mirage

Molecular characterization of FK-506 binding protein 38 and its potential regulatory role on the anti-apoptotic protein Bcl-2

DSpace/Manakin Repository

 

Search DR-NTU


Advanced Search Subject Search

Browse

My Account

Molecular characterization of FK-506 binding protein 38 and its potential regulatory role on the anti-apoptotic protein Bcl-2

Show simple item record

dc.contributor.author Kang, Cong Bao
dc.contributor.author Feng, Lin
dc.contributor.author Chia, Joel
dc.contributor.author Yoon, Ho Sup
dc.date.accessioned 2012-10-30T04:12:02Z
dc.date.available 2012-10-30T04:12:02Z
dc.date.copyright 2005
dc.date.issued 2012-10-30
dc.identifier.citation Kang, C. B., Feng, L., Chia, J., & Yoon, H. S. (2005). Molecular characterization of FK-506 binding protein 38 and its potential regulatory role on the anti-apoptotic protein Bcl-2. Biochemical and Biophysical Research Communications, 337(1), 30-38.
dc.identifier.issn 0006-291X
dc.identifier.uri http://hdl.handle.net/10220/8825
dc.description.abstract The immunosuppressant FK-506 binding protein 38 (FKBP38) is localized at the mitochondrial membrane and appears to play an important role in apoptosis. Recent reports about the potential functions of FKBP38 in apoptosis appear to be controversial. To further understand the biological function of FKBP38, here, we studied its molecular characteristics and a potential regulatory role on the anti-apoptotic protein Bcl-2. Our results suggest that FKBP38 appears to show chaperone activities in the citrate synthase aggregation assays during thermal denaturation and affect solubility of Bcl-2 when they are co-expressed. The FKBP family proteins bind the immunosuppressive drug FK-506 through the FK-506 binding domain and consequently inhibit the activity of calcineurin. In this study, from our NMR studies and calcineurin assays in vitro, we demonstrate that the N-terminal fragment of FKBP38 which contains the FK-506 binding domain does not bind FK-506 at molecular level. Lastly, to investigate the effect of FKBP38 on Bcl-2, we suppressed FKBP38 by RNA interference (RNAi) of FKBP38. Our results suggest that the suppression of FKBP38 appears to make Bcl-2 unstable or unprotected from degradation in an unknown mechanism.
dc.language.iso en
dc.relation.ispartofseries Biochemical and biophysical research communications
dc.rights © 2005 Elsevier Inc. This is the author created version of a work that has been peer reviewed and accepted for publication by Biochemical and Biophysical Research Communications, Elsevier Inc. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [http://dx.doi.org/10.1016/j.bbrc.2005.09.023].
dc.subject DRNTU::Science::Biological sciences.
dc.title Molecular characterization of FK-506 binding protein 38 and its potential regulatory role on the anti-apoptotic protein Bcl-2
dc.type Journal Article
dc.contributor.school School of Biological Sciences
dc.identifier.doi http://dx.doi.org/10.1016/j.bbrc.2005.09.023
dc.description.version Accepted version

Files in this item

Files Size Format View
31. Molecular c ... FK-506 binding protein.pdf 702.8Kb PDF View/Open

This item appears in the following Collection(s)

Show simple item record

Statistics

Total views

All Items Views
Molecular characterization of FK-506 binding protein 38 and its potential regulatory role on the anti-apoptotic protein Bcl-2 298

Total downloads

All Bitstreams Views
31. Molecular characterization of FK-506 binding protein.pdf 180

Top country downloads

Country Code Views
United States of America 68
China 48
Singapore 16
Taiwan 10
Japan 6

Top city downloads

city Views
Mountain View 47
Beijing 28
Singapore 15
Taipei 5
Redwood City 4

Downloads / month

  2014-07 2014-08 2014-09 total
31. Molecular characterization of FK-506 binding protein.pdf 0 0 8 8