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LIFE 210 (38)
Lecture

Actin filaments, microtubules, filament structure/formation/dynamics

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Department
Life Science
Course
LIFE 210
Professor
Paul Laybourn
Semester
Fall

Description
11 November Nucleation is the rate-limiting step in polymer formation Formins nucleate the growth of straight, unbranched filaments Remains associated with the growing plus end as the filament elongates Dimeric protein Proteins that bind to the free actin subunit modify filament elongation Thymosin binds actin subunits and prevents incorporation in the filament. Profilin does the opposite. Stathmin binds to tubulin dimers and inhibits polymerization. Signals such as phosphorylation change the equilibrium. Severing proteins regulate the length and kinetic behavior of actin filaments and microtubules Katanin severs microtubules. Requires ATP. Gelsolin severs actin filaments. Proteins that bind along the sides of filaments can either stabilize or destabilize them Microtubule-associated proteins (MAPs) stabilize microtubules Different lengths of projecting domain bundles microtubules at different density. Tau – axon MAP2 – dendrites and cell body Tropomyosin stabilizes actin filaments. Important for muscle contraction. Cofilin forces the filament to twist more and become brittle. It also speeds up ADP-actin dissociation from the minus end. Proteins that interact with filament ends can dramatically change filament dynamics Large effect on filament dynamics with low protein amounts Capping protein (Ca
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