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The P4‐ATPase Drs2 interacts with and stabilizes the multisubunit tethering complex TRAPPIII in yeast

Multisubunit Tethering Complexes (MTCs) are a set of conserved protein complexes that tether vesicles at the acceptor membrane. Interactions with other components of the trafficking machinery regulate MTCs through mechanisms that are partially understood. Here, we systematically investigate the inte...

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Detalles Bibliográficos
Autores principales: Pazos, Irene, Puig‐Tintó, Marta, Betancur, Laura, Cordero, Jorge, Jiménez‐Menéndez, Nereida, Abella, Marc, Hernández, Altair C, Duran, Ana G, Adachi‐Fernández, Emi, Belmonte‐Mateos, Carla, Sabido‐Bozo, Susana, Tosi, Sébastien, Nezu, Akiko, Oliva, Baldomero, Colombelli, Julien, Graham, Todd R, Yoshimori, Tamotsu, Muñiz, Manuel, Hamasaki, Maho, Gallego, Oriol
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10157312/
https://www.ncbi.nlm.nih.gov/pubmed/36929574
http://dx.doi.org/10.15252/embr.202256134
Descripción
Sumario:Multisubunit Tethering Complexes (MTCs) are a set of conserved protein complexes that tether vesicles at the acceptor membrane. Interactions with other components of the trafficking machinery regulate MTCs through mechanisms that are partially understood. Here, we systematically investigate the interactome that regulates MTCs. We report that P4‐ATPases, a family of lipid flippases, interact with MTCs that participate in the anterograde and retrograde transport at the Golgi, such as TRAPPIII. We use the P4‐ATPase Drs2 as a paradigm to investigate the mechanism and biological relevance of this interplay during transport of Atg9 vesicles. Binding of Trs85, the sole‐specific subunit of TRAPPIII, to the N‐terminal tail of Drs2 stabilizes TRAPPIII on membranes loaded with Atg9 and is required for Atg9 delivery during selective autophagy, a role that is independent of P4‐ATPase canonical functions. This mechanism requires a conserved I(S/R)TTK motif that also mediates the interaction of the P4‐ATPases Dnf1 and Dnf2 with MTCs, suggesting a broader role of P4‐ATPases in MTC regulation.