Cytoskeleton
Cytoskeleton Overview
Lesson Objectives
Describe the components and function of the cytoskeleton.
Describe the molecular structure of actin microfilaments.
Summarize how microfilaments change the shape of the cell.
Predict the effects of changes to actin or actin-affiliated protein structure.
Role of the Cytoskeleton
The cytoskeleton plays a crucial role in:
Adopting a variety of shapes in cells
Carrying out coordinated directed movements
Dividing during cell division
Organizing intracellular space
Definition: Cytoskeleton is defined as a dynamic and complex network of protein filaments that extend throughout the cell.
Types of Filaments
Microfilaments
Building Block: Actin
Purpose: Membrane motility and structure; facilitates movement and transport.
Location: Cytoplasm of all cells, particularly near the membrane.
Microtubules
Building Block: Tubulin
Purpose: Cargo transport; facilitates cell cycle division.
Location: Cytoplasm of all cells.
Intermediate Filaments
Building Block: Varies (depends on cell type)
Purpose: Provides structural support to cells.
Location: Intra- or extracellularly.
Microfilaments and Phagocytosis
Microfilaments are essential in phagocytosis due to various factors:
The actin gene is present in every cell of the human body.
Actin is more flexible than microtubules or intermediate filaments.
Actin is encoded by nearly every eukaryote.
Myosin only binds to actin, making it crucial for motor functions in cellular processes.
Molecular Structure of Microfilaments
Monomer: Globular actin (G-actin)
Filament: Filamentous actin (F-actin)
They are involved in various cellular processes related to cell shape and intracellular transport.
Growth Dynamics: G-actin builds faster at the (+) end than at the (-) end.
Assembly of Microfilaments
Three Steps in Assembly:
Nucleation Phase:
This is the rate-limiting step and is facilitated by seed proteins such as formin or Arp2/3.
Elongation Phase:
Rapid expansion of filament assembly occurs once oligomers of 2-3 subunits form.
Steady-State Phase:
Assembly continues until the concentration of G-actin/F-actin reaches equilibrium.
Critical Concentration
Actin exists in a dynamic equilibrium between globular and filamentous forms.
This equilibrium is referred to as the critical concentration.
Factors affecting critical concentration:
Increased cation concentration or ADP can decrease the critical concentration of actin filaments.
Treadmilling Phenomenon
Definition: Treadmilling occurs when there is asymmetry in the rate of elongation at the two ends (poles) of a filament, coupled with a symmetric rate of dissociation at both poles.
Treadmilling is a dynamic process that balances addition and removal of actin monomers, maintaining filament length while allowing for flexibility in cellular processes.
Actin-Binding Proteins
Different proteins play specific roles in regulating the dynamics of actin:
Polymerization Regulators:
Profilin (positive regulator)
Thymosin b4 (negative regulator)
Length Regulators:
Cofilin
Nucleation and Branching:
Arp2/3 complex
Cross-linking Proteins:
Filamin
Motor Proteins:
Myosin
Stability (Capping):
Capping proteins regulate the growth/shrinkage of filaments.
Enhancing Actin Building
Profilin and cofilin enhance polymerization rates of actin filaments.
Thymosin and capping proteins can suppress or halt actin building.
Impact of Toxins on Actin Dynamics
Toxin Example: Paraquat is a widely used herbicide that binds to G-actin.
It facilitates polymerization into filaments irreversibly.
These changing filaments alter the shape and ultimately the function of cells.
The low concentration of G-actin within the cell causes it to respond by increasing actin expression (Wang et al., 2023).
Actin in Cell Motility
Actin filaments (either unbranched via formin or branched via Arp2/3) contribute to the mechanical forces that push or pull the plasma membrane and intracellular vesicles.
Actin filaments are also involved in endocytosis.
Illustrative Figures:
Effects of actin on cell structures are detailed in Figures 17-17, 17-4, and 17-19 in the MCB textbook.
Movement of Amoebae
Conceptual diagram required:
Discuss how pseudopodia are formed and how actin filaments are involved in this process of cell movement.
Cross-linking of Actin Filaments
Actin filaments often bundle together due to the action of cross-linking proteins, which increases their mechanical strength.
Adapter proteins frequently connect microfilaments to the cell membrane, contributing to overall cell stability.
Myosin Structure and Function
Composition: Each myosin molecule consists of 1-2 actin-binding heads, light chain "necks," and heavy chain tails.
ATPase Activity: The head of the myosin is where the ATPase activity occurs, essential for actin-myosin interactions during muscle contraction.
Power Stroke Mechanism:
During a power stroke, ADP is replaced with ATP in the myosin head, causing myosin to release from actin.
Hydrolysis of the ATP molecule leads to a conformational change in the neck region of myosin.
Myosin rebinds to a new actin residue, returning to its original position.
Myosin heads operate in an alternating "hand over hand" pattern to create movement along actin filaments.
Implications for Rigor Mortis
Rigor Mortis Mechanism:
ATP depletion during rigor mortis leads to muscle cells becoming incapable of detaching myosin heads from actin filaments, thus freezing muscles in their current contracted shape.
This phenomenon illustrates the crucial role of ATP in muscle function and contraction.
Myosin as a Carrier Protein
Myosin can serve a dual function as both a motor and a carrier protein.
If myosin's tail is attached to cargo, it can effectively transport this cargo along actin trackways using the hand-over-hand mechanism.
Conclusion: Lesson Objectives Review
Review and recap:
Components and functions of the cytoskeleton
Molecular structure of actin microfilaments
Summary of the role of microfilaments in altering cell shape
Predictions regarding structural changes in actin or actin-affiliated proteins and their potential effects on cellular function and dynamics.