Claudin-16 is directly phosphorylated by protein kinase a independently of a vasodilator-stimulated phosphoprotein-mediated pathway.

Claudin-16 is directly phosphorylated by protein kinase a independently of a vasodilator-stimulated phosphoprotein-mediated pathway. Research Abstract Details 

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Claudin-16 is directly phosphorylated by protein kinase a independently of a vasodilator-stimulated phosphoprotein-mediated pathway. Abstract Text:

Akira Ikari,Midori Ito,Chiaki Okude,Hayato Sawada,Hitoshi Harada,Masakuni Degawa,Hideki Sakai,Tadanobu Takahashi,Junko Sugatani,Masao Miwa,Akira Ikari,Midori Ito,Chiaki Okude,Hayato Sawada,Hitoshi Harada,Masakuni Degawa,Hideki Sakai,Tadanobu Takahashi,Junko Sugatani,Masao Miwa,

Claudin-16 (CLDN-16) is involved in the paracellular reabsorption of Mg(2+) in the thick ascending limb of Henle. The tight junctional localization and Mg(2+) transport of CLDN-16 are regulated by cAMP/PKA-dependent phosphorylation. Here, we examined whether PKA phosphorylates CLDN-16 in a direct or indirect manner. CLDN-16 was stably expressed in Madin-Darby canine kidney (MDCK) cells using a Tet-OFF system. The phosphorylation of CLDN-16 is upregulated by fetal calf serum (FCS). This phosphorylation was completely inhibited by a PKA inhibitor, N-[2-(p-bromocinnamylamino)ethyl]-5-isoquinolinesulfonamide dihydrochloride. Without FCS, dibutyryl cAMP (DBcAMP) increased the phosphoserine level of CLDN-16 in a concentration-dependent manner. The phosphorylated CLDN-16 elicited increases of transepithelial electrical resistance (TER) and transepithelial transport of Mg(2+). Vasodilator-stimulated phosphoprotein (VASP) was also phosphorylated in the presence of FCS or DBcAMP. In the glutathione-S-transferase (GST) pull down assay, a cytosolic carboxyl domain of CLDN-16 was associated with PKA, but not with VASP. Furthermore, PKA was immunoprecipitated with CLDN-16 in MDCK cells, but VASP was not. In cells expressing a dephosphorylated mutant (Ser160Ala) of VASP, CLDN-16 was phosphorylated by DBcAMP and was associated with ZO-1, a tight junctional-scaffolding protein, without integral cell-cell junctions. We suggest that PKA directly phosphorylates CLDN-16, resulting in the localization to tight junctions (TJs) and the maintenance of Mg(2+) reabsorption.

Claudin-16 is directly phosphorylated by protein kinase a independently of a vasodilator-stimulated phosphoprotein-mediated pathway. Publishing Authors By Initials

A Ikari,M Ito,C Okude,H Sawada,H Harada,M Degawa,H Sakai,T Takahashi,J Sugatani,M Miwa,A Ikari,M Ito,C Okude,H Sawada,H Harada,M Degawa,H Sakai,T Takahashi,J Sugatani,M Miwa,

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Claudin-16 is directly phosphorylated by protein kinase a independently of a vasodilator-stimulated phosphoprotein-mediated pathway. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of cellular physiology

VOLUME: 214

Page Numbers: 221-9

Journal Abbreviation: J. Cell. Physiol.

ISSN: 1097-4652

DAY: 31

MONTH: Jan

YEAR: 2008

Claudin-16 is directly phosphorylated by protein kinase a independently of a vasodilator-stimulated phosphoprotein-mediated pathway. Information

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LANGUAGE: eng

NlmUniqueID: 50222

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AFFILIATION: Department of Pharmaco-Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka, 52-1 Yada, Suruga-ku, Shizuoka, Japan. ikari@u-shizuoka-ken.ac.jp

Country: United States

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MEDLINETA: J Cell Physiol

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