The flexible loop of Bcl-2 is required for molecular interaction with immunosuppressant FK-506 binding protein 38 (FKBP38)

Bcl-2 contains an unusually long loop between the first and the second helices. This loop has been shown to be highly flexible based on NMR and X-ray crystallographic analyses of this region. Bcl-2 is regulated at the posttranslational level through phosphorylation of specific residues within the fl...

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Main Authors:	Kang, Cong Bao, Tai, Jeff, Chia, Joel, Yoon, Ho Sup
Other Authors:	School of Biological Sciences
Format:	Article
Language:	English
Published:	2012
Subjects:	DRNTU::Science::Biological sciences
Online Access:	https://hdl.handle.net/10356/95126 http://hdl.handle.net/10220/8822
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Institution:	Nanyang Technological University
Language:	English

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spelling	sg-ntu-dr.10356-951262023-02-28T17:03:51Z The flexible loop of Bcl-2 is required for molecular interaction with immunosuppressant FK-506 binding protein 38 (FKBP38) Kang, Cong Bao Tai, Jeff Chia, Joel Yoon, Ho Sup School of Biological Sciences DRNTU::Science::Biological sciences Bcl-2 contains an unusually long loop between the first and the second helices. This loop has been shown to be highly flexible based on NMR and X-ray crystallographic analyses of this region. Bcl-2 is regulated at the posttranslational level through phosphorylation of specific residues within the flexible loop. The biological role and posttranslational modifications of the loop of Bcl-2 is currently unclear. FK-506 binding protein 38 (FKBP38) has been reported to interact with Bcl-2, suggesting that FKBP38 could act as a docking molecule to localize Bcl-2 at the mitochondrial membrane [Shirane, M. and Nakayama, K.I. (2003) Inherent calcineurin inhibitor FKBP38 targets Bcl-2 to mitochondria and inhibits apoptosis. Nat. Cell Biol. 5, 28-37]. Here, we investigated the molecular interaction between FKBP38 and Bcl-2, and demonstrated that Bcl-2 interacts with FKBP38 through the unstructured loop, and the interaction appears to regulate phosphorylation in the loop of Bcl-2. Accepted version 2012-10-29T09:06:36Z 2019-12-06T19:08:45Z 2012-10-29T09:06:36Z 2019-12-06T19:08:45Z 2005 2005 Journal Article Kang, C. B., Tai, J., Chia, J., & Yoon, H. S. (2005). The flexible loop of Bcl-2 is required for molecular interaction with immunosuppressant FK-506 binding protein 38 (FKBP38). FEBS Letters, 579(6), 1469-1476. 0014-5793 https://hdl.handle.net/10356/95126 http://hdl.handle.net/10220/8822 10.1016/j.febslet.2005.01.053 en FEBS letters © 2005 Federation of Europian Biochemical Societies. This is the author created version of a work that has been peer reviewed and accepted for publication in FEBS Letters, published by Elsevier B.V. on behalf of Federation of Europian Biochemical Societies. 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.febslet.2005.01.053]. application/pdf
institution	Nanyang Technological University
building	NTU Library
continent	Asia
country	Singapore Singapore
content_provider	NTU Library
collection	DR-NTU
language	English
topic	DRNTU::Science::Biological sciences
spellingShingle	DRNTU::Science::Biological sciences Kang, Cong Bao Tai, Jeff Chia, Joel Yoon, Ho Sup The flexible loop of Bcl-2 is required for molecular interaction with immunosuppressant FK-506 binding protein 38 (FKBP38)
description	Bcl-2 contains an unusually long loop between the first and the second helices. This loop has been shown to be highly flexible based on NMR and X-ray crystallographic analyses of this region. Bcl-2 is regulated at the posttranslational level through phosphorylation of specific residues within the flexible loop. The biological role and posttranslational modifications of the loop of Bcl-2 is currently unclear. FK-506 binding protein 38 (FKBP38) has been reported to interact with Bcl-2, suggesting that FKBP38 could act as a docking molecule to localize Bcl-2 at the mitochondrial membrane [Shirane, M. and Nakayama, K.I. (2003) Inherent calcineurin inhibitor FKBP38 targets Bcl-2 to mitochondria and inhibits apoptosis. Nat. Cell Biol. 5, 28-37]. Here, we investigated the molecular interaction between FKBP38 and Bcl-2, and demonstrated that Bcl-2 interacts with FKBP38 through the unstructured loop, and the interaction appears to regulate phosphorylation in the loop of Bcl-2.
author2	School of Biological Sciences
author_facet	School of Biological Sciences Kang, Cong Bao Tai, Jeff Chia, Joel Yoon, Ho Sup
format	Article
author	Kang, Cong Bao Tai, Jeff Chia, Joel Yoon, Ho Sup
author_sort	Kang, Cong Bao
title	The flexible loop of Bcl-2 is required for molecular interaction with immunosuppressant FK-506 binding protein 38 (FKBP38)
title_short	The flexible loop of Bcl-2 is required for molecular interaction with immunosuppressant FK-506 binding protein 38 (FKBP38)
title_full	The flexible loop of Bcl-2 is required for molecular interaction with immunosuppressant FK-506 binding protein 38 (FKBP38)
title_fullStr	The flexible loop of Bcl-2 is required for molecular interaction with immunosuppressant FK-506 binding protein 38 (FKBP38)
title_full_unstemmed	The flexible loop of Bcl-2 is required for molecular interaction with immunosuppressant FK-506 binding protein 38 (FKBP38)
title_sort	flexible loop of bcl-2 is required for molecular interaction with immunosuppressant fk-506 binding protein 38 (fkbp38)
publishDate	2012
url	https://hdl.handle.net/10356/95126 http://hdl.handle.net/10220/8822
_version_	1759856556923420672

The flexible loop of Bcl-2 is required for molecular interaction with immunosuppressant FK-506 binding protein 38 (FKBP38)

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