Introduction to Molecular and Cell Biology, Biol. 220

Lecture 27: Actin

Three types of cytosolic fibers:

 

Actin

Actin is the most abundant intracellular protein in eukaryotic cells (10% by weight of total cell protein).

Actin cytoskeleton (Fig. 18.1)

Fig. 18.1  (a) external view of cell and types of podia projections. (b) localization of actin at lamellipodium and as stress fibers.


Yeast have a single actin gene, humans have six actin genes, and some plants have 60 actin genes.
Highly conserved but isoforms exist.

Actin exists in two interchangeable forms

Increasing the ionic strength of a solution by the addition of Mg2+, K+, or Na+ causes G-actin to be converted into F-actin.  Conversely, lowering the ionic strength causes depolymerization back to the G-actin form.

F-actin shows polarity

Fig. 18.2  (a) Structure of actin.  (b) Actin filaments.  (c) Stacking of actin monomers in the F-actin showing polarity of filament.

F-actin stacks in a helical filament (Fig. 18.2c).

Fig. 18.5  (a) Bundled actin filaments (short crosslinker).  (b) Network of actin filaments (long, flexible crosslinker).

Actin is organized into bundles and networks (Fig. 18.4) through the binding of crosslinking protein (Table 18.1). Table 18.1 

Short crosslinking proteins assemble actin filaments into bundles(Fig. 18.5a).
Long, flexible crosslinking proteins can connect actin filament pairs lying at various angles (Fig. 18.5b).

Membrane-bound networks provide a membrane mesh (Fig. 18.6)

Fig. 18.6  Human erythrocyte showing the hubs and linking spectrin network.

that actin presses against to move and support membrane position (Fig. 18.7).

Fig. 18.7  The organization of the major erythrocyte cytoskeletal proteins and their interactions with integral membrane proteins.

Examples

 

 

Activity
Created 2004 by CA Rinehartemail CA Rinehart IndexCourseInfo LogInSyllabusReferencesOther Resources