An invasion-associated Salmonella protein modulates the actin-bundling activity of plastin
AUTOR(ES)
Zhou, Daoguo
FONTE
The National Academy of Sciences
RESUMO
The entry of Salmonella typhimurium into nonphagocytic cells requires a panel of bacterial effector proteins that are delivered to the host cell via a type III secretion system. These proteins modulate host–cell signal-transduction pathways and the actin cytoskeleton to induce membrane ruffling and bacterial internalization. One of these bacterial effectors, termed SipA, is an actin-binding protein that is required for efficient Salmonella entry into host cells. We report here that SipA forms a complex with T-plastin on bacterial infection. Formation of such a complex, which requires the presence of F-actin, results in a marked increase in the actin-bundling activity of T-plastin. We also report that T-plastin is recruited to S. typhimurium-induced membrane ruffles by a CDC42-dependent signaling process and is required for bacterial entry. We propose that modulation of the actin-bundling activity of T-plastin by SipA results in the stabilization of the actin filaments at the point of bacterial–host cell contact, which leads to more efficient Salmonella internalization.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=17862Documentos Relacionados
- A role for the actin-bundling protein l-plastin in the regulation of leukocyte integrin function
- Fascin, an echinoid actin-bundling protein, is a homolog of the Drosophila singed gene product.
- Bromophenacyl bromide binding to the actin-bundling protein l-plastin inhibits inositol trisphosphate-independent increase in Ca2+ in human neutrophils.
- Fascin, an Actin-bundling Protein, Induces Membrane Protrusions and Increases Cell Motility of Epithelial Cells
- Calcium-Calmodulin Suppresses the Filamentous Actin-Binding Activity of a 135-Kilodalton Actin-Bundling Protein Isolated from Lily Pollen Tubes