SopD from Salmonella specifically inactivates Rab8

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SopD from Salmonella specifically inactivates Rab8. / Savitskiy, Sergey; Itzen, Aymelt.

In: BBA-PROTEINS PROTEOM, Vol. 1869, No. 8, 08.2021, p. 140661.

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@article{08d1164145cf4825967245daabdc11d7,
title = "SopD from Salmonella specifically inactivates Rab8",
abstract = "Salmonella outer protein D (SopD) is secreted into a host during the first stages of the Salmonella infection and contributes to the systemic virulence of the bacterium. SopD2 is a SopD homolog and possesses GTPase activating protein (GAP) activity towards Rab32. Here, we identified Rab-proteins as putative SopD-targets using a yeast two-hybrid approach. In vitro investigations subsequently revealed Rab8a as an exclusive SopD substrate in contrast to SopD2, which has a broader specificity targeting Rab29, Rab32 and Rab38 in vitro. Additionally, we determined the catalytic efficiencies of SopD and SopD2 towards their physiologically relevant substrates. Moreover, mutagenesis studies provided insights into possible key residues of the Rab-protein and the GAP involved in the conversion of active to inactive GTPase. In conclusion, we demonstrate that Salmonella SopD and SopD2 act as RabGAPs and can inactivate Rab signaling.",
author = "Sergey Savitskiy and Aymelt Itzen",
note = "Copyright {\textcopyright} 2021 Elsevier B.V. All rights reserved.",
year = "2021",
month = aug,
doi = "10.1016/j.bbapap.2021.140661",
language = "English",
volume = "1869",
pages = "140661",
journal = "BBA-PROTEINS PROTEOM",
issn = "1570-9639",
publisher = "ELSEVIER SCIENCE BV",
number = "8",

}

RIS

TY - JOUR

T1 - SopD from Salmonella specifically inactivates Rab8

AU - Savitskiy, Sergey

AU - Itzen, Aymelt

N1 - Copyright © 2021 Elsevier B.V. All rights reserved.

PY - 2021/8

Y1 - 2021/8

N2 - Salmonella outer protein D (SopD) is secreted into a host during the first stages of the Salmonella infection and contributes to the systemic virulence of the bacterium. SopD2 is a SopD homolog and possesses GTPase activating protein (GAP) activity towards Rab32. Here, we identified Rab-proteins as putative SopD-targets using a yeast two-hybrid approach. In vitro investigations subsequently revealed Rab8a as an exclusive SopD substrate in contrast to SopD2, which has a broader specificity targeting Rab29, Rab32 and Rab38 in vitro. Additionally, we determined the catalytic efficiencies of SopD and SopD2 towards their physiologically relevant substrates. Moreover, mutagenesis studies provided insights into possible key residues of the Rab-protein and the GAP involved in the conversion of active to inactive GTPase. In conclusion, we demonstrate that Salmonella SopD and SopD2 act as RabGAPs and can inactivate Rab signaling.

AB - Salmonella outer protein D (SopD) is secreted into a host during the first stages of the Salmonella infection and contributes to the systemic virulence of the bacterium. SopD2 is a SopD homolog and possesses GTPase activating protein (GAP) activity towards Rab32. Here, we identified Rab-proteins as putative SopD-targets using a yeast two-hybrid approach. In vitro investigations subsequently revealed Rab8a as an exclusive SopD substrate in contrast to SopD2, which has a broader specificity targeting Rab29, Rab32 and Rab38 in vitro. Additionally, we determined the catalytic efficiencies of SopD and SopD2 towards their physiologically relevant substrates. Moreover, mutagenesis studies provided insights into possible key residues of the Rab-protein and the GAP involved in the conversion of active to inactive GTPase. In conclusion, we demonstrate that Salmonella SopD and SopD2 act as RabGAPs and can inactivate Rab signaling.

U2 - 10.1016/j.bbapap.2021.140661

DO - 10.1016/j.bbapap.2021.140661

M3 - SCORING: Journal article

C2 - 33872771

VL - 1869

SP - 140661

JO - BBA-PROTEINS PROTEOM

JF - BBA-PROTEINS PROTEOM

SN - 1570-9639

IS - 8

ER -