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Title 

A critical step for JNK activation: isomerization by the prolyl isomerase Pin1

 

정크 활성화에 중요한 단계인 핀1에의한 이성체화

Authors 

J E ParkJ A LeeSung Goo ParkD H LeeSeung Jun KimH J KimC UchidaT UchidaByoung Chul ParkS Cho

Publisher 

Nature Publishing Group

Issue Date 

2012

Citation 

Cell Death and Differentiation, vol. 19, no. 1, pp. 153-161

Keywords 

apoptosisc-Jun N-terminal kinasepeptidyl-prolyl cis/trans-isomerase

Abstract 

c-Jun N-terminal kinase (JNK) is activated by dual phosphorylation of both threonine and tyrosine residues in the phosphorylation loop of the protein in response to several stress factors. However, the precise molecular mechanisms for activation after phosphorylation remain elusive. Here we show that Pin1, a peptidyl-prolyl isomerase, has a key role in the JNK1 activation process by modulating a phospho-Thr-Pro motif in the phosphorylation loop. Pin1 overexpression in human breast cancer cell lines correlates with increased JNK activity. In addition, small interfering RNA (siRNA) analyses showed that knockdown of Pin1 in a human breast cancer cell line decreased JNK1 activity. Pin1 associates with JNK1, and then catalyzes prolyl isomerization of the phospho-Thr-Pro motif in JNK1 from trans- to cis-conformation. Furthermore, Pin1 enhances the association of JNK1 with its substrates. As a result, Pin1 -/- cells are defective in JNK activation and resistant to oxidative stress. These results provide novel insights that, following stress-induced phosphorylation of Thr in the Thr-Pro motif of JNK1, JNK1 associates with Pin1 and undergoes conformational changes to promote the binding of JNK1 to its substrates, resulting in cellular responses from extracellular signals.Cell Death and Differentiation advance online publication, 10 June 2011; doi:10.1038/cdd.2011.82.

ISSN 

1350-9047

Link 

http://dx.doi.org/10.1038/cdd.2011.82

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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