Abstract:
:Activation and invasion of the vascular endothelium by Staphylococcus aureus is a major cause of sepsis and endocarditis. For endothelial cell invasion, S. aureus triggers actin polymerization through Cdc42, N-WASp (also known as WASL) and the Arp2/3 complex to assemble a phagocytic cup-like structure. Here, we show that after stimulating actin polymerization staphylococci recruit Cdc42GAP (also known as ARHGAP1) which deactivates Cdc42 and terminates actin polymerization in the phagocytic cups. Cdc42GAP is delivered to the invading bacteria on recycling endocytic vesicles in concert with the exocyst complex. When Cdc42GAP recruitment by staphylococci was prevented by blocking recycling endocytic vesicles or the exocyst complex, or when Cdc42 was constitutively activated, phagocytic cup closure was impaired and endothelial cell invasion was inhibited. Thus, to complete invasion of the endothelium, staphylococci reorient recycling endocytic vesicles to recruit Cdc42GAP, which terminates Cdc42-induced actin polymerization in phagocytic cups. Analogous mechanisms might govern other Cdc42-dependent cell functions.
journal_name
J Cell Scijournal_title
Journal of cell scienceauthors
Rauch L,Hennings K,Trasak C,Röder A,Schröder B,Koch-Nolte F,Rivera-Molina F,Toomre D,Aepfelbacher Mdoi
10.1242/jcs.186213subject
Has Abstractpub_date
2016-08-01 00:00:00pages
2937-49issue
15eissn
0021-9533issn
1477-9137pii
jcs.186213journal_volume
129pub_type
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