Proteomics

Dataset Information

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LFQ of UMR106 pY-IP

ABSTRACT: UMR106 cells were untreated or treated with 5 mM Pi or 100 ng/ml FGF2 for 15 min. The lysates were digested with trypsin, and tyrosine-phosphorylated peptides were enriched by anti-phosphotyrosine antibody and subjected to LC-MS/MS analysis. Raw data were directly analyzed against the SwissProt database restricted to Rattus using Proteome Discoverer version 2.2 for identification and label-free precursor ion quantification.

ORGANISM(S): Rattus Rattus (black Rat)

SUBMITTER: Hidetaka Kosako 

PROVIDER: PXD010790 | JPOST Repository | Sun May 05 00:00:00 BST 2019

REPOSITORIES: jPOST

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Dataset's files

Source:
Action DRS
DDA_UMR106_pY_FGF2.raw Raw
DDA_UMR106_pY_Pi.raw Raw
DDA_UMR106_pY_control.raw Raw
UMR106_pY_IP_LFQ_PD22.xlsx Xlsx
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Publications

Activation of unliganded FGF receptor by extracellular phosphate potentiates proteolytic protection of FGF23 by its O-glycosylation.

Takashi Yuichi Y   Kosako Hidetaka H   Sawatsubashi Shun S   Kinoshita Yuka Y   Ito Nobuaki N   Tsoumpra Maria K MK   Nangaku Masaomi M   Abe Masahiro M   Matsuhisa Munehide M   Kato Shigeaki S   Matsumoto Toshio T   Fukumoto Seiji S  

Proceedings of the National Academy of Sciences of the United States of America 20190516 23

Fibroblast growth factor (FGF) 23 produced by bone is a hormone that decreases serum phosphate (Pi). Reflecting its central role in Pi control, serum FGF23 is tightly regulated by serum Pi alterations. FGF23 levels are regulated by the transcriptional event and posttranslational cleavage into inactive fragments before its secretion. For the latter, O-glycosylation of FGF23 by <i>GALNT3</i> gene product prevents the cleavage, leading to an increase in serum FGF23. However, the molecular basis of  ...[more]

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