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Pex30-dependent membrane contacts sites maintain ER lipid homeostasis

ABSTRACT: In eukaryotic cells, communication between organelles and the coordination of their activities depend on membrane contact sites (MCS). How MCS are regulated under the dynamic cellular environment remains poorly understood. Here, we investigate how Pex30, a membrane protein localized to the endoplasmic reticulum (ER), regulates multiple MCS in budding yeast. We show that Pex30 is critical for the integrity of ER MCS with peroxisomes and vacuoles. This requires the Dysferlin domain (DysF) on Pex30 cytosolic tail. This domain binds to phosphatidic acid (PA) both in vitro and in silico, and it is important for normal PA metabolism in vivo. The DysF domain is evolutionarily conserved and may play a general role in PA homeostasis across eukaryotes. We further show that ER-Vacuole MCS requires Pex30 C-terminal Domain of Unknown Function and that its activity is controlled by phosphorylation in response to metabolic cues. These findings provide new insights into the dynamic nature of MCS and their coordination with cellular metabolism.

INSTRUMENT(S):

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Pedro Carvalho

LAB HEAD: Pedro Carvalho

PROVIDER: PXD056055 | Pride | 2025-05-08

REPOSITORIES: Pride

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			Action	DRS
	20210623_HF1_MaRa_SA_P0129_Pex28_log_01.raw	Raw
	20210623_HF1_MaRa_SA_P0129_Pex28_log_02.raw	Raw
	20210623_HF1_MaRa_SA_P0129_Pex28_log_03.raw	Raw
	20210623_HF1_MaRa_SA_P0129_Pex29_log_01.raw	Raw
	20210623_HF1_MaRa_SA_P0129_Pex29_log_02.raw	Raw

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