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Interaction proteins of cGAS and PSMA4 with lactate treatment

ABSTRACT: Sample 1: Control Sample 2: Interaction proteins of Flag-cGAS Sample 3: Interaction proteins of Flag-cGAS with lactate treatment Sample 4: Interaction proteins of Flag-PSMA4 Sample 5: Interaction proteins of Flag-PSMA4 with lactate treatment

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture, Colon Epithelial Cell

DISEASE(S): Colon Cancer

SUBMITTER: Ke Zheng

LAB HEAD: Jing He

PROVIDER: PXD053886 | Pride | 2025-03-21

REPOSITORIES: Pride

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			Action	DRS
	HFX_20240605-1_F1_R1.raw	Raw
	HFX_20240605-1_F1_R1.txt	Txt
	HFX_20240605-2_F1_R1.raw	Raw
	HFX_20240605-2_F1_R1.txt	Txt
	HFX_20240605-3_F1_R1.raw	Raw

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1 - 5 of 11

Publications

Lactylation orchestrates ubiquitin-independent degradation of cGAS and promotes tumor growth.

Rao Keqiang K Zhang Xinchao X Luo Yi Y Xia Qiang Q Jin Yuting Y He Jing J

Cell reports 20250318 4

Lactate extensively associates with metabolic reprogramming, signal transduction, and immune modulation. Nevertheless, the regulatory role of lactate in immune sensing of cytosolic DNA remains uncertain. Here, we report that lactate serves as an initiator to facilitate proteasomal degradation of cyclic GMP-AMP synthase (cGAS) independent of ubiquitin, thus repressing the production of interferon and contributing to tumor growth. Mechanistically, lactylation of K21 stimulates cGAS translocation f ...[more]

PMID: 40106438

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cGAS Senses Translation Stress Through Direct Binding to Ribosomes

Project description:The cGAS-STING pathway, a central component of the innate immune system, senses cytosolic DNA and induces interferon-stimulated genes (ISGs) to mediate inflammation. Here we report the unexpected discovery that cGAS senses dysfunctional protein production. Purified ribosomes interact with and stimulate the catalytic activity of recombinant cGAS in vitro. Disruption of the ribosome-associated protein quality control pathway, which detects and resolves ribosome collisions, results in cGAS- and STING-dependent ISG expression, and causes the re-localization of cGAS from the nucleus to the cytosol. Indeed, cGAS preferentially binds collided ribosomes in vitro, and other orthogonal perturbations that lead to elevated levels of collided ribosomes cause re-localization of cGAS as well. Thus, the cGAS-STING pathway senses and responds to translation stress. These findings have implications for the inflammatory responses to viral infection and tumorigenesis, both of which substantially reprogram cellular protein synthesis.

2021-09-09 | PXD019359 | Pride

Identification of cGAS acetylation and phosphorylation

Project description:DNA derived from the genetic material of pathogens or from cellular DNA damage provides a molecular pattern that can be sensed by pattern-recognition receptors of the mammalian innate immune system. In recent years, the cyclic GMP-AMP synthase (cGAS) protein has been characterized as a primary cytosolic DNA sensor during infection with bacteria, DNA viruses, or retroviruses. While the role of cGAS in downstream immune signaling through STING-TBK1-IRF3 proteins is well-defined, regulatory mechanisms of cGAS activity, such as through post-translational modifications (PTMs), are still an active area of research. Here, we report a comprehensive characterization of cGAS phosphorylations and acetylations in three different cell types. Data-dependent proteomic analyses of immunoaffinity purified cGAS was performed in HEK293T cells under control and DNA-challenged conditions (N = 3 each) and human fibroblasts (HFF) cells under control and HSV-1 infected conditions (N = 4 each) to generate candidate cGAS PTM sites. Using parallel reaction monitoring, a total of 11 PTMs (4 phosphorylations and 7 acetylations) were validated in HEK293T, HFF, and THP-1 cells. Of these, 3 phosphorylations and 5 acetylations have not been previously identified. The functions of these modifications were by generating a series of mutants and measuring cGAS-dependent apoptotic and immune signaling activities.

2020-05-11 | PXD017109 | Pride

mTORC2-driven chromatin cGAS mediates chemoresistance in colorectal cancer

Project description:Cyclic GMP-AMP synthase (cGAS), a cytosolic DNA sensor that initiates a STING-dependent innate immune response, binds tightly to chromatin, where its catalytic activity is inhibited. However, the mechanisms underlying cGAS recruitment to chromatin and the functions of chromatin-bound cGAS (ccGAS) remain unclear. Here, we demonstrate that mTORC2-mediated serine 37 phosphorylation promotes human cGAS chromatin localization, regulating colorectal cancer cell growth and drug resistance independently of STING. We discovered that ccGAS recruits the SWI/SNF complex at specific chromatin regions to regulate expression of genes involved in glutaminolysis and DNA replication. Knockdown of ccGAS inhibits colorectal cancer cell growth but induces chemoresistance under fluorouracil exposure both in vitro and in vivo. Moreover, inhibition of kidney-type glutaminase (KGA), a downstream target of ccGAS, overcomes chemoresistance induced by ccGAS knockdown in human and murine colorectal cancer. Thus, our study demonstrates that ccGAS coordinates colorectal cancer plasticity and acquired chemoresistance through epigenetic patterning, and illustrates that simultaneously targeting mTORC2-ccGAS and KGA provides a promising theraputic strategy to eliminate quiescent resistant cancer cells.

