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Phophoproteomic identification of kinases downstream of RIPK2

ABSTRACT: Identification of kinases whose activities are regulated by RIPK2 in prostate cancer cells.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell

DISEASE(S): Prostate Adenocarcinoma

SUBMITTER: Wei Yang

LAB HEAD: Wei Yang

PROVIDER: PXD018871 | Pride | 2022-02-09

REPOSITORIES: Pride

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			Action	DRS
	Phosphoproteomics_G12S1.raw	Raw
	Phosphoproteomics_G12S2.raw	Raw
	Phosphoproteomics_G12S3.raw	Raw
	Phosphoproteomics_G1S1.raw	Raw
	Phosphoproteomics_G1S2.raw	Raw

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Publications

Receptor-interacting protein kinase 2 (RIPK2) stabilizes c-Myc and is a therapeutic target in prostate cancer metastasis.

Yan Yiwu Y Zhou Bo B Qian Chen C Vasquez Alex A Kamra Mohini M Chatterjee Avradip A Lee Yeon-Joo YJ Yuan Xiaopu X Ellis Leigh L Di Vizio Dolores D Posadas Edwin M EM Kyprianou Natasha N Knudsen Beatrice S BS Shah Kavita K Murali Ramachandran R Gertych Arkadiusz A You Sungyong S Freeman Michael R MR Yang Wei W

Nature communications 20220203 1

Despite progress in prostate cancer (PC) therapeutics, distant metastasis remains a major cause of morbidity and mortality from PC. Thus, there is growing recognition that preventing or delaying PC metastasis holds great potential for substantially improving patient outcomes. Here we show receptor-interacting protein kinase 2 (RIPK2) is a clinically actionable target for inhibiting PC metastasis. RIPK2 is amplified/gained in ~65% of lethal metastatic castration-resistant PC. Its overexpression i ...[more]

PMID: 35115556

Similar Datasets

Proteomic identification of RIPK2 interactome

Project description:Identification of proteins associated with RIPK2 via immunoprecipitation-mass spectrometry (IP-MS)

2022-02-09 | PXD018870 | Pride

Label-free proteomic identification of proteins regulated by RIPK2 in PC3 cells

Project description:Label-free proteomics comparison of PC3 cells with versus without CRISPR/Cas9 knockout of RIPK2. The goal was to identify proteins downstream of RIPK2 in prostate cancer cells.

2022-02-09 | PXD018890 | Pride

Small-molecule inhibitors reveal an indispensable scaffolding role of RIPK2 in NOD2 signaling

Project description:RIPK2 mediates inflammatory signaling by the bacteria-sensing receptors NOD1 and NOD2, and inhibition of RIPK2 by kinase inhibitors is an emerging strategy to ameliorate NOD-mediated pathologies. However, the role for RIPK2’s kinase activity remains unclear. Here, we reveal that RIPK2 kinase activity is dispensable for NOD2 inflammatory signaling and show that RIPK2 inhibitors function instead by antagonizing XIAP-binding and XIAP-mediated ubiquitination of RIPK2. We map the XIAP binding site on RIPK2 to the loop between 2 and 3 of the N-lobe of the kinase, which is in close proximity to the ATP-binding pocket. Through characterization of a new series of ATP-competitive RIPK2 inhibitors, we identify the molecular features that determine their inhibition of both the RIPK2-XIAP interaction, and of cellular and in vivo NOD2 signaling. Our study exemplifies how targeting of the ATP-binding pocket in RIPK2 can be exploited to interfere with the RIPK2-XIAP interaction for modulation of NOD signaling.

2018-07-25 | PXD009724 | Pride

Transcriptional profiles of PA1 teratoma cells transfected by RIPK1, RIPK2, RIPK3, or RIPK4

Project description:RIPK4 but not the related kinases RIPK1, RIPK2, and RIPK3 caused similar transcriptional changes to Wnt3a. PA1 cells were transfected by 8ug RIPK1, RIPK2, RIPK3, or RIPK4 for 48h, RNA were extracted and sequenced.

2013-02-04 | E-GEOD-43362 | biostudies-arrayexpress

Transcriptional profiles of PA1 teratoma cells transfected by RIPK1, RIPK2, RIPK3, or RIPK4

Project description:RIPK4 but not the related kinases RIPK1, RIPK2, and RIPK3 caused similar transcriptional changes to Wnt3a.

