Blocking actin depolymerization prevents normal filament turnover, producing unusually stable actin networks and bundles.
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28A cell has normal actin polymerization but defective myosin II activity. Which event would be most impaired?
Intermediate filaments and Actin Filaments
Medium
A.Transport toward microtubule minus ends
B.Assembly of nuclear pore subunits
C.Maintenance of nuclear lamina structure
D.Formation of the contractile ring
Correct Answer: Formation of the contractile ring
Explanation:
Myosin II interacts with actin filaments to generate contraction during cytokinesis and other contractile processes.
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29Which feature best explains why intermediate filaments are especially useful for resisting mechanical stress?
Intermediate filaments and Actin Filaments
Medium
A.They undergo rapid treadmilling
B.They form strong, flexible cable-like networks
C.They hydrolyze ATP during contraction
D.They organize chromosomes at kinetochores
Correct Answer: They form strong, flexible cable-like networks
Explanation:
Intermediate filaments form durable networks that withstand stretching and mechanical deformation better than many rapidly remodeling cytoskeletal structures.
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30A mutation removes a nucleoporin that forms part of the central transport channel. Which consequence is most likely?
Nuclear Envelope- structure of nuclear pore complex
Medium
A.Actin filaments cannot bind myosin
B.Microtubules lose their polarity
C.Selective nuclear transport becomes defective
D.Intermediate filaments become phosphorylated
Correct Answer: Selective nuclear transport becomes defective
Explanation:
Nucleoporins create the nuclear pore complex and its selective permeability barrier, so their loss disrupts regulated transport.
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31Why can small ions pass through nuclear pore complexes more freely than large protein complexes?
Nuclear Envelope- structure of nuclear pore complex
Medium
A.Small molecules contain nuclear localization signals, whereas large cargo lacks them
B.Large cargo crosses through the nuclear membrane, whereas ions use pores
C.Small molecules are actively transported by dynein through the pore
D.Small molecules diffuse through the pore, whereas larger cargo requires transport receptors
Correct Answer: Small molecules diffuse through the pore, whereas larger cargo requires transport receptors
Explanation:
Nuclear pores permit passive diffusion of small molecules, while larger macromolecules generally require receptor-mediated transport.
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32A defect prevents nuclear pore complexes from being inserted into the double membrane of the nuclear envelope. Which structure would be directly affected?
Nuclear Envelope- structure of nuclear pore complex
Medium
A.Attachment of ribosomes to rough endoplasmic reticulum
B.Exchange between nucleoplasm and cytoplasm
C.Formation of desmosomal intermediate filaments
D.Polymerization of cytoplasmic actin
Correct Answer: Exchange between nucleoplasm and cytoplasm
Explanation:
Nuclear pore complexes provide the main regulated pathways for movement between the nucleus and cytoplasm.
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33A mutation reduces lamin filament assembly. Which nuclear defect would be most likely?
The nuclear lamina supports the inner nuclear membrane and helps maintain nuclear shape and mechanical stability.
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34During mitosis, phosphorylation of nuclear lamins promotes which event?
Nuclear lamina
Medium
A.Permanent closure of nuclear pores
B.Activation of actin-based muscle contraction
C.Disassembly of the nuclear lamina
D.Assembly of cytoplasmic intermediate filaments
Correct Answer: Disassembly of the nuclear lamina
Explanation:
Mitotic phosphorylation reduces lamin interactions, allowing the nuclear lamina and nuclear envelope to disassemble.
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35A cell expresses a lamin variant that cannot be properly modified after translation. Which process may be disrupted during cell division?
Nuclear lamina
Medium
A.Movement of vesicles along intermediate filaments
B.Formation of actin branches at the leading edge
C.Polymerization of tubulin at axon terminals
D.Reassembly of the nuclear envelope
Correct Answer: Reassembly of the nuclear envelope
Explanation:
Post-translational processing helps regulate lamin association with the nuclear envelope, which is important during nuclear-envelope reassembly.
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36A protein containing a functional nuclear localization signal is synthesized in the cytoplasm. Which factor typically recognizes this signal?
Protein import and export through Nuclear pore complex
Medium
A.Importin
B.A lamin-associated protein
C.Exportin
D.Kinesin
Correct Answer: Importin
Explanation:
Importins recognize nuclear localization signals and escort cargo through the nuclear pore complex.
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37A nuclear protein remains in the cytoplasm even though its nuclear localization signal is intact. A mutation in which factor could explain this result?
