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Animal cells and systems v.14 no.2, 2010년, pp.99 - 114   SCIE 피인용횟수: 1
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The modulation of TRPV4 channel activity through its Ser 824 residue phosphorylation by SGK1

Lee, Run-Jeoung    (Department of Biology Education, Chungbuk National University   ); Shin, Sung-Hwa    (Department of Biology Education, Chungbuk National University   ); Chun, Jae-Sun    (Department of Biology Education, Korea National University of Education   ); Hyun, Sung-Hee    (Department of Pre-medicine, Eulji University School of Medicine   ); Kim, Yang-Mi    (Department of Physiology, College of Medicine, Chungbuk National University   ); Kang, Sang-Sun    (Department of Biology Education, Chungbuk National University  );
  • 초록

    With the consensus sequence information of the serum glucocorticoid-induced protein kinase-1 (SGK1) phosphorylation site {R-X-R-X-X-(S/T) $\Phi$ ; where $\Phi$ is any hydrophobic amino acid}, we noticed that the transient receptor potential vanilloid 4 (TRPV4) cation channel, a member of the TRP vanilloid subfamily, harbors the putative SGK1 phosphorylation site (on its Ser 824). We have demonstrated that TRPV4 is an SGK1 authentic substrate protein, with the phosphorylation on the Ser 824 of TRPV4 by SGK1. Further, using TRPV4 mutants (S824A and S824D), we noted that the modification of the Ser 824 activates its $Ca^{2+}$ entry, and sensitizes the TRPV4 channel to 4- $\alpha$ -phorbol 12,13-didecanoate (4- ${\alpha}PDD$ ) or heat, simultaneously enhancing its active state. Additionally, we determined that the modification of the Ser 824 controls both its plasma membrane localization and its protein interactions with calmodulin. Thus, we have proposed herein that phosphorylation on the Ser 824 of TRPV4 is one of the control points for the regulation of its functions.

  • 주제어

    TRPV4 .   SGK1 .   phosphorylation .   calmodulin.  

  • 참고문헌 (39)

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  • 이 논문을 인용한 문헌 (1)

    1. 2011. "" Animal cells and systems, 15(2): 123~130     

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