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 Detalle_Publicacion

Molecular mechanism for the subversion of the retromer coat by the Legionella effector RidL

Abstract: Microbial pathogens employ sophisticated virulence strategies to cause infections in humans. The intracellular pathogen Legionella pneumophila encodes RidL to hijack the host scaffold protein VPS29, a component of retromer and retriever complexes critical for endosomal cargo recycling. Here, we determined the crystal structure of L. pneumophila RidL in complex with the human VPS29?VPS35 retromer subcomplex. A hairpin loop protruding from RidL inserts into a conserved pocket on VPS29 that is also used by cellular ligands, such as Tre-2/Bub2/Cdc16 domain family member 5 (TBC1D5) and VPS9-ankyrin repeat protein for VPS29 binding. Consistent with the idea of molecular mimicry in protein interactions, RidL outcompeted TBC1D5 for binding to VPS29. Furthermore, the interaction of RidL with retromer did not interfere with retromer dimerization but was essential for association of RidL with retromer-coated vacuolar and tubular endosomes. Our work thus provides structural and mechanistic evidence into how RidL is targeted to endosomal membranes.

 Fuente: Proc Natl Acad Sci U S A. 2017 Dec 26;114(52):E11151-E11160.

Editorial: National Academy of Sciences

 Año de publicación: 2017

Nº de páginas: 10

Tipo de publicación: Artículo de Revista

 DOI: 10.1073/pnas.1715361115

ISSN: 0027-8424,1091-6490

Proyecto español: BFU2014-59759-R

Url de la publicación: www.pnas.org/cgi/doi/10.1073/pnas.1715361115

Autores/as

ROMANO-MORENO, MIGUEL

ROJAS, ADRIANA L.

WILLIAMSON, CHAD D.

GERSHLICK, DAVID C.

ISUPOV, MICHAIL N.

BONIFACINO, JUAN S.

MACHNER, MATTHIAS P.

HIERRO, AITOR