SAP97 promotes the stability of Nax channels at the plasma membrane

Masahito Matsumoto, Akihiro Fujikawa, Ryoko Suzuki, Hidetada Shimizu, Kazuya Kuboyama, Takeshi Y. Hiyama, Randy A. Hall, Masaharu Noda

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Nax is a sodium-level sensor for body fluids expressed in the circumventricular organs in the brain. Nax has a putative PSD-95/Disc-large/ZO-1 (PDZ)-binding motif at the carboxyl (C)-terminus. Here we found that several PDZ proteins bind to Nax by PDZ-array overlay assay. Among them, synapse-associated protein 97 (SAP97/DLG1) was coexpressed with Nax in the subfornical organ. In C6 glioblastoma cells, destruction of the PDZ-binding motif of Nax or depletion of SAP97 resulted in a decrease in cell-surface Nax, which was attenuated with inhibitors of endocytosis. These results indicate that SAP97 contributes to the stabilization of Nax channels at the plasma membrane. Structured summary of protein interactions: Nax physically interacts with SAP97 by anti tag coimmunoprecipitation (View interaction) CNRasGEF binds to Nax by protein array (View interaction) Nax and SAP97 colocalize by fluorescence microscopy (View interaction) GIPC1 binds to Nax by protein array (View interaction) ZO-1 binds to Nax by protein array (View interaction) SAP97 binds to Nax by protein array (View interaction) Densin-180 binds to Nax by protein array (View interaction) Beta-1-syntrophin binds to Nax by protein array (View interaction) ERBIN binds to Nax by protein array (View interaction) Nax physically interacts with SAP97 by pull down (View interaction) Lnx1 binds to Nax by protein array (View interaction) nNOS binds to Nax by protein array (View interaction)

Original languageEnglish
Pages (from-to)3805-3812
Number of pages8
JournalFEBS Letters
Volume586
Issue number21
DOIs
Publication statusPublished - Nov 2 2012
Externally publishedYes

Fingerprint

Protein Array Analysis
Cell membranes
Cell Membrane
Proteins
Subfornical Organ
Body Fluids
Glioblastoma
Endocytosis
Fluorescence Microscopy
Fluorescence microscopy
Body fluids
Sodium
Assays
Brain
Stabilization

Keywords

  • Astrocyte
  • MAGUK protein
  • PDZ array
  • PDZ-binding motif
  • Sodium channel
  • Subfornical organ

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

Matsumoto, M., Fujikawa, A., Suzuki, R., Shimizu, H., Kuboyama, K., Hiyama, T. Y., ... Noda, M. (2012). SAP97 promotes the stability of Nax channels at the plasma membrane. FEBS Letters, 586(21), 3805-3812. https://doi.org/10.1016/j.febslet.2012.09.018

SAP97 promotes the stability of Nax channels at the plasma membrane. / Matsumoto, Masahito; Fujikawa, Akihiro; Suzuki, Ryoko; Shimizu, Hidetada; Kuboyama, Kazuya; Hiyama, Takeshi Y.; Hall, Randy A.; Noda, Masaharu.

In: FEBS Letters, Vol. 586, No. 21, 02.11.2012, p. 3805-3812.

Research output: Contribution to journalArticle

Matsumoto, M, Fujikawa, A, Suzuki, R, Shimizu, H, Kuboyama, K, Hiyama, TY, Hall, RA & Noda, M 2012, 'SAP97 promotes the stability of Nax channels at the plasma membrane', FEBS Letters, vol. 586, no. 21, pp. 3805-3812. https://doi.org/10.1016/j.febslet.2012.09.018
Matsumoto M, Fujikawa A, Suzuki R, Shimizu H, Kuboyama K, Hiyama TY et al. SAP97 promotes the stability of Nax channels at the plasma membrane. FEBS Letters. 2012 Nov 2;586(21):3805-3812. https://doi.org/10.1016/j.febslet.2012.09.018
Matsumoto, Masahito ; Fujikawa, Akihiro ; Suzuki, Ryoko ; Shimizu, Hidetada ; Kuboyama, Kazuya ; Hiyama, Takeshi Y. ; Hall, Randy A. ; Noda, Masaharu. / SAP97 promotes the stability of Nax channels at the plasma membrane. In: FEBS Letters. 2012 ; Vol. 586, No. 21. pp. 3805-3812.
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abstract = "Nax is a sodium-level sensor for body fluids expressed in the circumventricular organs in the brain. Nax has a putative PSD-95/Disc-large/ZO-1 (PDZ)-binding motif at the carboxyl (C)-terminus. Here we found that several PDZ proteins bind to Nax by PDZ-array overlay assay. Among them, synapse-associated protein 97 (SAP97/DLG1) was coexpressed with Nax in the subfornical organ. In C6 glioblastoma cells, destruction of the PDZ-binding motif of Nax or depletion of SAP97 resulted in a decrease in cell-surface Nax, which was attenuated with inhibitors of endocytosis. These results indicate that SAP97 contributes to the stabilization of Nax channels at the plasma membrane. Structured summary of protein interactions: Nax physically interacts with SAP97 by anti tag coimmunoprecipitation (View interaction) CNRasGEF binds to Nax by protein array (View interaction) Nax and SAP97 colocalize by fluorescence microscopy (View interaction) GIPC1 binds to Nax by protein array (View interaction) ZO-1 binds to Nax by protein array (View interaction) SAP97 binds to Nax by protein array (View interaction) Densin-180 binds to Nax by protein array (View interaction) Beta-1-syntrophin binds to Nax by protein array (View interaction) ERBIN binds to Nax by protein array (View interaction) Nax physically interacts with SAP97 by pull down (View interaction) Lnx1 binds to Nax by protein array (View interaction) nNOS binds to Nax by protein array (View interaction)",
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