leads to the uncoating of the vesicle? A) Addition of new coat components B) Inactivation of the small GTPase C) Polymerization of SNAREs D) Binding of Rab proteins 6. What guides the naked vesicle to the acceptor compartment? A) SNARE proteins B) Cytoskeleton C) GTPase D) Phosphoinositides 7. What is the role of Rab proteins in vesicle transport? A) They sever the neck of the vesicle B) They assist in docking vesicles to target membranes C) They polymerize into a mesh-like structure D) They degrade misfolded proteins 8. What happens to SNAREs after the cargo is transferred to the acceptor compartment? A) They are degraded B) They are recycled C) They are phosphorylated D) They are transported back to the donor compartment 9. What can cause a single amino acid substitution in a protein? A) Phosphoinositide hydrolysis B) Point mutation C) GTPase activation D) SNARE complex formation 10. What is a potential consequence of protein misfolding in the ER? A) Increased protein synthesis B) Accumulation of misfolded proteins C) Enhanced vesicle budding D) Improved receptor binding 11. How can immunofluorescence techniques be used in studying mutant proteins? A) To enhance protein synthesis B) To detect mutant proteins using antibodies C) To increase vesicle docking D) To promote protein folding 12. What happens to transferrin in the absence of iron ions? A) It binds to its receptor B) It is endocytosed C) It circulates freely in the blood D) It releases iron in endosomes 13. What occurs when transferrin binds to iron? A) It is degraded by lysosomes B) It is recycled back to the cell surface C) It is released into the cytoplasm D) It prevents receptor binding 14. What is the role of dynamin in synaptic transmission? A) It promotes vesicle budding B) It facilitates endocytosis C) It assists in cargo transfer D) It stabilizes SNARE complexes 15. What happens if dynamin is defective? A) Vesicle retrieval from the membrane is enhanced B) Endocytosis is blocked C) SNARE proteins are overproduced D) Cargo is transferred more efficiently 16. What is the function of t-SNAREs in vesicle docking? A) They sever the vesicle neck B) They bind to Rab proteins C) They form a complex with v-SNAREs D) They promote uncoating 17. What is a potential effect of a mutation that interferes with the ER signal sequence?  A) Enhanced protein folding B) Prevention of protein entry into the ER C) Increased vesicle budding D) Stabilization of the protein structure 18. What is the role of lysosomal targeting signals? A) To promote protein synthesis B) To direct mutated proteins to lysosomes for degradation C) To enhance vesicle docking D) To stabilize SNARE complexes 19. What is the significance of phosphoinositide hydrolysis in vesicle uncoating? A) It promotes cargo transfer B) It activates Rab proteins C) It contributes to coat disassembly D) It enhances SNARE complex formation 20. What is the primary function of the trans-SNARE complex? A) To initiate coat assembly B) To promote fusion of vesicle and acceptor lipid bilayers C) To recycle coat proteins D) To sever the vesicle neck 21. What happens to the receptor after transferrin releases iron in endosomes? A) It is degraded B) It is recycled back to the cell surface C) It is transported to lysosomes D) It binds to new transferrin molecules 22. What is the role of accessory proteins during the scission step? A) They assist in coat assembly B) They sever the neck of the vesicle C) They promote cargo concentration D) They facilitate uncoating 23. What is the consequence of a continuous ER/Golgi retrieval signal? A) The protein is secreted B) The protein is trapped within the cell C) The protein is degraded D) The protein is synthesized more efficiently 24. How does the cytoskeleton assist in vesicle transport? A) By degrading misfolded proteins B) By guiding the vesicle to the acceptor compartment C) By promoting coat assembly D) By enhancing SNARE complex formation 25. What is the primary role of transmembrane cargo proteins during coat assembly? A) To sever the vesicle neck  B) To bind to GTPases C) To gather at the assembling coat D) To promote uncoating 26. What is the effect of a point mutation on protein synthesis? A) It always enhances synthesis B) It may lead to defective protein synthesis C) It has no effect on synthesis D) It guarantees proper folding 27. What is the role of the acceptor compartment in vesicle transport? A) To initiate coat assembly B) To serve as the destination for cargo transfer C) To degrade misfolded proteins D) To recycle SNARE proteins 28. What happens to coat proteins after uncoating? A) They are degraded B) They are recycled for additional rounds of vesicle budding C) They are permanently inactivated D) They are transported to lysosomes 29. What is the significance of the lower pH in endosomes for transferrin? A) It enhances receptor binding B) It promotes iron release C) It