W2 Cytoskeleton Flashcards
Cytoskeleton
Keep shape + modify to environmental clues
Dynamic structure
Monomers not covalently linked
Network of polymers + function
Microtubules, actin/intermediate filaments
For → shape of cell, intracellular movement of organelles + cell movement
Accessory proteins regulate…?
Site/rate of filament formation = nucleation (polymerisation or assembly reactions where the first steps are energetically less favoured than the continuation of growth)
Polymerization/depolymerization
Function
Cross linking of filaments = forming higher order structures
Signalling of intra/extra w/cytoskeleton assembly modules
What are actin filaments
Helical polymers made of actin
Flexible, organised into 2D networks + 3D gels
Cell/organelle shape
Cell migration
Organisation/regulation = ABP (actin binding proteins)
Actin filaments structure
Twisted chain of units (monomers) of the protein actin (G-actin, approx.43 KDa kilodaltons). This chain constitutes the filamentous form (F-actin)
Helical repeat every 37 nm
Thinnest class of the cytoskeleton filaments (7 nm)
Presents structural polarity = binding of myosin subfragment (S1) to filament causes barbed +ve and pointed -ve ends on filament
Associated with a large number of actin-binding proteins (ABP) = variety of organization and function
There are 3 isoforms (different form of a protein) of G-actin with different isoelectric point (pH were molecule carries no net electrical charge):
α-actin found mainly in muscle cells
β-actin and γ-actin in nonmuscle cells
Actin filaments polymerization
Actin filaments (F-actin) can grow by addition of actin monomers (G-actin) at either end.
The length of the filament is determined by:
Concentration of G-actin.
Presence of Actin Binding proteins (ABPs)
Capping proteins = control access to free barbed ends of actin filaments as have high affinity for barbed ends + micromolar conc in CT ensures most barbed ends capped
Regulation of G actin levels
Profilin: facilitates actin polymerization
Thymosin β4: prevents the addition of actin monomers to F-actin
Actin bundling proteins
Keep F-actin in parallel bundles (as in the microvilli observed in epithelial cells)
Cross-linking proteins
Maintain F-actin in a gel-like meshwork (as seen in the cell cortex, underneath the plasma membrane)
Lamellipodia
Thin protein sheet on actin (propels cell across a substrate)
Filopodia
Thin, tubular protrusions formed at leading edge of motile cells that are composed of linear bundles of actin filaments
Actin in skeletal muscle
Arranged in a paracrystalline array integrated with different ABPs
Interaction with myosin motors allow muscle contraction
Actin in non muscle
Cell cortex = form a thin sheath beneath the plasma membrane
Associated with myosin to form a purse string ring result in cleavage of mitotic cells
Cytokinesis
Actin-myosin ring called contractile forms around equator of cell tightens to form cleavage furrow
Cell migration w/actin
The cell pushes out protrusions at its front (lamellipodia & filopodia)
Actin polymerization
These protrusions adhere to the surface
Integrins (link the actin filaments to the extracellular matrix surrounding the cell)
Cell contraction and retraction of the rear part of the cell
Interaction between actin filaments and myosin