Proteomics

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Cunjie_SLC3A2_Agilent6550_Fig2_S5


ABSTRACT: This dataset consists of 57 raw MS files acquired on Agilent 6550 iFunnel Q-TOF MS (Agilent Inc., Santa Clara, CA) mass spectrometer operated in data dependent acquisition (DDA) and target MS/MS mode. Code for variants with additional NXS/T sites: 255I WTseq: (N365, N381, N424, N506) 256G N273A (+1 site) 257A N273A; N355D (+2 sites) 258F N355D; N492D (+2 sites) 259J N273A; N355D; N492D (+3 sites) CJ1 D365N (-1 site) CJ2 D381N (-1 site) Cunjie Zhang did all the sample preparation, mass spectrometric acquisition and data analysis. The files are associated with a manuscript submitted for publication by Cunjie Zhang et al. SLC3A2 (4F2hc, CD98) is a single-pass transmembrane glycoprotein and acts as a disulfide-linked adaptor to the SLC7A5 and SLC7A11 exchangers which import essential amino acids and cystine while exporting Gln and Glu, respectively. Cancer cells often over-express SLC3A2, SLC7A5, SLC7A11 and the N-glycans branching, which support tumor progression by increasing mTOR signaling and mitigation of oxidative stress (ox-stress). Branched chain amino acids and mitigation of oxidative stress are also central to aging. Furthermore, the evolution of N-glycosylation sites on SLC3A adaptors and SLC7A transporters suggests a critical but poorly understood role for N-glycans. We have profiled the N-glycan structures at each site SLC3A2 (4F2hc, CD98) and analyzed their impact on trafficking, protein interactions, cellular AA balance and sensitivity to ox-stress. James W. Dennis is the corresponding author of the manuscript; James W. Dennis should be contacted for questions on this dataset DENNIS@lunenfeld.ca This submission is associated with: Figure 2 Figure S5 Table S1 Site-specific FLAG-SLC3A2 WTseq and variants Table S3: Site-specific FLAG-SLC3A2_GlcNAc-supplement

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

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Anne-Claude Gingras  

PROVIDER: MSV000092980 | MassIVE |

REPOSITORIES: MassIVE

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