![]() |
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
| Created 2004 by CA Rinehart email CA Rinehart | Index CourseInfo LogIn Syllabus References Other Resources |