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Title: Functional role of the flexible N-terminal extension of FKBP38 in catalysis
Authors: Yoon, Ho Sup
Choi, Bo-Hwa
Kang, CongBao
Ye, Hong
Chia, Joel
Dhe-Paganon, Sirano
Simon, Bernd
Schütz, Ulrike
Sattler, Michael
Keywords: DRNTU::Science::Biological sciences
Issue Date: 2013
Source: Kang, C., Ye, H., Chia, J., Choi, B.-H., Dhe-Paganon, S., Simon, B., et al. (2013). Functional role of the flexible N-terminal extension of FKBP38 in catalysis. Scientific reports, 3, 1-8.
Series/Report no.: Scientific reports
Abstract: FKBP38 regulates apoptosis through unique interactions with multiple regulators including Bcl-2. Interestingly, the peptidylprolyl isomerase activity of FKBP38 is only detectable when it binds to calcium-saturated calmodulin (CaM/Ca2+). This, in turn, permits the formation of a complex with Bcl-2. FKBP38 thereby provides an important link between isomerase activity and apoptotic pathways. Here, we show that the N-terminal extension (residues 1-32) preceding the catalytic domain of FKBP38 has an autoinhibitory activity. The core isomerase activity of FKBP38 is inhibited by transient interactions involving the flexible N-terminal extension that precedes the catalytic domain. Notably, CaM/Ca2+ binds to this N-terminal extension and thereby releases the autoinhibitory contacts between the N-terminal extension and the catalytic domain, thus potentiating the isomerase activity of FKBP38. Our data demonstrate how CaM/Ca2+ modulates the catalytic activity of FKBP38.
ISSN: 2045-2322
DOI: 10.1038/srep02985
Schools: School of Biological Sciences 
Rights: © 2013 The Authors. This paper was published in Scientific Reports and is made available as an electronic reprint (preprint) with permission of the authors. The paper can be found at the following official DOI: []. One print or electronic copy may be made for personal use only. Systematic or multiple reproduction, distribution to multiple locations via electronic or other means, duplication of any material in this paper for a fee or for commercial purposes, or modification of the content of the paper is prohibited and is subject to penalties under law.
Fulltext Permission: open
Fulltext Availability: With Fulltext
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