2013-02-04 | GSE43362 | GEO

RNA seq HT-29 wild type, IRGM depleted, or IRGM and RIPK2 depleted cells with Shigella flexneri

Project description:To understand the regulation of NODs-RIPK2 signaling during microbial infection

2022-09-16 | E-MTAB-12067 | biostudies-arrayexpress

A new regulatory interface on RIPK2 controls XIAP binding and NOD signaling activity

Project description:Signaling via the intracellular pathogen receptors Nucleotide-binding oligomerization domain-containing proteins NOD1 and NOD2 requires Receptor Interacting Kinase 2 (RIPK2), an adaptor kinase that can be targeted for the treatment of various inflammatory diseases. However, the molecular mechanisms of how RIPK2 contributes to NOD signaling are not completely understood. We generated FLAG-tagged RIPK2 knock-in mice using CRISPR/Cas9 technology to study NOD signaling mechanisms on an endogenous level. Using cells from these mice we were able to generate a detailed map of post-translational modifications on RIPK2 during NOD signaling using mass spectrometry analysis and we identified a new regulatory interface on RIPK2, which dictates the crucial interaction with the E3 ligase XIAP.

2020-08-13 | PXD017741 | Pride

RNA seq HT-29 wild type, IRGM depleted, or IRGM and RIPK2 depleted cells with Shigella flexneri

Project description:RNA seq HT-29 wild type, IRGM depleted, or IRGM and RIPK2 depleted cells with Shigella flexneri

| PRJEB55304 | ENA

Gene expression profile after oral vaccination against infectious pancreatic necrosis virus (IPNV)

Project description:Oral immunization of trout against infectious pancreatic necrosis virus (IPNV) have been recently reported by using a DNA vector coding the viral capsid VP2 gene encapsulated in alginate microspheres. We report here an study of the transcripts in head kidney and pyloric ceca 7 days after oral vaccination of rainbow trout by using a newly designed rainbow trout 60-mer oligo microarray focused in their immune-related genes. Trout were obtained from 4 different farms, one group of trout was defined as belonging to one of the farms. Each of the trout 4 groups were divided into two subgroups of 6 trout for each subgroup. Subgroup I was orally vaccinated with 10 M-BM-5l of suspension of the vaccine microspheres each containing 10 M-BM-5g of pcDNA-VP2 diluted in 10M-BM-5l of PBS, while subgroup II received similar microspheres suspension but pcDNA. Head kidney and pyloric ceca were collected from each subgroup and RNA was extracted.

2012-07-18 | E-GEOD-31591 | biostudies-arrayexpress

Nod1-dependent NF-kB activation initiates hematopoietic stem cell specification in response to small Rho GTPases

Project description:The possibility of specifying functional hematopoietic stem and progenitor cells (HSPCs) from human pluripotent stem cells (hPSCs) would overcome current limitations related to HSPC transplantation. However, generating hPSC-derived HSPCs has been elusive, necessitating a better understanding of the native developmental mechanisms that trigger HSPC specification. Here, we revealed in vivo an intrinsic inflammatory mechanism triggered by Nod1 that drives early hemogenic endothelium (HE) patterning to specify HSPCs. Our genetic and chemical experiments showed that HSPCs failed to specify in the absence of Nod1 and its downstream kinase Ripk2. Rescue experiments demonstrated that Nod1 and Ripk2 acted through NF-kB, and that small Rho GTPases are at the apex of this mechanism. Manipulation of NOD1 in a human system of hPSCs differentiation towards the definitive hematopoietic lineage indicated functional conservation. This work establishes the RAC1-NOD1-RIPK2-NFkB axis as the earliest inflammatory inductor that intrinsically primes the HE for proper HSPC specification. Manipulation of this pathway could help derive a competent HE amenable to specify functional patient specific HSPCs for the treatment of blood disorders. Keywords: NOD1, RIPK2, NF-kB, RAC1, Rho GTPases, Hematopoietic Stem and Progenitor Cell Specification, Hemogenic Endothelium.

2023-10-26 | GSE224708 | GEO

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