The regulation of actin polymerization and cross-linking in Dictyostelium.
It is clear that the polymerization and organization of actin filament networks plays a critical role in numerous cellular processes. Inhibition of actin polymerization by pharmacological agents will completely prevent chemotactic motility, macropinocytosis, endocytosis, and phagocytosis. Recently there has been great progress in understanding the mechanisms that control the assembly and structure of the actin cytoskeleton. Members of the Rho family of GTPases have been identified as major players in the signal transduction pathway leading from a cell surface signal to actin polymerization. The Arp2/3 complex has been added to the list of means by which new actin filaments can be nucleated. However, it is clear that actin polymerization by Arp2/3 complex is not the whole story. In principle, the final structures formed by actin filaments will depend on factors such as: the length of actin filaments, the degree of branching, how they are cross-linked and the tensions imparted on them. In addition, the means by which actin polymerization generates protrusion of membranes is still controversial. A phagosome, filopodium and a lamellipodium all require polymerization of new actin filaments, but each has a characteristic morphology and cytoskeletal structure. In the following chapter, we will discuss actin polymerization and filament organization, especially as it relates to the machinery of phagocytosis in Dictyostelium.
Department of Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269, USA.
E
E
Lee
K
K
Pang
D
D
Knecht
D008841:Actin Cytoskeleton / Q000737:chemistry; D000199:Actins / Q000737:chemistry*; D000818:Animals; D003599:Cytoskeleton / Q000737:chemistry; D004023:Dictyostelium / Q000737:chemistry / Q000502:physiology*; D010587:Phagocytosis; D011108:Polymers / Q000737:chemistry; D015398:Signal Transduction
D000199:Actins; D011108:Polymers