Dataset Information

S-nitrosylation in P301S mouse tauopathy model

ABSTRACT: We looked to find earlier molecular changes in 2-month-old transgenic P301S mice. S-nitrosylated (SNO) proteins were identified in two brain regions, cortex and hippocampus, in P301S and Wild Type (WT) littermate control mice.

INSTRUMENT(S): 6550 iFunnel Q-TOF LC/MS

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Brain

DISEASE(S): Tauopathy

SUBMITTER: Haitham Amal

LAB HEAD: Steven R. Tannenbaum

PROVIDER: PXD010106 | Pride | 2019-11-08

REPOSITORIES: Pride

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Publications

S-nitrosylation of E3 ubiquitin-protein ligase RNF213 alters non-canonical Wnt/Ca+2 signaling in the P301S mouse model of tauopathy.

Amal Haitham H Gong Guanyu G Gjoneska Elizabeta E Lewis Sarah M SM Wishnok John S JS Tsai Li-Huei LH Tannenbaum Steven R SR

Translational psychiatry 20190129 1

Mutations in the MAPT gene, which encodes the tau protein, are associated with several neurodegenerative diseases, including frontotemporal dementia (FTD), dementia with epilepsy, and other types of dementia. The missense mutation in the Mapt gene in the P301S mouse model of FTD results in impaired synaptic function and microgliosis at three months of age, which are the earliest manifestations of disease. Here, we examined changes in the S-nitrosoproteome in 2-month-old transgenic P301S mice in ...[more]

PMID: 30696811

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Project description:Trypomastigotes from Trypanosoma cruzi adhere to the extracellular matrix (ECM) in order to invade mammalian host cells. Incubation of trypomastigotes with ECM leads to a decrease of nitric oxide synthase (NOS) activity and associated post-translational modifications (PTMs). Herein, resin-assisted enrichment of thiols combined with mass spectrometry were employed to map site-specific S-nitrosylated (SNO) proteins from T. cruzi trypomastigotes incubated (MTy) or not (Ty) with ECM. We confirmed the reduction of S-nitrosylation upon incubation with ECM, associated to a rewiring of the subcellular distribution and intracellular signaling pathways of the SNO proteins between MTy and Ty conditions. Forty (~10.7%) and 248 (~66.4%) SNO-peptides were uniquely identified in MTy and Ty, respectively, in addition to 85 peptides (~22.7%) quantified in both conditions. S-nitrosylated proteins were enriched in a wide range of cellular components, including surface membranes and vesicles, and are involved in ribosome, transport, carbohydrate and lipid metabolisms. Of note, we described for the first time nytrosylation of histones H2B and H3 on Cys64 and Cys126, respectively, which is was more abundant in MTy. Additionally, sequence alignment shows that H3 (Cys126) histone is also present in T.b.brucei, but not in L. major, while H2B (Cys64) is absent in both parasites and other higher eukaryotes. Protein-protein interaction networks analyzed by STRING revealed ribosomal proteins, proteins involved in carbon and fatty acid metabolism to be among the enriched protein complexes. Among the SNO ribosomal proteins, 90% were identified and quantified uniquely or upregulated in the Ty fraction. Enzymes involved in oxidoreductase, kinases and phosphatases were identified as nitrosylated and phosphorylated in the same conditions suggesting a crosstalk between these modifications linked to regulation of energy metabolism of T. cruzi in the presence of ECM. Although enzymatic activity of NOS was described in T. cruzi, its identification is elusive. In silico mapping of putative nitric oxide synthase (NOS) gene(s) based on domain architecture identified four putative T. cruzi proteins expressing a putative C-terminal NOS domain: two putative P450 reductases, a putative FMN/FAD containing oxidoreductase and a putative oxidoreductase-protein. Our results provide the first site-specific characterization of S-nitrosylated proteins in T. cruzi linked to the roles of NO in reprogramming parasite cells to invade mammalian hosts.

			Action	DRS
	Protein_summary_SNOinP301S_PRIDE.xlsx	Xlsx
	Tg-Cor.zip	Other
	Tg-Hip.zip	Other
	WT-Cor.zip	Other
	WT-Hip.zip	Other