prevents endocytosis D) It stabilizes the transferrin structure 30. What is the function of the v-SNAREs in the docking process? A) They sever the vesicle neck B) They bind to Rab proteins C) They form a complex with t-SNAREs D) They promote uncoating 31. What is the role of GTPase in the initiation of coat assembly? A) It promotes vesicle fusion B) It recruits coat components to the donor compartment C) It degrades misfolded proteins D) It assists in cargo transfer 32. What is a potential outcome of protein misfolding in the ER? A) Increased protein secretion B) Accumulation of misfolded proteins C) Enhanced vesicle docking D) Improved receptor binding 33. How does the binding of Rab proteins to effectors assist in vesicle transport? A) By promoting uncoating B) By facilitating docking to target membranes  C) By severing the vesicle neck D) By enhancing cargo concentration 34. What is the primary function of the coat components during vesicle budding? A) To degrade misfolded proteins B) To polymerize into a mesh-like structure C) To assist in cargo transfer D) To recycle SNARE proteins 35. What happens to the receptor after transferrin binds to iron? A) It is degraded B) It is recycled back to the cell surface C) It is transported to lysosomes D) It is released into the cytoplasm 36. What is the role of the cytoskeleton in vesicle transport? A) To degrade misfolded proteins B) To guide the vesicle to the acceptor compartment C) To promote coat assembly D) To enhance SNARE complex formation 37. What is the consequence of a mutation that destabilizes a protein? A) Enhanced protein function B) Increased protein synthesis C) Defective protein synthesis D) Improved protein folding 38. What is the role of the trans-SNARE complex in vesicle fusion? A) To sever the vesicle neck B) To promote the fusion of vesicle and acceptor lipid bilayers C) To recycle coat proteins D) To enhance cargo concentration 39. What is the effect of phosphoinositide hydrolysis on vesicle uncoating? A) It promotes cargo transfer B) It activates Rab proteins C) It contributes to coat disassembly D) It enhances SNARE complex formation 40. What is the primary function of the coat proteins during vesicle budding? A) To degrade misfolded proteins B) To polymerize into a mesh-like structure C) To assist in cargo transfer D) To recycle SNARE proteins 41. What happens to the receptor after transferrin releases iron in endosomes? A) It is degraded B) It is recycled back to the cell surface C) It is transported to lysosomes  D) It binds to new transferrin molecules 42. What is the role of dynamin in synaptic transmission? A) It promotes vesicle budding B) It facilitates endocytosis C) It assists in cargo transfer D) It stabilizes SNARE complexes 43. What happens if dynamin is defective? A) Vesicle retrieval from the membrane is enhanced B) Endocytosis is blocked C) SNARE proteins are overproduced D) Cargo is transferred more efficiently 44. What is the consequence of a continuous ER/Golgi retrieval signal? A) The protein is secreted B) The protein is trapped within the cell C) The protein is degraded D) The protein is synthesized more efficiently 45. How does the cytoskeleton assist in vesicle transport? A) By degrading misfolded proteins B) By guiding the vesicle to the acceptor compartment C) By promoting coat assembly D) By enhancing SNARE complex formation 46. What is the primary role of transmembrane cargo proteins during coat assembly? A) To sever the vesicle neck B) To bind to GTPases C) To gather at the assembling coat D) To promote uncoating 47. What is the effect of a point mutation on protein synthesis? A) It always enhances synthesis B) It may lead to defective protein synthesis C) It has no effect on synthesis D) It guarantees proper folding 48. What is the role of the acceptor compartment in vesicle transport? A) To initiate coat assembly B) To serve as the destination for cargo transfer C) To degrade misfolded proteins D) To recycle SNARE proteins 49. What happens to coat proteins after uncoating? A) They are degraded B) They are recycled for additional rounds of vesicle budding C) They are permanently inactivated D) They are transported to lysosomes 50. What is the significance of the lower pH in endosomes for transferrin? A) It enhances receptor binding B) It promotes iron release C) It prevents endocytosis D) It stabilizes the transferrin structure 51. What is the function of the v-SNAREs in the docking process? A) They sever the vesicle neck B) They bind to Rab proteins C) They form a complex with t-SNAREs D) They promote uncoating 52. What is the role of GTPase in the initiation of coat assembly? A) It promotes vesicle fusion B) It recruits coat components to the donor compartment C) It degrades misfolded proteins D) It assists in cargo transfer 53. What is a potential outcome of protein misfolding in the ER? A) Increased protein secretion