-
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
-
References:
-
Nat Microbiol. 2016 Dec 12;2:16236. (PMID: 27941800)
Cell Host Microbe. 2011 Aug 18;10(2):89-91. (PMID: 21843863)
Cell Microbiol. 2014 Jan;16(1):15-26. (PMID: 24168696)
J Cell Biol. 1998 Aug 10;142(3):665-81. (PMID: 9700157)
Acta Crystallogr D Biol Crystallogr. 2010 Apr;66(Pt 4):486-501. (PMID: 20383002)
Mol Biol Cell. 2005 Nov;16(11):5294-303. (PMID: 16120649)
Cell Microbiol. 2015 Jul;17(7):935-50. (PMID: 25903720)
Clin Microbiol Rev. 2010 Apr;23(2):274-98. (PMID: 20375353)
PLoS Pathog. 2015 Dec 03;11(12):e1005307. (PMID: 26633832)
EMBO Rep. 2017 Oct;18(10 ):1817-1836. (PMID: 28835546)
Cell Host Microbe. 2013 Sep 11;14 (3):256-68. (PMID: 24034612)
J Appl Crystallogr. 2007 Aug 1;40(Pt 4):658-674. (PMID: 19461840)
J Biol Chem. 2009 Feb 20;284(8):4846-56. (PMID: 19095644)
Curr Opin Cell Biol. 2008 Aug;20(4):427-36. (PMID: 18472259)
Proc Natl Acad Sci U S A. 2012 Aug 21;109 (34):13567-72. (PMID: 22872863)
Traffic. 2015 Jan;16(1):68-84. (PMID: 25367362)
Biochemistry. 2011 Apr 19;50(15):3272-8. (PMID: 21410291)
PLoS Pathog. 2006 May;2(5):e46. (PMID: 16710455)
Acta Crystallogr D Biol Crystallogr. 2010 Apr;66(Pt 4):479-85. (PMID: 20383001)
Structure. 2011 Dec 7;19(12):1744-51. (PMID: 22153497)
EMBO Rep. 2014 Apr;15(4):392-401. (PMID: 24603492)
J Immunol Methods. 2015 Dec;427:73-84. (PMID: 26476130)
Nucleic Acids Res. 2014 Jul;42(Web Server issue):W252-8. (PMID: 24782522)
Traffic. 2014 May;15(5):471-87. (PMID: 24499450)
Annu Rev Cell Dev Biol. 2010;26:261-83. (PMID: 20929312)
Environ Microbiol Rep. 2011 Jun;3(3):286-96. (PMID: 23761274)
Methods Mol Biol. 2013;954:309-21. (PMID: 23150404)
Cell. 2016 Dec 1;167(6):1623-1635.e14. (PMID: 27889239)
Nat Cell Biol. 2011 Dec 22;14(1):29-37. (PMID: 22193161)
J Cell Sci. 2012 Oct 15;125(Pt 20):4693-702. (PMID: 23148298)
Nat Rev Mol Cell Biol. 2006 Aug;7(8):568-79. (PMID: 16936697)
Cell Microbiol. 2008 Dec;10(12):2416-33. (PMID: 18673369)
Traffic. 2012 Sep;13(9):1187-97. (PMID: 22340894)
Cell Microbiol. 2014 Jul;16(7):1034-52. (PMID: 24373249)
J Cell Biol. 2008 Nov 3;183(3):513-26. (PMID: 18981234)
Cell Host Microbe. 2013 Jul 17;14(1):38-50. (PMID: 23870312)
PLoS Pathog. 2013 Sep;9(9):e1003598. (PMID: 24068924)
FEBS Lett. 2015 Sep 14;589(19 Pt A):2620-6. (PMID: 26072290)
Curr Top Microbiol Immunol. 2013;376:155-73. (PMID: 23918172)
Cell Microbiol. 2007 Dec;9(12):2903-20. (PMID: 17614967)
Infect Immun. 2000 Sep;68(9):5154-66. (PMID: 10948139)
Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):213-21. (PMID: 20124702)
Mol Cell Proteomics. 2017 Apr;16(4):622-641. (PMID: 28183814)
Annu Rev Cell Dev Biol. 2014;30:79-109. (PMID: 25103867)
J Cell Sci. 2009 Jul 15;122(Pt 14):2371-82. (PMID: 19531583)
J Mol Biol. 2016 Feb 22;428(4):720-725. (PMID: 26410586)
MBio. 2014 Jan 28;5(1):e00839-13. (PMID: 24473127)
Nucleic Acids Res. 2010 Jul;38(Web Server issue):W545-9. (PMID: 20457744)
Curr Opin Microbiol. 2016 Feb;29:22-9. (PMID: 26529574)
Curr Protoc Cell Biol. 2010 Mar;Chapter 3:Unit 3.34. (PMID: 20235103)
Trends Microbiol. 2016 Jun;24(6):450-62. (PMID: 26924068)
Cell Microbiol. 2009 Mar;11(3):442-60. (PMID: 19021631)
J Cell Sci. 2010 Nov 1;123(Pt 21):3703-17. (PMID: 20923837)
Methods Enzymol. 2000;326:430-40. (PMID: 11036656)
Nat Commun. 2016 Nov 09;7:13305. (PMID: 27827364)
Gene. 1995 Aug 30;162(1):129-34. (PMID: 7557400)
Cell. 2008 Dec 26;135(7):1175-87. (PMID: 19109890)
J Biol Chem. 2014 Dec 5;289(49):34175-88. (PMID: 25339170)
Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):125-32. (PMID: 20124692)
Dev Cell. 2009 Jul;17 (1):110-22. (PMID: 19619496)
Nature. 2007 Oct 25;449(7165):1063-7. (PMID: 17891154)
Traffic. 2009 Jan;10(1):76-87. (PMID: 18980612)
-
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
-
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.