Protein import and export through Nuclear pore complex
Medium
A.Nuclear exportin
B.Intermediate-filament cross-linker
C.Actin nucleator
D.Cytoplasmic importin
Correct Answer: Cytoplasmic importin
Explanation:
Importin is required to bind the nuclear localization signal and deliver the protein to the nuclear pore complex.
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38A newly synthesized RNA-binding protein must leave the nucleus after binding an export receptor. Which signal would most directly support this transport?
Protein import and export through Nuclear pore complex
Medium
A.Nuclear localization signal
B.Actin-binding domain
C.Microtubule plus-end cap
D.Nuclear export signal
Correct Answer: Nuclear export signal
Explanation:
Export receptors recognize nuclear export signals and transport their cargo from the nucleus to the cytoplasm.
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39A transcription factor is retained in the cytoplasm when a signaling pathway keeps it bound to an inhibitory protein. How does this regulation work?
Regulation of Nuclear protein import and export
Medium
A.The inhibitor converts the nuclear pore into a lipid channel
B.The inhibitor depolymerizes all nuclear lamins
C.The inhibitor changes importin into a microtubule motor
D.The inhibitor masks the transcription factor's nuclear localization signal
Correct Answer: The inhibitor masks the transcription factor's nuclear localization signal
Explanation:
Binding of an inhibitor can hide the localization signal, preventing importin recognition and nuclear entry.
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40Why is the Ran-GTP/Ran-GDP gradient important for directional nuclear transport?
Regulation of Nuclear protein import and export
Medium
A.It provides spatial information that controls receptor-cargo binding
B.It polymerizes the nuclear lamina during interphase
C.It supplies ATP directly to nuclear pore complexes
D.It creates actin filaments inside the nuclear envelope
Correct Answer: It provides spatial information that controls receptor-cargo binding
Explanation:
High Ran-GTP in the nucleus and high Ran-GDP in the cytoplasm regulate importin and exportin interactions, giving transport directionality.
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41A cell expresses a tubulin mutant that retains GTP binding but cannot hydrolyze tubulin-bound GTP after polymerization. Which phenotype is most likely?
Structure and functions of Microtubules
Hard
A.Microtubules become shorter and more dynamic
B.Microtubules assemble only from intermediate filaments
C.Microtubules become unusually stable and resist catastrophe
D.Microtubules lose polarity but retain normal length
Correct Answer: Microtubules become unusually stable and resist catastrophe
Explanation:
GTP hydrolysis creates a destabilizing GDP-tubulin lattice. Preventing hydrolysis preserves the stabilizing GTP cap and reduces catastrophe.
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42A drug selectively prevents microtubule minus ends from being anchored at centrosomes but does not affect tubulin polymerization. Which consequence is most likely in a migrating animal cell?
Structure and functions of Microtubules
Hard
A.Permanent activation of myosin contraction
B.Loss of all actin-based protrusions
C.Conversion of microtubules into intermediate filaments
D.Randomization of microtubule array orientation
Correct Answer: Randomization of microtubule array orientation
Explanation:
Centrosomal anchoring normally focuses minus ends near the nucleus and directs plus ends toward the cell periphery. Loss of anchoring disrupts array organization without directly blocking polymerization.
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43A vesicle normally transported toward the cell center continues moving after dynein inhibition but accumulates near the cell cortex. Which interpretation best explains the result?
B.Kinesin drives transport toward microtubule plus ends
C.Myosin drives transport along microtubule plus ends
D.Dynein drives transport toward microtubule plus ends
Correct Answer: Kinesin drives transport toward microtubule plus ends
Explanation:
In most radial arrays, plus ends extend toward the cortex. Kinesin-driven outward transport can continue when dynein-mediated inward transport is inhibited.
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44A mitotic cell is treated with a compound that suppresses microtubule catastrophe but leaves kinetochore attachment intact. Which defect is most likely?
Structure and functions of Microtubules
Hard
A.Failure to assemble intermediate filament dimers
B.Failure to correct improper kinetochore attachments
C.Failure to synthesize actin monomers
D.Failure to form nuclear pores
Correct Answer: Failure to correct improper kinetochore attachments
Explanation:
Microtubule turnover is required to test and correct erroneous kinetochore attachments. Excessive stabilization can preserve incorrect attachments and impair chromosome segregation.
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45A keratin mutation prevents formation of stable lateral interactions between keratin tetramers but does not affect keratin expression. Which cellular property is most directly compromised?
