The HOPS tethering complex is required to maintain signaling endosome identity and TORC1 activity

Autor(en): Gao, Jieqiong
Nicastro, Raffaele
Peli-Gulli, Marie-Pierre
Grziwa, Sophie
Chen, Zilei
Kurre, Rainer 
Piehler, Jacob 
De Virgilio, Claudio
Froehlich, Florian 
Ungermann, Christian 
Stichwörter: BINDING; Cell Biology; COMPARTMENTS; CORVET COMPLEX; FUSION; MEMBRANE; PHOSPHOINOSITIDES; RAB GTPASES; TRANSPORT; VPS PROTEIN COMPLEX; YEAST SACCHAROMYCES-CEREVISIAE
Erscheinungsdatum: 2022
Herausgeber: ROCKEFELLER UNIV PRESS
Enthalten in: JOURNAL OF CELL BIOLOGY
Band: 221
Ausgabe: 5
Zusammenfassung: 
The endomembrane system of eukaryotic cells is essential for cellular homeostasis during growth and proliferation. Previous work showed that a central regulator of growth, namely the target of rapamycin complex 1 (TORC1), binds both membranes of vacuoles and signaling endosomes (SEs) that are distinct from multivesicular bodies (MVBs). Interestingly, the endosomal TORC1, which binds membranes in part via the EGO complex, critically defines vacuole integrity. Here, we demonstrate that SEs form at a branch point of the biosynthetic and endocytic pathways toward the vacuole and depend on MVB biogenesis. Importantly, function of the HOPS tethering complex is essential to maintain the identity of SEs and proper endosomal and vacuolar TORC1 activities. In HOPS mutants, the EGO complex redistributed to the Golgi, which resulted in a partial mislocalization of TORC1. Our study uncovers that SE function requires a functional HOPS complex and MVBs, suggesting a tight link between trafficking and signaling along the endolysosomal pathway.
ISSN: 0021-9525
DOI: 10.1083/jcb.202109084

Show full item record

Page view(s)

4
Last Week
0
Last month
0
checked on Jun 19, 2024

Google ScholarTM

Check

Altmetric