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Protein complexes between PGRMC1 and actin-associated proteins are disrupted by AG-205

ABSTRACT: PGRMC1 is a protein from the MAPR family with a range of cellular functions. PGRMC1 has been described to play a role in regulating membrane trafficking and in cancer progression and response to therapies. To further understand the functions of PGRMC1 and the mechanism of the small molecule inhibitor of PGRMC1, AG-205, proteins differentially bound to PGRMC1 were identified following AG-205 treatment of MIA PaCa-2 cells.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Pancreas

SUBMITTER: Gereon Poschmann

LAB HEAD: Gereon Poschmann

PROVIDER: PXD016455 | Pride | 2020-01-24

REPOSITORIES: Pride

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Protein complexes including PGRMC1 and actin-associated proteins are disrupted by AG-205.

Teakel Sarah L SL Ludescher Marina M Thejer Bashar M BM Poschmann Gereon G Forwood Jade K JK Neubauer Hans H Cahill Michael A MA

Biochemical and biophysical research communications 20200121 1

PGRMC1 is a protein from the MAPR family with a range of cellular functions. PGRMC1 has been described to play a role in fertility, neuroprotection, steroidogenesis, membrane trafficking and in cancer cell biology. PGRMC1 represents a likely key regulator of cell metabolism and proliferation, as well as a potential target for anti-cancer therapies. To further understand the functions of PGRMC1 and the mechanism of the small molecule inhibitor of PGRMC1, AG-205, proteins differentially bound to P ...[more]

PMID: 31980178

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RNA sequencing of human endometrial epithelial and stromal cell lines treated with AG-205

Project description:Inappropriate response to progesterone or synthetic progestogens by the endometrial tissue may penalize the efficiency of treatments against endometriosis. The response pathways to progesterone involve its nuclear receptor but alternative mechanisms seem to play complementary roles. Recent studies have shown that Progesterone Receptor Membrane Component-1 (PGRMC1) can control various physiological or pathological processes in the breast and ovary. However, its functions in the human endometrium remain largely unknown. The small compound AG-205 is an alleged specific inhibitor of PGRMC1. Transcriptomes were obtained by RNA sequencing from cells of two endometrial cell lines (HEC-1A of epithelial origin and T-HESC of fibroblast origin) cultured in the presence or not of AG-205.

2021-10-27 | GSE174305 | GEO

Effects of PGRMC1 phosphorylation status on MIA PaCa-2 cells

Project description:Progesterone Receptor Membrane Component 1 (PGRMC1) is expressed in many cancer cells, where it is associated with detrimental patient outcomes. Multiple different functions and cellular locations have been attributed to PGRMC1 in a variety of contexts, however the mechanisms underlying PGRMC1 biology remain obscure. The protein contains several phosphorylated residues including tyrosines which were acquired early in animal evolution and could be involved with animal cell differentiation mechanisms. Here we demonstrate that mutagenic manipulation of PGRMC1phosphorylation status in MIA PaCa-2 (MP) pancreatic cells exerts broad pleiotropic effects, influencing cell plasticity and tumorigenicity, as assayed by cell biological and proteomics measurements. Relative to MP cells over-expressing hemagglutinin (HA)-tagged wild-type PGRMC1- HA (WT), cells expressing a PGRMC1-HA-S57A/S181A double mutant (DM) exhibited reduced levels of proteins involved in energy metabolism and mitochondrial function. This was associated with Rho-kinase inhibitor (ROCKI)-sensitive changes including altered cell shape, motility, increased PI3K/Akt and JNK activity, and fragmented mitochondrial morphology. An S57A/Y180F/S181A triple mutant (TM) reduced PI3K/Akt and JNK activation, indicating involvement of Y180. Both TM cells and Y180F single mutant cells exhibited attenuated mouse xenograft tumor growth. Tyrosine 180 phosphorylation status of PGRMC1 exerts dramatic influence over cancer cell biology.