Intermediate filaments and Actin Filaments
Hard
A.Resistance to tensile stress
B.ATP-dependent vesicle transport
C.Chromosome attachment to kinetochores
D.GTP-dependent microtubule growth
Correct Answer: Resistance to tensile stress
Explanation:
Intermediate filaments form mechanically resilient networks. Defective lateral assembly weakens tissues that depend on keratin-mediated resistance to stretching and shear.
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46A nonhydrolyzable ATP-actin analog is incorporated into a growing filament. Compared with normal actin, what is the most likely effect?
Intermediate filaments and Actin Filaments
Hard
A.Loss of all actin-myosin binding
B.Altered treadmilling dynamics
C.Reduced filament polarity
D.Conversion of actin into a microtubule
Correct Answer: Altered treadmilling dynamics
Explanation:
ATP hydrolysis in filamentous actin contributes to age-dependent differences between filament ends. Blocking hydrolysis changes subunit turnover and treadmilling behavior.
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47A cell has normal actin polymerization but lacks functional profilin. Which process is most likely impaired under conditions requiring rapid filament growth?
Intermediate filaments and Actin Filaments
Hard
A.Delivery of ATP-actin to growing barbed ends
B.Dynein movement toward microtubule minus ends
C.Nuclear lamina disassembly
D.Keratin filament cross-linking
Correct Answer: Delivery of ATP-actin to growing barbed ends
Explanation:
Profilin promotes nucleotide exchange on actin and helps channel actin monomers toward polymerizing barbed ends, especially during rapid remodeling.
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48A migrating cell expresses a constitutively active cofilin phosphatase. Which outcome is most likely if cofilin remains persistently active?
Intermediate filaments and Actin Filaments
Hard
A.Selective depolymerization of microtubules
B.Permanent stabilization of stress fibers
C.Enhanced actin turnover and network remodeling
D.Reduced actin filament severing
Correct Answer: Enhanced actin turnover and network remodeling
Explanation:
Active cofilin binds actin filaments, promotes severing and disassembly, and increases the supply of monomers for renewed polymerization.
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49A mutation removes the cytoplasmic filaments of the nuclear pore complex but leaves the central channel intact. Which defect is most likely?
Nuclear Envelope- structure of nuclear pore complex
Hard
A.Complete loss of Ran-GTP production
B.Failure of inner nuclear membrane lipid synthesis
C.Loss of nuclear-envelope membrane continuity
D.Impaired initial capture of import cargo
Correct Answer: Impaired initial capture of import cargo
Explanation:
Cytoplasmic filaments help capture and guide import complexes toward the central transport channel. Their loss can impair cargo engagement without eliminating the pore itself.
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50A nuclear pore complex retains its scaffold but has altered phenylalanine-glycine-rich nucleoporins that no longer form a selective permeability barrier. Which result is expected?
Nuclear Envelope- structure of nuclear pore complex
Hard
A.The nuclear envelope becomes a single membrane
B.Macromolecular selectivity is reduced
C.Ribosomes become permanently attached to lamins
D.Small molecules become unable to diffuse
Correct Answer: Macromolecular selectivity is reduced
Explanation:
FG-repeat nucleoporins form the selective barrier and interact with transport receptors. Disrupting them can permit inappropriate macromolecular passage.
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51A cell contains normal nuclear pores but develops a mutation that prevents fusion of the inner and outer nuclear membranes at pore sites. What is the direct consequence?
Nuclear Envelope- structure of nuclear pore complex
Hard
A.Pores cannot create continuous transport channels
B.Chromatin cannot bind histones
C.Actin filaments cannot nucleate
D.Lamins cannot undergo phosphorylation
Correct Answer: Pores cannot create continuous transport channels
Explanation:
Nuclear pore complexes span both nuclear-envelope membranes. Membrane fusion at pore sites is required to connect the cytoplasm and nucleoplasm.
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52A lamin mutant cannot be phosphorylated during mitosis but retains normal polymerization in interphase. Which phenotype is most likely?
Nuclear lamina
Hard
A.Persistent nuclear-lamina association during mitosis
B.Failure of actin polymerization at the cortex
C.Loss of all nuclear pore complexes during interphase
D.Inability of ribosomes to enter the cytoplasm
Correct Answer: Persistent nuclear-lamina association during mitosis
Explanation:
Mitotic phosphorylation of lamins promotes filament disassembly and nuclear-envelope breakdown. Preventing this modification can maintain an abnormally persistent lamina.
