Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/94816
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dc.contributor.authorKang, Cong Baoen
dc.contributor.authorFeng, Linen
dc.contributor.authorChia, Joelen
dc.contributor.authorYoon, Ho Supen
dc.date.accessioned2012-10-30T04:12:02Zen
dc.date.accessioned2019-12-06T19:02:50Z-
dc.date.available2012-10-30T04:12:02Zen
dc.date.available2019-12-06T19:02:50Z-
dc.date.copyright2005en
dc.date.issued2005en
dc.identifier.citationKang, 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.en
dc.identifier.issn0006-291Xen
dc.identifier.urihttps://hdl.handle.net/10356/94816-
dc.identifier.urihttp://hdl.handle.net/10220/8825en
dc.description.abstractThe 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.en
dc.language.isoenen
dc.relation.ispartofseriesBiochemical and biophysical research communicationsen
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].en
dc.subjectDRNTU::Science::Biological sciencesen
dc.titleMolecular characterization of FK-506 binding protein 38 and its potential regulatory role on the anti-apoptotic protein Bcl-2en
dc.typeJournal Articleen
dc.contributor.schoolSchool of Biological Sciencesen
dc.identifier.doihttp://dx.doi.org/10.1016/j.bbrc.2005.09.023en
dc.description.versionAccepted versionen
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