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Large‐scale identification of phosphorylation sites in renal cortical transporters
Author(s) -
Feric Marina,
Hoffert J D,
Pisitkun T,
Knepper M A
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.1002.2
Subject(s) - transporter , phosphorylation , phosphoproteomics , chemistry , biochemistry , renal cortex , biology , microbiology and biotechnology , protein phosphorylation , kidney , protein kinase a , gene , endocrinology
Recent advances in mass spectrometry have provided means for large‐scale phosphoproteomic profiling of specific tissues. Here we report results from large‐scale LC‐MS/MS‐based phosphoproteomic profiling of biochemically isolated membranes from the renal cortex, focusing on transporters. Final data sets were filtered (target‐decoy) to limit false‐positive identifications to <2%. A total of 7,125 unique non‐phosphorylated and 744 unique phosphorylated peptides were identified. Over half of the phosphorylation sites identified on membrane transporters are novel. Phosphopeptides found included sites in Slc (n=63), Abc (n=4), and Aqp (n=3) family proteins. Most of the Slc family proteins are apical or basolateral transporters expressed in proximal tubule cells, including proteins known to mediate transport of glucose, amino acids, organic ions and inorganic ions. In addition, we also identified potentially important phosphorylation sites for transport proteins from other nephron segments, including NKCC2 and NCC. An online database from this study provides a resource for future studies of transporter regulation.