Dynamic remodeling of the actin cytoskeleton: lessons learned from Listeria locomotion.
The bacterial pathogen Listeria monocytogenes displays the remarkable ability to reorganize the actin cytoskeleton within host cells as a means for promoting cell-to-cell transfer of the pathogen, in a manner that evades humoral immunity. In a series of events commencing with the biosynthesis of the bacterial surface protein ActA, host cell actin and many actin-associated proteins self-assemble to form rocket-tail structures that continually grow at sites proximal to the bacterium and depolymerize distally. Widespread interest in the underlying molecular mechanism of Listeria locomotion stems from the likelihood that the dynamic remodeling of the host cell actin cytoskeleton at the cell's leading edge involves mechanistically analogous interactions. Recent advances in our understanding of these fundamental cytoskeletal rearrangements have been achieved through a clearer recognition of the central role of oligo-proline sequence repeats present in ActA, and these findings provide a basis for inferring the role of analogous host cell proteins in the force-producing and position-securing steps in pseudopod and lamellipod formation at the peripheral membrane.
Southwick
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FS
Department of Medicine, University of Florida College of Medicine, Gainesville 32610-0277.
Purich
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DL
D000199:Actins / Q000737:chemistry*; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry; D002465:Cell Movement; D003599:Cytoskeleton / Q000737:chemistry*; D008089:Listeria monocytogenes / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry; D008969:Molecular Sequence Data; D010587:Phagocytosis
D000199:Actins; D001426:Bacterial Proteins; D008565:Membrane Proteins; C072980:actA protein, Listeria monocytogenes