An actin filament undergoing treadmilling at the leading edge of a lamellipodium can do what? Choose one: add actin monomers to its minus end while losing them from its plus end experience exponential growth collapse and instantly disappear remain the same size
Added by Heather B.
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Step 1: Actin filament undergoing treadmilling at the leading edge of a lamellipodium adds actin monomers to its plus end while losing them from its minus end. Show more…
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Consider an actin subunit that has just been incorporated into an actin filament at the leading edge of a lamellipodium. Before its ATP is hydrolyzed, how does its distance from the leading front edge of the plasma membrane change over time? How does its distance from the F-actin minus end change over time? Decreases; decreases Decreases; remains constant Decreases; increases Increases; decreases Increases; remains constant
Qudsiya A.
Under certain stable concentration conditions, actin monomers in their ATP form will polymerize to form filaments that disperse again into free actin monomers over time. Explain.
Actin monomers (globular actin or G-actin) are organized into linear, double-stranded microfilaments which undergo constant formation by polymerization and destruction by depolymerization, so changes in the structure of actin filaments can occur quickly by balancing or unbalancing these processes. Cytochalasin D is a drug isolated from mushrooms that inhibits actin polymerization, while leaving depolymerization unaffected. The figure shows rates of cytoplasmic streaming in Nitella under control, after addition of Cytochalasin D and then following washout of the drug. Mark on the figure one time each when (i) polymerization > depolymerization and (ii) depolymerization > polymerization of actin filaments.
Madhur L.
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