(Q48559464)

12 February 2018

title

Direct modulation of the host cell cytoskeleton by Salmonella actin-binding proteins. (English)

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12 February 2018

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1

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12 February 2018

Vassilis Koronakis

series ordinal

2

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12 February 2018

publication date

1 January 2002

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12 February 2018

published in

Trends in Cell Biology

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12 February 2018

volume

12

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12 February 2018

issue

1

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12 February 2018

page(s)

15-20

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12 February 2018

Intracellular pathogens and the actin cytoskeleton

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Direct nucleation and bundling of actin by the SipC protein of invasive Salmonella

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Role of the S. typhimurium actin-binding protein SipA in bacterial internalization.

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Cooperation between actin-binding proteins of invasive Salmonella: SipA potentiates SipC nucleation and bundling of actin

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S. typhimurium encodes an activator of Rho GTPases that induces membrane ruffling and nuclear responses in host cells.

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A Salmonella inositol polyphosphatase acts in conjunction with other bacterial effectors to promote host cell actin cytoskeleton rearrangements and bacterial internalization

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Salmonella strikes a balance.

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The Salmonella type III secretion translocon protein SspC is inserted into the epithelial cell plasma membrane upon infection.

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The Salmonella typhimurium tyrosine phosphatase SptP is translocated into host cells and disrupts the actin cytoskeleton

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An invasion-associated Salmonella protein modulates the actin-bundling activity of plastin

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Abp1p and cortactin, new "hand-holds" for actin

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Cytoskeleton: actin and endocytosis--no longer the weakest link

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IpaC induces actin polymerization and filopodia formation during Shigella entry into epithelial cells

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Enteropathogenic E. coli Tir binds Nck to initiate actin pedestal formation in host cells

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Enteropathogenic E. coli translocated intimin receptor, Tir, interacts directly with alpha-actinin

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Identifiers

DOI

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12 February 2018

1 reference

12 February 2018