FEBS Lett 2005,
PMID: 15733859
Kang, Cong Bao; Tai, Jeff; Chia, Joel; Yoon, Ho Sup
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.
Document information provided by NCBI PubMed
Text Mining Data
Dashed line = No text mining data
Manually curated Databases
-
IRef Biogrid Interaction:
BCL2
—
FKBP8
(direct interaction, pull down)
-
IRef Biogrid Interaction:
BCL2
—
FKBP8
(direct interaction, two hybrid)
-
IRef Biogrid Interaction:
BCL2
—
MAPK8
(direct interaction, enzymatic study)
-
IRef Innatedb Interaction:
FKBP8
—
BCL2
(unknown, -)
-
IRef Innatedb Interaction:
MAPK8
—
BCL2L1
(unknown, -)
-
IRef Innatedb Interaction:
MAPK8
—
BCL2
(unknown, -)
-
IRef Intact Interaction:
FKBP8
—
BCL2
(physical association, imaging technique)
-
IRef Intact Interaction:
FKBP8
—
BCL2
(physical association, two hybrid)
-
IRef Intact Interaction:
MAPK8
—
BCL2L1
(phosphorylation reaction, experimental interaction detection)
-
IRef Intact Interaction:
MAPK8
—
BCL2
(phosphorylation reaction, experimental interaction detection)
-
IRef Intact Interaction:
FKBP8
—
BCL2L1
(direct interaction, pull down)
-
NCI Pathway Database Role of Calcineurin-dependent NFAT signaling in lymphocytes:
CaM/Ca2+/Calcineurin A alpha-beta B1 complex (CALM2)
→
Calcineurin A alpha-beta B1/BCL2 complex (BCL2)
(modification, collaborate)
Evidence: mutant phenotype, physical interaction
-
NCI Pathway Database Role of Calcineurin-dependent NFAT signaling in lymphocytes:
CaM/Ca2+/Calcineurin A alpha-beta B1 complex (CALM2)
→
CaM/Ca2+/FKBP38 complex (CALM2-FKBP8)
(modification, collaborate)
Evidence: mutant phenotype, physical interaction
-
NCI Pathway Database Role of Calcineurin-dependent NFAT signaling in lymphocytes:
CaM/Ca2+/Calcineurin A alpha-beta B1 complex (CALM2)
→
FKBP38/BCL2 complex (FKBP8-BCL2)
(modification, collaborate)
Evidence: mutant phenotype, physical interaction
-
NCI Pathway Database Role of Calcineurin-dependent NFAT signaling in lymphocytes:
Calcineurin A alpha-beta B1/BCL2 complex (BCL2)
→
CaM/Ca2+/FKBP38 complex (CALM2-FKBP8)
(modification, collaborate)
Evidence: mutant phenotype, physical interaction
-
NCI Pathway Database Role of Calcineurin-dependent NFAT signaling in lymphocytes:
Calcineurin A alpha-beta B1/BCL2 complex (BCL2)
→
FKBP38/BCL2 complex (FKBP8-BCL2)
(modification, collaborate)
Evidence: mutant phenotype, physical interaction
-
NCI Pathway Database Role of Calcineurin-dependent NFAT signaling in lymphocytes:
CaM/Ca2+/FKBP38 complex (CALM2-FKBP8)
→
FKBP38/BCL2 complex (FKBP8-BCL2)
(modification, collaborate)
Evidence: mutant phenotype, physical interaction
In total, 9 gene pairs are associated to this article in curated databases