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Kang, C.B.* ; Ye, H.* ; Chia, J.* ; Choi, B.H.* ; Dhe-Paganon, S.* ; Simon, B.* ; Schütz, U. ; Sattler, M. ; Yoon, H.S.*

Functional role of the flexible N-terminal extension of FKBP38 in catalysis.

Sci. Rep. 3:2985 (2013)
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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.
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Publication type Article: Journal article
Document type Scientific Article
Keywords N-15 Nmr Relaxation ; Steroid-receptor Complexes ; Fk506-binding Protein ; Fk-506 Binding-protein-38 ; Inhibits Apoptosis ; Backbone Dynamics ; Bcl-2 ; Domain ; Immunophilin ; Spectroscopy
Language english
Publication Year 2013
HGF-reported in Year 2013
ISSN (print) / ISBN 2045-2322
e-ISSN 2045-2322
Journal Scientific Reports
Quellenangaben Volume: 3, Issue: , Pages: , Article Number: 2985 Supplement: ,
Publisher Nature Publishing Group
Publishing Place London
Reviewing status Peer reviewed
Institute(s) Institute of Structural Biology (STB)
POF-Topic(s) 30203 - Molecular Targets and Therapies
Research field(s) Enabling and Novel Technologies
PSP Element(s) G-503000-001
PubMed ID 24145868
DOI 10.1038/srep02985
WOS ID WOS:000325926300001
Scopus ID 84886561469
Erfassungsdatum 2013-11-08
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