Cytoskeleton Quiz

A network of protein filaments in the cytoplasm that maintain cell shape and enable cell and organelle movement.

Thin protein filaments made of actin; part of the cytoskeleton.

A protein that forms microfilaments, important for cell movement and shape.

Globular form of actin monomer; building block for microfilaments.

Filamentous form of actin; formed from multiple G-actin monomers.

Different forms of actin found in muscle (α-actin) and non-muscle cells (β- and γ-actin).

The faster-growing end of an actin filament.

The slower-growing end of an actin filament.

Proteins that regulate the length of actin filaments.

Protein bundles formed by fimbrin and villin, crucial for microspikes and microvilli structure.

Network of intermediate filaments and spectrin, anchoring actin bundles in cells.

Cytoskeleton components, 8-10 nm in diameter, supporting cell structure and anchoring.

Provide structural support, anchor the nucleus, and connect to the cell membrane and cytoskeleton.

Constructed from eight tetramers of rod-like proteins, forming a rope-like structure.

Various types include keratins, desmin, vimentin, glial fibrillary acidic protein, neurofilaments, and nuclear lamins.

Actin filaments, also known as microfilaments, are protein structures that form bundles in non-muscle cells. These bundles come in three types: contractile bundles, gel-like networks, and parallel bundles.

Contractile bundles are a type of actin filament arrangement in non-muscle cells characterized by loosely packed, parallel actin filaments arranged with alternating plus and minus ends. Myosin is usually associated with these bundles for movement.

The cell cortex is a layer of the cell, right beneath the membrane, which is a primary factor in determining cell shape.

Stress fibers are contractile actin bundles found in non-muscle cells that provide strength.

Areas where the cell connects to the extracellular matrix. Actin is involved in these connections.

Actin filament arrangements that form a network in the cell cortex; they are responsible for providing structural support

A protein that interacts with actin filaments to drive movement in the cell. It's crucial for many cell activities like cell division.

A transmembrane protein that plays a role in the cell's attachment to the extracellular matrix.

Extensions of the cell membrane used by cells to sense their environment during migration, and are part of contractile bundles.

Some drugs, such as Taxol, stabilize microtubules rather than inhibiting their assembly.

Taxol stabilizes microtubules, reducing their flexibility, which arrests cell division and leads to cell death.

An inherited disorder causing cilia dysfunction, leading to respiratory issues (bronchiectasis) and infertility.

A genetic skin disorder causing blisters due to defective keratin proteins.

Proteins that provide structural strength and stability to skin cells.

Directional property of microtubules enabling specific transport routes for vesicles.

Affects microtubule stability, causing mitotic arrest, resulting in cell death.

A heterodimer of alpha-tubulin (minus end) and beta-tubulin (plus end), polymerizing to form hollow tubes with a spiral organization.

Provides cell structure, regulates organelle transport, establishes compartments, and enables ciliary/flagellar motion.

Structures that direct microtubule polymerization.

Organized around two centrioles, each with nine microtubule triplets.

Microtubules facilitate transport of vesicles, organelles, and macromolecules within the cell..

Proteins that use ATP to move material along microtubules.

Motor proteins that carry material away from the MTOC (anterograde transport).

Motor proteins that carry material toward the MTOC (retrograde transport).

The plus and minus ends of microtubules determine the direction of vesicular transport.

Drugs that interfere with microtubule function, often for treatment of cancer or other conditions.

Drugs that inhibit microtubule polymerization, stopping cell division.

A family of proteins that form heterodimer subunits of intermediate filaments in epithelial cells, maintaining cellular mechanical stability.

Inherited skin disease caused by mutations in keratin 5 and 14 genes, causing skin blisters after minor trauma.

Skin disease with excessive keratinization due to mutations in keratin 1 and 10 genes.

Skin disease causing epidermis fragmentation, especially on palms and soles; caused by a mutation in the keratin 9 gene.

Common intermediate filament protein found in cells from embryonic mesenchyme.

Vimentin-like protein found in muscle cells.

Vimentin-like protein found in astrocytes (nervous system support cells).

Proteins forming the subunits of intermediate filaments in neurons.

Structural framework inside the nucleus formed by lamins, a family of proteins.

Hollow, tubular structures in eukaryotic cell cytoplasm, maintaining cell shape.

Proteins linking intermediate filaments to form a complex network in the cytoskeleton.

Protein that bundles keratin filaments.

Proteins binding intermediate filaments (desmin/vimentin) to form 3D networks.

Proteins maintaining connections between keratin filaments and hemidesmosomes, as well as actin and neurofilaments.