RNAi of 14-3-3η protein increases intracellular stability of tyrosine hydroxylase

Akira Nakashima, Nobuhiro Hayashi, Yoko S. Kaneko, Keiji Mori, Esther L. Sabban, Toshiharu Nagatsu, Akira Ota

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

Tyrosine hydroxylase is the rate-limiting enzyme in catecholamine biosynthesis, and its N-terminus plays a critical role in the intracellular stability of the enzyme. In the present study, we investigated the mechanism by which the N-terminus of human tyrosine hydroxylase type 1 (hTH1) affects the stability. The results obtained by using N-terminus-deleted hTH1 mutants identified the sequence up to Ala23 as mediating the stability. The down-regulation of 14-3-3η proteins in PC12D cells exogenously expressing hTH1, enhanced the stability of the wild-type enzyme and that of the mutant lacking the N-terminus up to Ala23. However, the stability of the mutant was reduced compared to the wild-type enzyme. The stability of the mutant with the N-terminus deleted up to Glu43 was not affected by the down-regulation of 14-3-3η. These results suggest that the 14-3-3η protein regulates hTH1 stability by acting on the N-terminus.

Original languageEnglish
Pages (from-to)817-821
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume363
Issue number3
DOIs
Publication statusPublished - 23-11-2007

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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