Dataset Information

Multi-omics studies reveal how ambient temperatures govern Chlamydomonas’ cellular responses

ABSTRACT: Understanding microalgal responses to subtle temperature changes is critical, as they are primary producers that drive ecosystem productivity and food web dynamics. Even small shifts may alter algal fitness and reshape interactions with other microbes. In this study, C. reinhardtii was grown at non-stress, ambient temperatures of 18 °C and 28 °C. Proteomic analysis of isolated cilia and secreted proteins identified major changes in abundance within these sub-proteomes, particularly intraflagellar transport (IFT) complexes in cilia and mating-related proteins in the secretome that are both upregulated at higher temperature.

INSTRUMENT(S):

ORGANISM(S): Chlamydomonas Reinhardtii

TISSUE(S): Cell Culture

SUBMITTER: PRATEEK SHETTY

LAB HEAD: Prof. Dr. Maria Mittag

PROVIDER: PXD067459 | Pride | 2026-05-19

REPOSITORIES: Pride

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Source:

			Action	DRS
	FlagellarProteome_18_Rep1.raw	Raw
	FlagellarProteome_18_Rep2.raw	Raw
	FlagellarProteome_18_Rep3.raw	Raw
	FlagellarProteome_18_Rep4.raw	Raw
	FlagellarProteome_28_Rep1.raw	Raw

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Project description:Organelle fragmentation is crucial for the onset of autophagic programs that control lysosomal clearance of portions of organelles to be removed from cells. It is driven by membrane-bound organello-phagy receptors that display cytoplasmic intrinsically disordered modules (IDRs) containing short LC3-interacting regions (LIRs). Studies on ER-phagy receptors of the FAM134 family revealed the importance of transcriptional induction, and receptors phosphorylation, ubiquitylation and clustering for execution of the ER-phagy programs. In this model, ER fragmentation is promoted by the membrane-remodeling function of FAM134 reticulon homology domains (RHDs)18,19. However, RHDs are not conserved in ER-phagy receptors, nor in receptors for autophagy of other organelles that also require fragmentation such as the mitochondria. Thus, membrane remodeling by RHDs is unlikely to be a conserved mechanism to regulate organelle turnover. Here, we show that the membrane-tethering modules of ER-phagy receptors (RHDs for FAM134B, single/multi spanning transmembrane domains for TEX264 and SEC62) determine the sub-compartmental distribution of the receptors but are dispensable for ER fragmentation, regardless of their propensity to remodel the ER membrane. Our experiments reveal that the information encoding for ER fragmentation is contained in the cytoplasmic IDR modules of the ER-phagy receptors, which also control delivery of the ER fragments within degradative acidic compartments upon engagements of lipidated LC3/GABARAP proteins via their LIRs. Notably, the transplantation of ER-phagy receptors IDRs at the mitochondrial membrane induces DRP1-driven mitochondrial fragmentation and mitophagy, and the transplantation of mitophagy receptors IDRs at the ER membrane induces ER fragmentation and ER-phagy. Our work reveals the functional conservation of membrane-exposed IDRs in promoting organelle fragmentation and offers a method to control integrity and activity of intracellular organelles by surface activation of IDR modules with net negative charges.

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Multi-omics studies reveal how ambient temperatures govern Chlamydomonas’ cellular responses

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