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Staphylococcus aureus recruits Cdc42GAP through recycling endosomes and the exocyst to invade human endothelial cells

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Staphylococcus aureus recruits Cdc42GAP through recycling endosomes and the exocyst to invade human endothelial cells. / Rauch, Liane; Hennings, Kirsten; Trasak, Claudia; Röder, Anja; Schröder, Barbara; Nolte, Friedrich; Rivera-Molina, Felix; Toomre, Derek; Aepfelbacher, Martin.

in: J CELL SCI, Jahrgang 129, Nr. 15, 01.08.2016, S. 2937-49.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Rauch, L, Hennings, K, Trasak, C, Röder, A, Schröder, B, Nolte, F, Rivera-Molina, F, Toomre, D & Aepfelbacher, M 2016, 'Staphylococcus aureus recruits Cdc42GAP through recycling endosomes and the exocyst to invade human endothelial cells', J CELL SCI, Jg. 129, Nr. 15, S. 2937-49. https://doi.org/10.1242/jcs.186213

APA

Rauch, L., Hennings, K., Trasak, C., Röder, A., Schröder, B., Nolte, F., Rivera-Molina, F., Toomre, D., & Aepfelbacher, M. (2016). Staphylococcus aureus recruits Cdc42GAP through recycling endosomes and the exocyst to invade human endothelial cells. J CELL SCI, 129(15), 2937-49. https://doi.org/10.1242/jcs.186213

Vancouver

Rauch L, Hennings K, Trasak C, Röder A, Schröder B, Nolte F et al. Staphylococcus aureus recruits Cdc42GAP through recycling endosomes and the exocyst to invade human endothelial cells. J CELL SCI. 2016 Aug 1;129(15):2937-49. https://doi.org/10.1242/jcs.186213

Bibtex

@article{c63c417ae6f0421fa00f3b787072da80,
title = "Staphylococcus aureus recruits Cdc42GAP through recycling endosomes and the exocyst to invade human endothelial cells",
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.",
keywords = "Journal Article",
author = "Liane Rauch and Kirsten Hennings and Claudia Trasak and Anja R{\"o}der and Barbara Schr{\"o}der and Friedrich Nolte and Felix Rivera-Molina and Derek Toomre and Martin Aepfelbacher",
note = "{\textcopyright} 2016. Published by The Company of Biologists Ltd.",
year = "2016",
month = aug,
day = "1",
doi = "10.1242/jcs.186213",
language = "English",
volume = "129",
pages = "2937--49",
journal = "J CELL SCI",
issn = "0021-9533",
publisher = "Company of Biologists Ltd",
number = "15",

}

RIS

TY - JOUR

T1 - Staphylococcus aureus recruits Cdc42GAP through recycling endosomes and the exocyst to invade human endothelial cells

AU - Rauch, Liane

AU - Hennings, Kirsten

AU - Trasak, Claudia

AU - Röder, Anja

AU - Schröder, Barbara

AU - Nolte, Friedrich

AU - Rivera-Molina, Felix

AU - Toomre, Derek

AU - Aepfelbacher, Martin

N1 - © 2016. Published by The Company of Biologists Ltd.

PY - 2016/8/1

Y1 - 2016/8/1

N2 - 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.

AB - 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.

KW - Journal Article

U2 - 10.1242/jcs.186213

DO - 10.1242/jcs.186213

M3 - SCORING: Journal article

C2 - 27311480

VL - 129

SP - 2937

EP - 2949

JO - J CELL SCI

JF - J CELL SCI

SN - 0021-9533

IS - 15

ER -