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Cytoskeleton, GTP-binding causes a conformational switch that dictates…

- - - - no distinct ends/polarity
    - - overlapping lateral, noncovalent interactions along length of intermediate filament protein
    - - unstructured domains are exposed on surface of filament, allowing it to interact with specific components in the cytoplasm
  - - - Connective Tiss
    - - Nerve cells
        
        ALS, Lou Gehrig's Disease
    - - epithelial cells
        
        epidermolysis bullosa simplex
    - - nuclear envelope
        
        progeria
  - - - IFs in mescule
      - neurofilaments
      - skin keratin
- - - - alpha-beta dimer
        
        alpha -end
        
        beta +end
        
        has GTP molecule bound to it
    - - 13 of them arranged parallel and slightly staggered make up a microtubule
    - - polymerization
        
        addition of dimers faster than hydrolyzing GTP
      - depolymerization
        
        hydrolyzing GTP faster than addition of dimers
      - driven by local pool of GTP heterodimer
  - - - dynein
        
        move towards - end, inwards towards cell body
      - kinesin
        
        move towards + end, outward from cell body
      - globular head
        
        ATPase (ATP-hydrolyzing activity) that provides E for driving directed series of conformational changes in head that enables movement
      - tail
        
        determines type of cargo being transported bc binds stable to a cell component (vesicle or organelle)
- - - - halt polymerization
        
        Thymosin, profilin
        
        keep actin monomers in reserve until required to regulate actin polymerization
      - promote polymerization
        
        formins, actin-related proteins (ARPs)
        
        come into play when actin filaments are needed
      - actin bundling proteins
        
        hold actin filaments together in parallel bundles- microvilli
  - - - can grow via addition of monomers at either end
        
        growth at + end is faster than - end