Journal of Life Science (생명과학회지)

Korean Society of Life Science (한국생명과학회)
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Characterization of a Dual-Specificity Protein Phosphatase, Human DUSP28

인간유래의 dual-specificity protein phosphatase, DUSP28의 활성분석

  • Jeong, Dae-Gwin (Medical Genomics Research Center, Korea Research Institute of Bioscience and Biotechnology) ;
  • Kim, Song-Yi (Medical Genomics Research Center, Korea Research Institute of Bioscience and Biotechnology) ;
  • Yun, Jeong-Hun (Faculty of Biotechnology, College of Applied Life Science, Jeju National University) ;
  • Kim, Jae-Hoon (Faculty of Biotechnology, College of Applied Life Science, Jeju National University)
  • 정대균 (한국생명공학연구원 단백체의학연구센터) ;
  • 김송이 (한국생명공학연구원 단백체의학연구센터) ;
  • 윤정훈 (제주대학교 생명공학부) ;
  • 김재훈 (제주대학교 생명공학부)
  • Received : 2010.11.10
  • Accepted : 2010.12.07
  • Published : 2011.01.30
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Abstract

Dual-specificity protein phosphatases (DUSPs) constitute a family of protein phosphatase characterized by the ability to dephosphorylate phospho-tyrosyl and phospho-seryl/threonyl residues. Most DUSPs are involved in regulation of cell survival and differentiation. In this study, a human dual-specificity protein phosphatase, DUSP28, was isolated from a human kidney cDNA. The recombinant protein was successfully produed in E.coli and showed sufficient phosphatase activity toward DiFMUP (6,8-difluoro-4-methylumbelliferyl phosphate). Various phosphatase inhibitors and divalent metals were tested for their effects on the DUSP28 phosphatase activity. As a result, $Zn^{2+}$ was found to strongly inhibit DUSP28 phosphatase activity, suggesting DUSP28 is involved in Zn-related signal transduction pathway. Furthermore, the DUSP28 protein preferred phospho-tyrosyl residues to phospho-threonyl residues, implying its physiological roles in the cellular process.

Dual-specificity protein phosphatase (DUSP)들은 인산화된 티로신 잔기와 인산화된 세린 또는 트레오닌 잔기를 탈인산화시키는 단백질 탈인산화효소 군을 이루고 있으며, 대부분의 DUSP들은 세포의 생존이나 분화에 관여하고 있다. 본 연구에서는 잘 알려지지 않은 인간 유래의 dual-specificity protein phosphatase인 DUSP28을 인간신장 cDNA에서 분리하였다. 대장균에서 생산된 재조합단백질은 6,8-difluoro-4-methylumbelliferyl phosphate (DiFMUP)에 대하여 좋은 활성을 보였다. 다양한 저해제와 2가 금속이온들이 DUSP28의 활성에 미치는 영향을 조사하였다. 다른 DUSP들에서와는 다르게, $Zn^{2+}$은 DUSP28의 탈인산화활성을 강하게 억제하였다. 이러한 결과로부터 DUSP28이 Zn과 연관된 신호전달경로에 관여할 것으로 추정된다. 더욱이, DUSP28은 인산화된 티로신잔기를 더욱 선호하는 경향이 있는 것으로 나타났고, 이는 세포 내에서도 비슷한 작용을 할 것으로 예상된다.

Keywords

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