Ume6 Coordinates Lysosomal Remodeling and Autophagy Through Transcriptional Repression in S. cerevisiae
Abstract
Lysosome function and autophagy are highly regulated processes that must be coordinated to enable cellular adaptation to stress. However, the transcriptional mechanisms linking these pathways remain incompletely understood. Here, we identify Ume6 as a transcriptional repressor that regulates vacuolar protein composition and autophagy in Saccharomyces cerevisiae (budding yeast). Dysregulation of Ume6 alters vacuolar protein composition through two distinct mechanisms: increased abundance of multiple vacuolar components and enhanced degradation of selected vacuolar membrane proteins by elevated expression of the vacuolar E3 ubiquitin ligases. UME6 deletion also increases autophagic activity, whereas UME6 overexpression delays autophagy induction. Furthermore, we find that Ume6 coordinates with another transcriptional repressor, Rph1, and its regulatory activity is regulated by multiple protein kinases, including Rim15, Rim11, and Mck1. Together, our study reveal a broad transcriptional regulatory mechanism through which Ume6 coordinates vacuolar protein composition and autophagy, providing new insights into the regulation of lysosome-related functions in response to cellular stress.
Related
- Dynamic TET1 repression coordinates activation of macroH2A.2-poised bivalent genes during neuroectoderm differentiation
- Transcriptional control of higher alcohol formation in Saccharomyces cerevisiae: a systems framework linking nutrient sensing, precursor allocation, Ehrlich output, and stress adaptation
- A GacS-mediated regulatory framework coordinates bacterial competition and rhizosphere microbiome remodeling in Pseudomonas fluorescens
- OPA1-dependent mitochondrial remodeling coordinates TCR signaling and metabolic adaptation during iNKT cell differentiation
- SIM2s coordinates programmed mitophagy with respiratory chain supercomplex remodeling during mammary epithelial differentiation
BibTeX
@misc{evans2026ume6,
title = {{Ume6 Coordinates Lysosomal Remodeling and Autophagy Through Transcriptional Repression in S. cerevisiae}},
author = {Olivia Evans and Alexis Hoy and Isabel Woo and Xi Yang},
howpublished = {bioRxiv},
year = {2026},
month = oct,
doi = {10.64898/2026.10.29.762757},
url = {https://www.biorxiv.org/content/10.64898/2026.10.29.762757v1},
note = {CC BY},
}
RIS
TY - UNPB
TI - Ume6 Coordinates Lysosomal Remodeling and Autophagy Through Transcriptional Repression in S. cerevisiae
AU - Olivia Evans
AU - Alexis Hoy
AU - Isabel Woo
AU - Xi Yang
PY - 2026
DA - 2026/10/29
PB - bioRxiv
DO - 10.64898/2026.10.29.762757
UR - https://www.biorxiv.org/content/10.64898/2026.10.29.762757v1
AB - Lysosome function and autophagy are highly regulated processes that must be coordinated to enable cellular adaptation to stress. However, the transcriptional mechanisms linking these pathways remain incompletely understood. Here, we identify Ume6 as a transcriptional repressor that regulates vacuolar protein composition and autophagy in Saccharomyces cerevisiae (budding yeast). Dysregulation of Ume6 alters vacuolar protein composition through two distinct mechanisms: increased abundance of multiple vacuolar components and enhanced degradation of selected vacuolar membrane proteins by elevated expression of the vacuolar E3 ubiquitin ligases. UME6 deletion also increases autophagic activity, whereas UME6 overexpression delays autophagy induction. Furthermore, we find that Ume6 coordinates with another transcriptional repressor, Rph1, and its regulatory activity is regulated by multiple protein kinases, including Rim15, Rim11, and Mck1. Together, our study reveal a broad transcriptional regulatory mechanism through which Ume6 coordinates vacuolar protein composition and autophagy, providing new insights into the regulation of lysosome-related functions in response to cellular stress.
SN - 2692-8205
ER -