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- Title
Mass spectrometric analysis of novel phosphorylation sites in the TRPC4β channel.
- Authors
Lee, Ji Eun; Song, Min-Young; Shin, Seok Kyo; Bae, Seong Han; Park, Kang-Sik
- Abstract
RATIONALE The transient receptor potential canonical (TRPC) channel 4β is a non-selective cation channel that is regulated by intracellular Ca2+ and G protein-coupled receptors. Tyrosine phosphorylation of TRPC4β is important in mediating the activity and membrane expression of this channel protein. However, studies of TRPC4β Ser/Thr phosphorylation are lacking. METHODS To investigate the phosphorylation sites involved in regulating the diverse functions of TRPC4β in mammalian cells, we used nano-liquid chromatography/tandem mass spectrometry to identify key phosphorylation sites in TRPC4β that was immunopurified from HEK293 cells with monoclonal anti-TRPC4β antibody. RESULTS We identified four phosphorylation sites in the C-terminus of TRPC4β, none of which had been previously reported. Our data show that TRPC4β in mammalian cells is highly phosphorylated under basal conditions at multiple sites, and that a mass spectrometric proteomic technique combined with antibody-based affinity purification is an effective approach to define the phosphorylation sites of TRPC4β channels in mammalian cells. CONCLUSIONS These novel phosphorylation sites on TRPC4β may play a potential role in the phosphorylation-mediated regulation of TRPC4β channel activity and function in mammalian cells. Copyright © 2012 John Wiley & Sons, Ltd.
- Publication
Rapid Communications in Mass Spectrometry: RCM, 2012, Vol 26, Issue 17, p1965
- ISSN
0951-4198
- Publication type
Article
- DOI
10.1002/rcm.6305