B) Accumulation of misfolded proteins C) Enhanced vesicle docking D) Improved receptor binding 54. How does the binding of Rab proteins to effectors assist in vesicle transport? A) By promoting uncoating B) By facilitating docking to target membranes C) By severing the vesicle neck D) By enhancing cargo concentration 55. What is the primary function of the coat components during vesicle budding? A) To degrade misfolded proteins B) To polymerize into a mesh-like structure C) To assist in cargo transfer D) To recycle SNARE proteins 56. What happens to the receptor after transferrin binds to iron? A) It is degraded B) It is recycled back to the cell surface C) It is transported to lysosomes D) It is released into the cytoplasm 57. What is the role of the cytoskeleton in vesicle transport? A) To degrade misfolded proteins B) To guide the vesicle to the acceptor compartment C) To promote coat assembly D) To enhance SNARE complex formation 58. What is the consequence of a mutation that destabilizes a protein?  A) Enhanced protein function B) Increased protein synthesis C) Defective protein synthesis D) Improved protein folding 59. What is the role of the trans-SNARE complex in vesicle fusion? A) To sever the vesicle neck B) To promote the fusion of vesicle and acceptor lipid bilayers C) To recycle coat proteins D) To enhance cargo concentration 60. What is the effect of phosphoinositide hydrolysis on vesicle uncoating? A) It promotes cargo transfer B) It activates Rab proteins C) It contributes to coat disassembly D) It enhances SNARE complex formation 61. What is the primary function of the coat proteins during vesicle budding? A) To degrade misfolded proteins B) To polymerize into a mesh-like structure C) To assist in cargo transfer D) To recycle SNARE proteins 62. What happens to the receptor after transferrin releases iron in endosomes? A) It is degraded B) It is recycled back to the cell surface C) It is transported to lysosomes D) It binds to new transferrin molecules 63. What is the role of dynamin in synaptic transmission? A) It promotes vesicle budding B) It facilitates endocytosis C) It assists in cargo transfer D) It stabilizes SNARE complexes 64. What happens if dynamin is defective? A) Vesicle retrieval from the membrane is enhanced B) Endocytosis is blocked C) SNARE proteins are overproduced D) Cargo is transferred more efficiently 65. What is the consequence of a continuous ER/Golgi retrieval signal? A) The protein is secreted B) The protein is trapped within the cell C) The protein is degraded D) The protein is synthesized more efficiently 66. How does the cytoskeleton assist in vesicle transport? A) By degrading misfolded proteins  B) By guiding the vesicle to the acceptor compartment C) By promoting coat assembly D) By enhancing SNARE complex formation 67. What is the primary role of transmembrane cargo proteins during coat assembly? A) To sever the vesicle neck B) To bind to GTPases C) To gather at the assembling coat D) To promote uncoating 68. What is the effect of a point mutation on protein synthesis? A) It always enhances synthesis B) It may lead to defective protein synthesis C) It has no effect on synthesis D) It guarantees proper folding 69. What is the role of the acceptor compartment in vesicle transport? A) To initiate coat assembly B) To serve as the destination for cargo transfer C) To degrade misfolded proteins D) To recycle SNARE proteins 70. What happens to coat proteins after uncoating? A) They are degraded B) They are recycled for additional rounds of vesicle budding C) They are permanently inactivated D) They are transported to lysosomes 71. What is the significance of the lower pH in endosomes for transferrin? A) It enhances receptor binding B) It promotes iron release C) It prevents endocytosis D) It stabilizes the transferrin structure 72. What is the function of the v-SNAREs in the docking process? A) They sever the vesicle neck B) They bind to Rab proteins C) They form a complex with t-SNAREs D) They promote uncoating 73. What is the role of GTPase in the initiation of coat assembly? A) It promotes vesicle fusion B) It recruits coat components to the donor compartment C) It degrades misfolded proteins D) It assists in cargo transfer 74. What is a potential outcome of protein misfolding in the ER? A) Increased protein secretion B) Accumulation of misfolded proteins  C) Enhanced vesicle docking D) Improved receptor binding 75. How does the binding of Rab proteins to effectors assist in vesicle transport? A) By promoting uncoating B) By facilitating docking to target membranes C) By severing the vesicle neck D) By enhancing cargo concentration 76. What is the primary function of the coat components during vesicle budding? A) To degrade misfolded proteins B) To polymerize into a mesh-like structure C) To assist in cargo transfer D) To recycle SNARE proteins 77. What happens to the receptor