|
KMID : 0613820110210010031
|
|
Journal of Life Science
2011 Volume.21 No. 1 p.31 ~ p.35
|
|
|
Characterization of a Dual-Specificity Protein Phosphatase, Human DUSP28
|
|
Jeong Dae-Gwin
Kim Song-Yi
Yun Jeong-Hun
Kim Jae-Hoon
|
|
|
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, Zn2+ 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.
|
|
|
KEYWORD
|
|
|
Dual-specificity protein phosphatase 28, recombinant protein, 6, 8-difluoro-4-methylumbelliferyl phosphate, phosphatase activity, inhibitors
|
|
|
FullTexts / Linksout information
|
|
|
|
|
|
Listed journal information
|
|
|
|