2025-05-07 | PXD053068 | Pride

Mass spectrometry analysis of proteins interacting with cGAS

Project description:o identify the potential associated proteins of cGAS, we performed co-IP followed by mass spectrometry analysis in HEK293A cells stably expressing SFB-tagged cGAS.

2022-02-07 | PXD023597 | Pride

Human 293T -cGAS-MYO1F-KAT2A,LC-MS

Project description:To identify cGAS acetylation sites, 293T cells coexpressing the PCDH-EGFP-puro empty vector or PCDH-EGFP-puro-Flag-cGAS with KAT2A and MYO1F were subjected to immunoprecipitation with an anti-Flag antibody. After washing four times with IP buffer, the protein was eluted with IP buffer containing 0.1% SDS and analyzed by mass spectrometry.

2024-12-14 | PXD057694 | Pride

Gene induction in STAT1-/- fibroblasts transduced with lentiviruses expressing human cGAS

Project description:The hypothesis tested was that lentiviral driven cGAS expression activates antiviral gene expression. Cells were transduced with lentiviruses expressing cGAS or a control (firefly luciferase). Total RNA was harvested 48 h post-transduction and processed for Illumina BeadArray.

2013-12-01 | E-GEOD-52241 | biostudies-arrayexpress

PDCD6 modulates LC3-associated phagocytosis-mediated antimicrobial defense by regulating lactate metabolism

Project description:LC3-associated phagocytosis (LAP) is critical in host defense against invading pathogens, but the molecular mechanism for LAP activation is still unclear. Here, we find programmed cell death 6 (PDCD6) as a negative regulator of LAP. PDCD6 deficiency in mice and macrophages induces enhanced bactericidal activity and LAP formation. In parallel, lactate dehydrogenase A (LDHA) activity and lactate production is induced in macrophages challenged with bacteria, Zymosan or Pam3CSK4, while genetic ablation or pharmacological inhibition of LDHA reduces lactate levels and impairs bactericidal activity in vivo and in vitro. Mechanistically, PDCD6 interacts with LDHA to downregulate lactate metabolism, leading to reduced RUBCN lactylation at lysine33 (K33). By contrast, PDCD6-deficiency increases RUBCN lactylation, thereby promotes RUBCN interaction with VPS34, LAP formation, and protective responses. Our results thus suggest a PDCD6-LDHA-lactate-RUBCN axis of innate immunity regulation that may both contribute to protection from infectious diseases and serve as targets for therapeutic development.

2024-10-18 | PXD056047 | Pride

Identification of genes regulated by L-lactate and by DL-lactate in Lactobacillus plantarum

Project description:L. plantarum is known to possess an L-lactate inducible lactate racemase activity (Goffin et al. 2005. J. Bacteriol. 187:6750). In the present study, microarrays were used in order to identify all genes that are up-regulated by L-lactate, but not by a racemic mixture of D- and L-lactate. A mutant of L. plantarum NCIMB8826 deficient for NAD-dependent L-lactate activity (TF101; Ferain et al. 1994. 176:596), and thus producing no L-lactate, was grown in MRS medium at 28Â°C until mid-exponential phase (OD600nm 0.75). The culture was then divided into 3 sub-cultures. Optically pure sodium L-lactate (200 mM) was added to the first sub-culture (TF101 + L-lac 200 mM). An equimolar mixture of sodium D- and L-lactate (100 mM each) was added to the second sub-culture (TF101 + L/D-lac 200 mM). The third sub-culture was not treated (TF101; reference sample). The three sub-cultures were further incubated at 28Â°C for 1h30 (a time known to be sufficient for induction of lactate racemase activity by L-lactate). Cells were harvested by centrifugation. Microarray data were used ot identify genes that are specifically induced by L-lactate (comparison of TF101 with TF101 + L-lac 200 mM), but not by DL-lactate (comparison of TF101 with T101 + L/D-lac 200 mM). There are no biological replicates.

2013-07-01 | E-GEOD-43518 | biostudies-arrayexpress

Determination of WatR binding site in Methylomonas sp. DH-1 after lactate adaptive evolution

Project description:JHM80 strain was obtained by adaptive evolution of Methylomonas sp. DH-1 strain against 8.0 g/L of lactate. The tolerance against lactate of JHM80 was obtained by the overexpression of watR (weak acid tolerance regulator). In order to discover the target genes of WatR, FLAG epitope tag was added to WatR of JHM80 strain and ChIP-seq was performed.

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Lactate Stress in L. plantarum WCFS1

Project description:Cultures were grown untill an optical density of 1.0. Cells were subsequently stressed with 2000 mM Na-lactate and samples were taken in time (15, 30, and 60 minutes). Samples were hybridized against a reference sample taken at t=0, just before addition of lactate. Biological duplicate was performed.

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