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Tytuł pozycji:

Structural insights into Legionella RidL-Vps29 retromer subunit interaction reveal displacement of the regulator TBC1D5.

Tytuł:
Structural insights into Legionella RidL-Vps29 retromer subunit interaction reveal displacement of the regulator TBC1D5.
Autorzy:
Bärlocher K; Institute of Medical Microbiology, University of Zürich, Gloriastrasse 30, 8006, Zürich, Switzerland.
Hutter CAJ; Institute of Medical Microbiology, University of Zürich, Gloriastrasse 30, 8006, Zürich, Switzerland.
Swart AL; Institute of Medical Microbiology, University of Zürich, Gloriastrasse 30, 8006, Zürich, Switzerland.
Steiner B; Institute of Medical Microbiology, University of Zürich, Gloriastrasse 30, 8006, Zürich, Switzerland.
Welin A; Institute of Medical Microbiology, University of Zürich, Gloriastrasse 30, 8006, Zürich, Switzerland.
Hohl M; Institute of Medical Microbiology, University of Zürich, Gloriastrasse 30, 8006, Zürich, Switzerland.
Letourneur F; UMR5235, DIMNP, CNRS/Université Montpellier, Place Eugène Bataillon, Montpellier, 34095, cedex 5, France.
Seeger MA; Institute of Medical Microbiology, University of Zürich, Gloriastrasse 30, 8006, Zürich, Switzerland. .
Hilbi H; Institute of Medical Microbiology, University of Zürich, Gloriastrasse 30, 8006, Zürich, Switzerland. .
Źródło:
Nature communications [Nat Commun] 2017 Nov 16; Vol. 8 (1), pp. 1543. Date of Electronic Publication: 2017 Nov 16.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
Język:
English
Imprint Name(s):
Original Publication: [London] : Nature Pub. Group
MeSH Terms:
Bacterial Proteins/*metabolism
GTPase-Activating Proteins/*metabolism
Legionella pneumophila/*metabolism
Vesicular Transport Proteins/*metabolism
Animals ; Bacterial Proteins/chemistry ; Dictyostelium ; GTPase-Activating Proteins/chemistry ; HeLa Cells ; Humans ; Legionella pneumophila/physiology ; Mice ; Microscopy, Confocal ; Models, Molecular ; Protein Binding ; Protein Domains ; Protein Transport ; RAW 264.7 Cells ; Vacuoles/metabolism ; Vacuoles/microbiology ; Vesicular Transport Proteins/chemistry
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Substance Nomenclature:
0 (Bacterial Proteins)
0 (GTPase-Activating Proteins)
0 (TBC1D5 protein, human)
0 (VPS29 protein, human)
0 (Vesicular Transport Proteins)
Entry Date(s):
Date Created: 20171118 Date Completed: 20180924 Latest Revision: 20181116
Update Code:
20240105
PubMed Central ID:
PMC5691146
DOI:
10.1038/s41467-017-01512-5
PMID:
29146912
Czasopismo naukowe
Legionella pneumophila can cause Legionnaires' disease and replicates intracellularly in a distinct Legionella-containing vacuole (LCV). LCV formation is a complex process that involves a plethora of type IV-secreted effector proteins. The effector RidL binds the Vps29 retromer subunit, blocks retrograde vesicle trafficking, and promotes intracellular bacterial replication. Here, we reveal that the 29-kDa N-terminal domain of RidL (RidL 2-281 ) adopts a "foot-like" fold comprising a protruding β-hairpin at its "heel". The deletion of the β-hairpin, the exchange to Glu of Ile 170 in the β-hairpin, or Leu 152 in Vps29 abolishes the interaction in eukaryotic cells and in vitro. RidL 2-281 or RidL displace the Rab7 GTPase-activating protein (GAP) TBC1D5 from the retromer and LCVs, respectively, and TBC1D5 promotes the intracellular growth of L. pneumophila. Thus, the hydrophobic β-hairpin of RidL is critical for binding of the L. pneumophila effector to the Vps29 retromer subunit and displacement of the regulator TBC1D5.

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