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Dynamic subcellular proteomics identifies novel regulators of adipocyte insulin action

ABSTRACT: Insulin acts on adipocytes to control whole-body glucose and lipid metabolism by increasing glucose uptake and inhibiting lipolysis. These processes are dependent on changes in protein localisation (e.g GLUT4 translocation to the plasma membrane (PM)). However, our knowledge of spatial proteomic changes in response to insulin is limited. Here, we use subcellular proteomics to map insulin-stimulated protein relocalisation at a cell-wide scale. Approximately 10% of proteins identified exhibited altered subcellular localisation in response to insulin. Since the PM was a major site of insulin-responsive proteome remodelling, we performed additional PM proteome profiling to quantify insulin-responsive changes at the cell surface. These orthologous proteomic approaches revealed insulin-stimulated redistribution of C3ORF18 to the PM. Studies in adipocytes depleted of C3ORF18 suggest this protein is required for maximal insulin signalling. Overall, our data provide an accessible resource of insulin-regulated changes in protein localisation and impetus for further work on how changes in protein localisation contribute to the cellular insulin response.

INSTRUMENT(S):

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): White Fat Cell

SUBMITTER: Olivia Conway

LAB HEAD: Daniel Fazakerley

PROVIDER: PXD061017 | Pride | 2026-02-06

REPOSITORIES: Pride

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Project description:Cyanobacteria are complex prokaryotes, incorporating a Gram-negative cell wall and internal thylakoid membranes (TM). However, localisation of proteins within cyanobacterial cells is poorly understood. Using subcellular fractionation and quantitative proteomics we report the first subcellular map of the proteome of an entire cyanobacterial (or any other prokaryotic) cell, identifying ~67% of Synechocystis sp. PCC 6803 proteins, ~1000 more than previous studies. 1,712 proteins were assigned to six specific subcellular regions. Proteins involved in energy generation localised to TMs. The majority of transporters, with the exception of the TM localised copper importer CtaA, resided in the plasma membrane (PM). Most metabolic enzymes are soluble although numerous pathways terminated in the TM (notably those involved in peptidoglycan monomer, NADP+, heme, lipid and carotenoid biosynthesis), or the PM (specifically those catalysing lipopolysaccharide, molybdopterin, flavin adenine dinucleotide and menaquinone biosynthesis). Furthermore, we identified the proteins involved in the TM and PM electron transport chains. The majority of ribosomal proteins and enzymes synthesising the storage compound polyhydroxybuyrate formed distinct clusters within the data suggesting that they have similar subcellular distributions to one another as one would expect for proteins operating within multi-component protein structures. Moreover, heterogeneity within membrane and cytoplasmic regions is observed, indicating further cellular complexity. Cyanobacterial TM protein localisation is conserved in Arabidopsis thaliana chloroplasts, suggesting similar proteome organisation in higher photosynthetic organisms. The organisation of a cyanobacterial cell revealed here will significantly aid our understanding of these environmentally and biotechnological important organisms. The successful application of this technique in Synechocystis suggests it could be applied to mapping the proteomes of other cyanobacteria and complex single-celled organisms.

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Dynamic subcellular proteomics identifies novel regulators of adipocyte insulin action

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