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Synechocystis sp. PCC 6803 proteome response to P-deficiency

ABSTRACT: Lipid droplets (LDs) are well integrated into multiple facets of cellular physiology and potentially represent an effective platform for the engineering of heterologous metabolic pathways. LDs of higher plant chloroplasts, known as plastoglobules (PGs), are critical mediators of stress tolerance through dynamic and reversible changes to morphology and molecular composition, however the dynamics and functional role(s) of cyanobacterial LDs are almost wholly unknown. Owing to their endosymbiotic origin as the progenitors of plant chloroplasts, we showed that cyanobacterial LDs designated as “cyanoglobule” share common characteristics with PGs, including molecular composition, structure, and their response under stress condition. We have monitored the dynamic accumulation of LDs, their protein, and lipid composition in response to phosphate deprivation. We are the first to describe cyanoglobule core proteome and lipidome in S6803 and their dynamics under P-deficiency. Our results showed that cyanoglobule share broadly similar protein and lipid compositions with plant plastoglobule, pointing to a central hub of cell lipid-protein metabolism and common role in stress adaptation, which then indicated their evolutionary relationship although specific differences may underscore an expansion of functions among higher plant PGs.

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ORGANISM(S): Synechocystis Sp. Pcc 6803

TISSUE(S): Photosynthetic Cell

SUBMITTER: Peter Lundquist

LAB HEAD: Peter K Lundquist

PROVIDER: PXD051903 | Pride | 2025-05-21

REPOSITORIES: Pride

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Project description:Progression and relapse-free survival of ovarian carcinoma are associated with the abundance of immunosuppressed CD163highCD206high tumor-associated macrophages (TAMs) and high levels of polyunsaturated fatty acids (PUFAs), in particular arachidonic acid (AA), in the tumor microenvironment. In the present study, we have investigated whether both associations are functionally linked. Methods: The effect of PUFAs on cytokine-mediated pro-inflammatory signal transduction was studied in primary monocyte-derived macrophages (MDMs) by transcriptomics, bioinformatics, phosphoprotein analysis of signal transduction proteins and MS-based proteomics of lipid rafts. Results: Pathway analysis of transcriptional profiles revealed that high CD163 and CD206/MRC1 expression in TAMs is strongly associated with an inhibition of cytokine-triggered signal transduction. This is mirrored by an impairment of the transcriptional response to interferon-beta (IFNbeta), IFNgamma and IL-6 in monocyte-derived macrophages (MDMs) by AA. This AA-mediated inhibition of pro-inflammatory signaling is caused by dysfunctions of the cognate receptors, as indicated by the inhibition by PUFAs of JAK1, JAK2, STAT1 and STAT3 phosphorylation, with the strongest inhibitory effects exerted by AA and its non-metabolizable analog ETYA. AA/ETYA treatment of MDMs results in altered composition of lipid rafts, including reduced amounts of the interferon receptor IFNAR1, STAT1 and other immune-regulatory proteins. The AA-mediated inhibition of IFN-triggered STAT1 phosphorylation was reversed by water-soluble cholesterol, known to prevent the perturbation of lipid raft structure by PUFAs. Conclusion: Our data suggest that AA, and to a lesser degree other PUFAs, impair pro-inflammatory signaling in macrophages, at least in part by altering the structure of lipid rafts, and thereby contribute to the reeducation of tumor-associated macrophages. Our findings also suggest that the pharmacologic restoration of lipid raft functions in TAM may be a promising strategy for the development of new therapeutic approaches.

			Action	DRS
	FileList_20210914.xlsx	Xlsx
	MaxQuant_1.6.15.0.zip	Other
	MaxQuant_Output.zip	Other
	UP000001425_1111708.fasta	Fasta
	hf2021102702.raw	Raw

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Synechocystis sp. PCC 6803 proteome response to P-deficiency

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