Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2019 Apr 1;30(8):1008–1019. doi: 10.1091/mbc.E18-09-0579

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© 2019 Chen, Wang, et al. “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology.

This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License.

PMC Copyright notice

FIGURE 8: — Model of Arl1-Imh1 acting on the Ypt6-independent endosome-to-TGN retrograde transport. (A) Under normal conditions, endosome-to-TGN retrograde transport is mainly mediated by the Ypt6-dependent GARP complex. (B) Dysfunction of YPT6 leads to a defective Golgi membrane environment, which impairs TGN localization of the GARP complex and endosome-to-TGN transport. (C) Overexpression of the N-terminal mutant Imh1 can stabilize active Arl1 at the TGN but cannot recruit the GARP complex to the TGN to promote proper targeting of endosome-derived vesicles. (D) We hypothesize that Imh1 might direct its function through indirect mechanisms, as the association of Imh1^dN100 with Vps53 is insufficient to restore GARP localization. Imh1 might recruit a protein X and either associate with the GARP complex through protein X or together with it contribute to restoring the defective membrane environment resulting from YPT6 deletion.