Actin lessons from pathogens.
Salmonella typhimurium secretes proteins that co-opt the host actin cytoskeleton to induce membrane ruffling, leading to the uptake of the bacterium. New information about the biochemical activities of the Salmonella protein SipA suggests that this protein might inhibit host cell actin dynamics by competing with ADF/cofilin and gelsolin, two key proteins that promote the turnover of actin filaments.
Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720, USA.
Christophe
C
Le Clainche
David G
DG
Drubin
D051339:Actin Depolymerizing Factors; D000199:Actins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism*; D001665:Binding Sites; D051345:Destrin; D004789:Enzyme Activation; D018260:Gelsolin / Q000378:metabolism; D006801:Humans; D008840:Microfilament Proteins / Q000378:metabolism*; D012486:Salmonella typhimurium / Q000235:genetics / Q000378:metabolism / Q000472:pathogenicity*; D020741:rho GTP-Binding Proteins / Q000378:metabolism
D051339:Actin Depolymerizing Factors; D000199:Actins; D001426:Bacterial Proteins; C495824:DSTN protein, human; D051345:Destrin; D018260:Gelsolin; D008840:Microfilament Proteins; C118287:SipA protein, Salmonella; C103987:SopE protein, Salmonella; D020741:rho GTP-Binding Proteins