2020-03-03 | PXD014716 | Pride

Effects of PGRMC1 phosphorylation on genome integrity and epigenetics

Project description:Progesterone receptor membrane component 1 (PGRMC1) is a protein that has been implicated in cancer biology and poor patient outcomes, which can be over-expressed in cancers, and exist in alternative states of phosphorylation.Here, we show that manipulation of PGRMC1 phosphorylation by mutagenesis results in altered cell metabolism. We examine the pathway by which nicotinamide-N-methyl transferase (NNMT) transfers a methyl group from S-adenosylmethionine (SAM) to produce 1-methylnicotinamide, lowering the levels of global methyl donor SAM. Hypothesizing that PGRMC1 phosphorylation status affects genome methylation, we discovered that each of several mutants elicited distinct patterns of CpG methylation.We conclude that PGRMC1 phosphorylation status, as controlled by unknown signaling processes, causes profound changes in cellular plasticity by affecting mechanisms also associated with early embryological tissue differentiation.

2019-12-01 | E-MTAB-8218 | biostudies-arrayexpress

LC-MSMS with isobaric tagging of Pgrmc1 KO mouse liver membranes expressing Flag-Pgrmc1 or Y113F Flag-Pgrmc1

Project description:Progesterone receptor membrane component 1 (PGRMC1) is a heme binding protein implicated in a wide range of cellular functions. Our previous studies showed that PGRMC1 binds to cytochromes P450 in yeast and mammalian cells and promotes activity of these enzymes. Recently, the paralog PGRMC2 was shown to function as an intracellular heme chaperone. Here, we examined the function of the Pgrmc1 Y113F mutant that is defective for heme iron coordination by measuring levels of membrane proteins in livers from Pgrmc1 knockout mice infected with AAV8 expressing either GFP, Flag-Pgrmc1, or Y113F Flag-Pgrmc1. These experiments (1) confirmed findings in uninfected wild-type and Pgrmc1 knockout mice and (2) revealed that Pgrmc1 Y113F functions to stabilize cytochrome P450 enzymes similar to wild-type Pgrmc1.

2022-02-16 | PXD028288 | Pride

LC-MSMS with isobaric tagging on Flag-coimmunoprecipitation eluates from Flag-Pgrmc1 and Y113F Flag-Pgrmc1 expressing Pgrmc1 KO mouse liver membranes

Project description:Progesterone receptor membrane component 1 (PGRMC1) is a heme binding protein implicated in a wide range of cellular functions. Our previous studies showed that PGRMC1 binds to cytochromes P450 in yeast and mammalian cells and promotes activity of these enzymes. Recently, the paralog PGRMC2 was shown to function as an intracellular heme chaperone. Here, we examined the function of the Pgrmc1 by identifying binding partners for wild-type Pgrmc1 and the Pgrmc1 Y113F mutant that is defective for heme iron coordination. Pgrmc1 knockout mice were infected with AAV8 expressing either GFP, Flag-Pgrmc1, or Y113F Flag-Pgrmc1, and Flag-Pgrmc1 was affinity purified using anti-Flag antibodies from extracts of liver membranes. These experiments (1) demonstrated that Pgrmc1 binds to different cytochrome P450 enzymes and (2) revealed that Pgrmc1 Y113F specifically fails to bind to ferrochelatase.

2022-02-15 | PXD028284 | Pride

Quantitative analysis of wild-type and Pgrmc1 knockout mouse liver transcriptomes

Project description:The goal of this study is to compare the next generation sequencing-derived liver transcriptome of Pgrmc1 KO mice to wild-type controls to identify differentially expressed genes.

2021-11-24 | GSE174375 | GEO

Compare total proteomics profile of PaCa-2 cells using 1D and 2D IDA LC and SWATH analysis

2020-03-03 | PXD014789 | Pride

siRNA knockdown of C1GALT1 in MIA PaCa-2 cells

Project description:To determine the C1GALT1 regulated gene expression profile in MIA PaCa-2 cells.

2017-12-04 | GSE90668 | GEO

RNA expression analysis after Mia PaCa 2 cell treatment with demethylating agent 5-Aza-2’-deoxycitidine (5-Aza)

Project description:Transcriptional profiling of Mia PaCa 2 cells treated with 5-Aza for 96 h. Relative abundance to untreated control cells was used to estimate the effect of DNA demethylation on the expression of the RNAs. Two-condition experiment, 5-Aza-treated vs. untretated Mia PaCa 2 cells. Biological replicates: 2. Technical replicates: 2.

2015-06-30 | E-GEOD-62959 | biostudies-arrayexpress

Human PDAC Cells: scramble Control vs. RINT shRNA downregulated

Project description:Time resolved transcriptional profiling of scramble and RINT1 down-regulated MIA PaCa-2 PDAC cells

2024-01-01 | GSE165629 | GEO