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53A mutation weakens lamin attachment to chromatin without changing lamin abundance. Which nuclear defect is most plausible?
Nuclear lamina
Hard
A.Loss of actin polarity at the leading edge
B.Failure of mitochondrial protein import
C.Increased microtubule catastrophe at centrosomes
The nuclear lamina interacts with chromatin and helps organize heterochromatin near the nuclear periphery. Weak attachment can alter gene positioning and expression.
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54A nucleus has a mechanically defective lamina but normal nuclear pores and normal chromatin composition. Which cellular response is most likely after repeated mechanical stress?
Nuclear lamina
Hard
A.Conversion of lamins into actin filaments
B.Complete inhibition of cytoplasmic translation
C.Increased nuclear deformation and envelope rupture
D.Permanent activation of kinesin motors
Correct Answer: Increased nuclear deformation and envelope rupture
Explanation:
Lamins provide structural support to the nucleus. Their mechanical failure increases nuclear deformation and susceptibility to transient or catastrophic envelope rupture.
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55A nuclear protein contains a functional nuclear localization signal, but its import receptor cannot bind Ran-GTP. Which outcome is most likely?
Protein import and export through Nuclear pore complex
Hard
A.Import can occur, but receptor recycling and cargo release are disrupted
B.Cargo is exported efficiently through CRM1
C.Import becomes independent of the Ran gradient
D.Cargo crosses the lipid bilayer without a pore
Correct Answer: Import can occur, but receptor recycling and cargo release are disrupted
Explanation:
Ran-GTP binding in the nucleus promotes importin release from cargo and supports receptor recycling. Loss of this interaction disrupts the import cycle even if initial cargo recognition remains possible.
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56A protein lacking a classical nuclear localization signal is nevertheless imported efficiently when bound to a partner containing such a signal. What mechanism explains this result?
Protein import and export through Nuclear pore complex
Hard
A.Passive diffusion through the lipid bilayer
B.Direct transport by cytoplasmic dynein
C.Export followed by spontaneous nuclear assembly
D.Piggyback import through an import-competent complex
Correct Answer: Piggyback import through an import-competent complex
Explanation:
A cargo lacking its own signal can enter the nucleus when associated with a partner that binds an import receptor and carries the complex through the pore.
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57A nuclear export cargo binds its export receptor only in the presence of Ran-GTP. If Ran-GTP is experimentally depleted from the nucleus, what happens first?
Protein import and export through Nuclear pore complex
Hard
Many exportins bind cargo cooperatively with Ran-GTP. Reducing nuclear Ran-GTP therefore impairs assembly of export complexes before affecting other nuclear-envelope structures.
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58A transcription factor is phosphorylated near its nuclear localization signal, reducing importin binding. What regulatory outcome is most likely?
Regulation of Nuclear protein import and export
Hard
A.Cytoplasmic retention of the transcription factor
B.Irreversible degradation of all importins
C.Uncoupling of Ran from GTP hydrolysis
D.Constitutive nuclear accumulation
Correct Answer: Cytoplasmic retention of the transcription factor
Explanation:
Modification near an NLS can mask the signal or lower its affinity for importin, shifting the factor toward cytoplasmic retention and reducing nuclear activity.
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59A signaling pathway inhibits the cytoplasmic Ran-GAP while leaving nuclear Ran-GEF active. Which change is expected in the Ran system?
Regulation of Nuclear protein import and export
Hard
A.An increased Ran-GTP gradient across the envelope
B.Ran becomes an integral membrane protein
C.Complete loss of nuclear Ran-GTP
D.A reduced Ran-GTP gradient across the envelope
Correct Answer: A reduced Ran-GTP gradient across the envelope
Explanation:
Ran-GAP normally promotes Ran-GTP hydrolysis in the cytoplasm. Its inhibition raises cytoplasmic Ran-GTP and reduces the nuclear-to-cytoplasmic Ran-GTP gradient.
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60A nuclear export signal is exposed only after ligand binding causes a conformational change in a regulatory protein. Which prediction is most appropriate?
Regulation of Nuclear protein import and export
Hard
A.The protein will enter the nucleus only by passive diffusion
B.Ligand binding can switch the protein from nuclear retention to export
C.Ligand binding must block all passage through nuclear pores
D.The export receptor will hydrolyze ATP to open the pore
Correct Answer: Ligand binding can switch the protein from nuclear retention to export
Explanation:
Conformational exposure of an export signal can permit export-receptor binding, allowing ligand-regulated redistribution between the nucleus and cytoplasm.
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