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Phosphorylation of Human Thyroid Hormone Receptor beta-1 by Casein Kinase II

Research Project

Project/Area Number 09671018
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field 内分泌・代謝学
Research InstitutionTohoku University

Principal Investigator

SUGAWARA Akira  Tohoku University, hospital Research Associate, 医学部・附属病院, 助手 (90270834)

Project Period (FY) 1997 – 1998
Project Status Completed (Fiscal Year 1998)
Budget Amount *help
¥3,100,000 (Direct Cost: ¥3,100,000)
Fiscal Year 1998: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 1997: ¥2,100,000 (Direct Cost: ¥2,100,000)
KeywordsThyroid Hormone / Receptor / Phosphorylation
Research Abstract

Bacterially-expressed human thyroid hormone receptor beta-1 (hTRbeta1) recently has been shown to be phosphorylated in vitro by HeLa cytoso1ic extract. In the present study, we first demonstrated that hTRbeta1 also could be phosphorylated in vitro b purified casein kinase II (CKII). Phosphoamino acid analysis revealed hTrbeta1 was phosphorylated on both serine and threonine residues. In vitro CKII phosphorylation of glutathione S-transferase (GST)-hTRbeta1 fusion proteins whose predicted CKII phosphorylation sites were mutated demonstrated that a threonine residue located in the hinge region(Thr-210) could be phosphorylated by CKII. In order to elucidate the functional significance of CKfl phosphorylation of Thr-210 in hTRbeta1, we next performed transient transfection studies using either wild type or Thr-210 mutated hTRbeta1.In terestingly, the basal repression eve in the absence of ligand was attenuated significantly when Thr-210 mutated hTRbeta1 was used. Since Thr-210 is located within the interacting domain with nudear receptor co-repressor (N-CoR), we next performed electrophoretic mobility shifi assay (EMSA)to examine the interaction between amino terminal-truncated N-CoR (NCoRI) and wild type or Thr-210 mutated hTRbeta1. Interestingly, in contrast to retinoid OMEGA receptor beta(RXRbeta) which equally formed heterodimers with both types of hTR beta1, N CoRIp referentially formed heterodimers with wild type hTRbeta1 than Thr-210mutated hTRbeta1. Taken together, we speculate that CKII phosphorylation ofThr-210 m hTRbeta1 might modulate interaction with N-Co R, and contribute tomediate basal repression in the absence of ligand.

Report

(3 results)
  • 1998 Annual Research Report   Final Research Report Summary
  • 1997 Annual Research Report
  • Research Products

    (2 results)

All Other

All Publications (2 results)

  • [Publications] 菅原 明、他: "ヒトβ1型甲状腺ホルモン受容体 (hTRβ1) のカゼインキナーゼII (CKII) によるリン酸化メカニズムの解明" 診療と新薬. 第36巻第7号 未定. (1999)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1998 Final Research Report Summary
  • [Publications] 菅原 明、他: "ヒトβ1型甲状腺ホルモン受容体(hTRβ1)のカゼインキナーゼII (CKII)によるリン酸化メカニズムの解明" 診療と新薬. 第36巻 第7号. (1999)

    • Related Report
      1998 Annual Research Report

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Published: 1997-04-01   Modified: 2016-04-21  

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