after transferrin binds to iron? A) It is degraded B) It is recycled back to the cell surface C) It is transported to lysosomes D) It is released into the cytoplasm 78. What is the role of the cytoskeleton in vesicle transport? A) To degrade misfolded proteins B) To guide the vesicle to the acceptor compartment C) To promote coat assembly D) To enhance SNARE complex formation 79. What is the consequence of a mutation that destabilizes a protein? A) Enhanced protein function B) Increased protein synthesis C) Defective protein synthesis D) Improved protein folding 80. What is the role of the trans-SNARE complex in vesicle fusion? A) To sever the vesicle neck B) To promote the fusion of vesicle and acceptor lipid bilayers C) To recycle coat proteins D) To enhance cargo concentration 81. What is the effect of phosphoinositide hydrolysis on vesicle uncoating? A) It promotes cargo transfer B) It activates Rab proteins C) It contributes to coat disassembly D) It enhances SNARE complex formation 82. What is the primary function of the coat proteins during vesicle budding? A) To degrade misfolded proteins B) To polymerize into a mesh-like structure C) To assist in cargo transfer  D) To recycle SNARE proteins 83. What happens to the receptor after transferrin releases iron in endosomes? A) It is degraded B) It is recycled back to the cell surface C) It is transported to lysosomes D) It binds to new transferrin molecules 84. What is the role of dynamin in synaptic transmission? A) It promotes vesicle budding B) It facilitates endocytosis C) It assists in cargo transfer D) It stabilizes SNARE complexes 85. What happens if dynamin is defective? A) Vesicle retrieval from the membrane is enhanced B) Endocytosis is blocked C) SNARE proteins are overproduced D) Cargo is transferred more efficiently 86. What is the consequence of a continuous ER/Golgi retrieval signal? A) The protein is secreted B) The protein is trapped within the cell C) The protein is degraded D) The protein is synthesized more efficiently 87. How does the cytoskeleton assist in vesicle transport? A) By degrading misfolded proteins B) By guiding the vesicle to the acceptor compartment C) By promoting coat assembly D) By enhancing SNARE complex formation 88. What is the primary role of transmembrane cargo proteins during coat assembly? A) To sever the vesicle neck B) To bind to GTPases C) To gather at the assembling coat D) To promote uncoating 89. What is the effect of a point mutation on protein synthesis? A) It always enhances synthesis B) It may lead to defective protein synthesis C) It has no effect on synthesis D) It guarantees proper folding 90. What is the role of the acceptor compartment in vesicle transport? A) To initiate coat assembly B) To serve as the destination for cargo transfer C) To degrade misfolded proteins D) To recycle SNARE proteins 91. What happens to coat proteins after uncoating? A) They are degraded B) They are recycled for additional rounds of vesicle budding C) They are permanently inactivated D) They are transported to lysosomes 92. What is the significance of the lower pH in endosomes for transferrin? A) It enhances receptor binding B) It promotes iron release C) It prevents endocytosis D) It stabilizes the transferrin structure 93. What is the function of the v-SNAREs in the docking process? A) They sever the vesicle neck B) They bind to Rab proteins C) They form a complex with t-SNAREs D) They promote uncoating 94. What is the role of GTPase in the initiation of coat assembly? A) It promotes vesicle fusion B) It recruits coat components to the donor compartment C) It degrades misfolded proteins D) It assists in cargo transfer 95. What is a potential outcome of protein misfolding in the ER? A) Increased protein secretion B) Accumulation of misfolded proteins C) Enhanced vesicle docking D) Improved receptor binding 96. How does the binding of Rab proteins to effectors assist in vesicle transport? A) By promoting uncoating B) By facilitating docking to target membranes C) By severing the vesicle neck D) By enhancing cargo concentration 97. What is the primary function of the coat components during vesicle budding? A) To degrade misfolded proteins B) To polymerize into a mesh-like structure C) To assist in cargo transfer D) To recycle SNARE proteins 98. What happens to the receptor after transferrin binds to iron? A) It is degraded B) It is recycled back to the cell surface C) It is transported to lysosomes D) It is released into the cytoplasm 99. What is the role of the cytoskeleton in vesicle transport?  A) To degrade misfolded proteins B) To guide the vesicle to the acceptor compartment C) To promote coat assembly D) To enhance SNARE complex formation 100. What is the consequence of a mutation that destabilizes a protein? A) Enhanced protein function B) Increased protein synthesis C) Defective protein synthesis D) Improved protein folding