Skip Navigation



Journal of Biochemistry Advance Access published online on November 3, 2009
Journal of Biochemistry, doi:10.1093/jb/mvp178
This Article
Right arrow Advance Access manuscript (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Huang, Y.-C.
Right arrow Articles by Lin, T.-H.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Huang, Y.-C.
Right arrow Articles by Lin, T.-H.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.

The effect of PKA-Phosphorylation on the structure of inhibitor-1 studied by NMR spectroscopy

Yi-Choang Huang1,2,3, Yi-Chen Chen4, Huey-Jen Tsay5, Chia-lin Chyan6, Chun-Yu Chen7, Hsien-bin Huang7,* and Ta-Hsien Lin1,2,3,*

1Institute of Biochemistry and Molecular Biology, 2Structural Biology Program, 5Institute of Neuroscience, National Yang-Ming University, Taipei 112, Taiwan, R. O. C.
3Department of Medical Research & Education, Taipei Veterans General Hospital, Taipei 112, Taiwan, R.O.C.
4Institute of Medical Science, Tzu Chi University, Hualien 970, Taiwan, R.O.C.
6Department of Chemistry, National Dong Hwa University, Hualien 974, Taiwan, R.O.C.
7Department of Life Science and Institute of Molecular Biology, National Chung Cheng University, Chia-Yi 621, Taiwan, R.O.C.

*To whom correspondence should be addressed Hsien-bin Huang, Department of Life Science and Institute of Molecular Biology, National Chung Cheng University, Chia-Yi, Taiwan; Fax: +886-5-2722871; Email: biohbh{at}ccu.edu.tw and Ta-Hsien Lin, Department of Medical Research & Education, Taipei Veterans General Hospital, Taipei, Taiwan; Fax: +886-2-8751562; Email: thlin{at}vghtpe.gov.tw

Received July 6, 2009; Accepted October 5, 2009


  Abstract

Inhibitor-1 is an acid- and heat-stable protein. It can be turned into a potent inhibitor of protein phosphatase-1 (PP1) after phosphorylation at Thr35 by c-AMP-dependent protein kinase (PKA). Although it has been known that pre-phosphorylation is essential for inhibition of PP1, the structure-function relationship of Thr35-phosphorylated inhibitor-1, such as whether or not PKA-phosphorylation pre-triggers conformational changes in inhibitor-1, remains unclear. In this study, we performed structural characterization of Thr35-phosphoroylated inhibitor-1 by using multi-dimensional heternuclear NMR spectroscopy. The result of structural comparison between Thr35-phosphoroylated and non-phosphorylated inhibitor-1 indicated that PKA-phosphorylation has no significant effect on the global conformation of free state inhibitor-1. This finding may support the inference that regulation of the interactions between inhibitor-1 and PP1 through PKA-phosphorylation mainly depends on the phosphate group instead of phosphorylation-induced conformational change.

Key Words: inhibitor-1, phosphorylation, protein phosphatase-1, PKA, NMR


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.