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Title 

PTP inhibitor IV protects JNK kinase activity by inhibiting dual-specificity phosphatase 14 (DUSP14)

Authors 

Jae Eun ParkByoung Chul ParkM SongSung Goo ParkD H LeeS Y ParkJ H KimS Cho

Publisher 

Elsevier

Issue Date 

2009

Citation 

Biochemical and Biophysical Research Communications, vol. 387, no. 4, pp. 795-799

Keywords 

DUSP14JNKPTP inhibitor IV

Abstract 

Protein phosphorylation plays critical roles in the regulation of protein activity and cell signaling. The level of protein phosphorylation is controlled by protein kinases and protein tyrosine phosphatases (PTPs). Disturbance of the equilibrium between protein kinase and PTP activities results in abnormal protein phosphorylation, which has been linked to the etiology of several diseases, including cancer. In this study, we screened protein tyrosine phosphatases (PTPs) by in vitro phosphatase assays to identify PTPs that are inhibited by bis (4-trifluoromethyl-sulfonamidophenyl, TFMS)-1,4-diisopropylbenzene (PTP inhibitor IV). PTP inhibitor IV inhibited DUSP14 phosphatase activity. Kinetic studies with PTP inhibitor IV and DUSP14 revealed a competitive inhibition, suggesting that PTP inhibitor IV binds to the catalytic site of DUSP14. PTP inhibitor IV effectively and specifically inhibited DUSP14-mediated dephosphorylation of JNK, a member of the mitogen-activated protein kinase (MAPK) family.

ISSN 

0006-291X

Link 

http://dx.doi.org/10.1016/j.bbrc.2009.07.127

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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