Jun 9, 2023 · To perform such secretory/trafficking function, MoRab7 first recruits the retromer complex to the vacuolar membrane, enabling recognition of a family of SNARE proteins, including MoSnc1.

We propose that the RAB7–retromer complex localizes to the interface between EEA1‐ and RAB5‐positive sorting endosomes and late endosomes/lysosomes, which reconciles the reported endosomal localization of retromer with the role of RAB7 on lysosomes and in endosome‐to‐lysosome fusion.

Jan 17, 2018 · Retromer is an endosomal multi-protein complex that organizes the endocytic recycling of a vast range of integral membrane proteins. Here, we establish an additional retromer function in controlling the activity and localization of the late endosomal small GTPase RAB7.

Mechanistically, retromer cooperates with the RAB7-specific GAP protein TBC1D5 to restrict RAB7 localization and activity to late endosomal microdomains, which enables amino acid sensing at the late endosome/lysosome to promote mTORC1 activity.

Jun 9, 2023 · Retromer, an ancient and highly conserved multimeric protein complex, is vital for regulating the retrieval and recycling of numerous cargoes away from the degradative pathway for delivery to the trans-Golgi network (TGN).

Sep 2, 2019 · Instead, retromer cooperates with the RAB7-GAP TBC1D5 to restrict late endosomal RAB7 into microdomains that are spatially separated from the amino acid-sensing domains. Upon loss of retromer, RAB7 expands into the ragulator-decorated amino acid-sensing domains and interferes with RAG-GTPase and mTORC1 recruitment.

Nov 3, 2008 · To analyze the interplay between PI3K and Rab7 in the regulation of retromer recruitment to membranes, we overexpressed a constitutively active GTP-locked form of Rab7 (GFP-Rab7–Q67L) and examined the effects of adding the PI3K inhibitor wortmannin.

Retromer is an endosomal multi‐protein complex that organizes the endocytic recycling of a vast range of integral membrane proteins. Here, we establish an additional retromer function in controlling the activity and localization of the late endosomal small GTP ase RAB 7.

Studies in yeast have shown that the membrane-associated SNX-BAR dimer of Vps5p-Vps17p can displace yeast Rab7 (Ypt7p) from the retromer CSC and thereby coordinate the cargo selection activity of the retromer CSC with tubule formation (Purushothaman et al., 2017).

Nov 20, 2017 · We propose that the RAB7–retromer complex localizes to the interface between EEA1‐ and RAB5‐positive sorting endosomes and late endosomes/lysosomes, which reconciles the reported endosomal localization of retromer with the role of RAB7 on lysosomes and in endosome‐to‐lysosome fusion.