Phosphorylation on the Ser 824 residue of TRPV4 prefers to bind with F-actin than with microtubules to expand the cell surface area

Cell Signal. 2012 Mar;24(3):641-51. doi: 10.1016/j.cellsig.2011.11.002. Epub 2011 Nov 10.


Previously, we demonstrated that the transient receptor potential vanilloid 4 (TRPV4) cation channel, a member of the TRP vanilloid subfamily, is one of the serum glucocorticoid-induced protein kinase1 (SGK1) authentic substrate proteins, and that the Ser 824 residue of TRPV4 is phosphorylated by SGK1. In this study, we demonstrated that phosphorylation on the Ser 824 residue of TRPV4 is required for its interaction with F-actin, using TRPV4 mutants (S824D; a phospho-mimicking TRPV4 mutant and S824A; a non-phosphorylatable TRPV4 mutant) and its proper subcellular localization. Additionally, we noted that the phosphorylation of the Ser824 residue promotes its single channel activity, Ca(2+) influx, protein stability, and cell surface area (expansion of plasma membrane).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism*
  • Amino Acid Sequence
  • Amino Acid Substitution
  • Calcium / metabolism
  • Cell Line
  • Cell Survival
  • Humans
  • Microtubules / metabolism*
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Phorbol Esters / pharmacology
  • Phosphorylation
  • Protein Binding
  • Serine / metabolism
  • TRPV Cation Channels / genetics
  • TRPV Cation Channels / metabolism*


  • Actins
  • Phorbol Esters
  • TRPV Cation Channels
  • TRPV4 protein, human
  • phorbol-12,13-didecanoate
  • Serine
  • Calcium