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Phosphoproteomic response in nitrosamine-exposed mice

ABSTRACT: The aim of this study was to characterize ATM/ATR substrate motif specific phosphoproteome (phospho-SQ/TQ) in response to N-nitrosodimethylamine (NDMA) in mice. Motif specific phosphorylation were measured using quantitative LC-MS/MS based on TMT labeling.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Liver

SUBMITTER: Ishwar Kohale

LAB HEAD: Forest Michael White

PROVIDER: PXD021142 | Pride | 2021-02-10

REPOSITORIES: Pride

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			Action	DRS
	20190421_NDMA_AagTg_Livers_TMT10plex_pY_Sup-1.msf	Msf
	20190421_NDMA_AagTg_Livers_TMT10plex_pY_Sup-1.mzML	Mzml
	20190421_NDMA_AagTg_Livers_TMT10plex_pY_Sup.raw	Raw
	20190422_NDMA_AagTg_Livers_TMT10plex_pSQ_AC11-1.msf	Msf
	20190422_NDMA_AagTg_Livers_TMT10plex_pSQ_AC11-1.mzML	Mzml

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Project description:Aluminum (Al) toxicity and phosphate (Pi) limitation are widespread chronic abiotic and mutually enhancing stresses that profoundly affect crop yield. Both stresses causes a strong inhibition of root growth due to a progressive exhaustion of the stem cell niche. Here we report on a CASEIN KINASE 2 (CK2) inhibitor identified by its capability to maintain a functional root stem cell niche under Al toxic conditions. CK2 operates through phosphorylation of the cell cycle checkpoint activator SUPPRESSOR OF GAMMA RADIATION 1 (SOG1), priming its activity under DNA damaging conditions. In addition to yielding Al tolerance, both CK2 and SOG1 inactivation result in resistance to phosphate starvation, revealing the existence of a low phosphate induced cell cycle checkpoint that depends on the DNA damage activator ATAXIA-TELANGIECTASIA MUTATED (ATM). Overall, our data reveal an important physiological role for the plant DNA damage response pathway under agricultural limiting growth conditions and opening new avenues to cope with the problem of Pi limitation. SOG1 can be phosphorylated by both ATM and ATR (Sjogren et al., 2015; Yoshiyama et al., 2017). ATM phosphorylation of SOG1 can occur at five different S/TQ sites upon treatment with double-stand break inducing compounds such as zeocin. This phosphorylation is important for its activity, as demonstrated by the inability of a phosphor-mutant allele to complement the sog1 mutant. In addition to the ATM/ATR-dependent phosphorylation sites, 11 putative CK2 phosphorylation sites [T/SXXE/D, with S or T serving as the phospho-acceptor site (Meggio and Pinna, 2003)] are found within the full length SOG1 proteins. Among these, four sites are conserved among orthologous proteins, stressing their potential importance to protein function. Of these, three cluster at the extreme C-terminus of SOG1, which also is also the location of the ATM/ATR phosphorylation sites. To test putative phosphorylation of any of these sites, TAP-tagged SOG1 protein was extracted and purified from cell cultures and subjected to phosphorylation analysis.

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Phosphoproteomic response in nitrosamine-exposed mice

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