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BCL2 — FKBP8

Pathways - manually collected, often from reviews:

• 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)
  Kang et al., FEBS Lett 2005*, Weiwad et al., FEBS Lett 2005
  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)
  Kang et al., FEBS Lett 2005*, Weiwad et al., FEBS Lett 2005
  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)
  Kang et al., FEBS Lett 2005*, Weiwad et al., FEBS Lett 2005
  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)
  Kang et al., FEBS Lett 2005*, Weiwad et al., FEBS Lett 2005
  Evidence: mutant phenotype, physical interaction

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: BCL2 — FKBP8 (direct interaction, pull down) Kang et al., FEBS Lett 2005*
• IRef Biogrid Interaction: BCL2 — FKBP8 (direct interaction, two hybrid) Kang et al., FEBS Lett 2005*
• IRef Biogrid Interaction: BCL2 — FKBP8 (physical association, affinity chromatography technology) Edlich et al., EMBO J 2005
• IRef Biogrid Interaction: BCL2 — FKBP8 (direct interaction, pull down) Edlich et al., EMBO J 2005
• IRef Biogrid Interaction: BCL2 — FKBP8 (direct interaction, far western blotting) Edlich et al., J Biol Chem 2007*
• IRef Biogrid Interaction: BCL2 — FKBP8 (physical association, affinity chromatography technology) Edlich et al., J Biol Chem 2007*
• IRef Biogrid Interaction: BCL2 — FKBP8 (physical association, affinity chromatography technology) Shirane et al., Nat Cell Biol 2003*
• IRef Biogrid Interaction: BCL2 — FKBP8 (direct interaction, pull down) Edlich et al., J Biol Chem 2007
• MIPS CORUM CALM1-FKBP38-BCL2 complex: CALM1-FKBP38-BCL2 complex complex (BCL2-CALM2-CALM3-CALM1-FKBP8) Edlich et al., EMBO J 2005
• IRef Corum Interaction: Complex of BCL2-CALM1-FKBP8 (association, coimmunoprecipitation) Edlich et al., EMBO J 2005
• IRef Hprd Interaction: BCL2 — FKBP8 (two hybrid) Shirane et al., Nat Cell Biol 2003*
• IRef Hprd Interaction: BCL2 — FKBP8 (in vitro) Shirane et al., Nat Cell Biol 2003*
• IRef Hprd Interaction: BCL2 — FKBP8 (in vivo) Shirane et al., Nat Cell Biol 2003*
• IRef Innatedb Interaction: FKBP8 — BCL2 (unknown, -) Shirane et al., Nat Cell Biol 2003*
• IRef Innatedb Interaction: FKBP8 — BCL2 (unknown, -) Edlich et al., J Biol Chem 2007*
• IRef Innatedb Interaction: FKBP8 — BCL2 (unknown, -) Kang et al., FEBS Lett 2005*
• IRef Intact Interaction: FKBP8 — BCL2 (physical association, imaging technique) Kang et al., FEBS Lett 2005*
• IRef Intact Interaction: FKBP8 — BCL2 (physical association, two hybrid) Kang et al., FEBS Lett 2005*
• IRef Ophid Interaction: FKBP8 — BCL2 (aggregation, confirmational text mining) Shirane et al., Nat Cell Biol 2003*
• IRef Ophid Interaction: FKBP8 — BCL2 (aggregation, interologs mapping) Brown et al., Bioinformatics 2005

Text-mined interactions from Literome

Kang et al., Biochem Biophys Res Commun 2005 : Molecular characterization of FK-506 binding protein 38 and its potential regulatory role on the anti-apoptotic protein Bcl-2 ... Lastly, to investigate the effect of FKBP38 on Bcl-2 , we suppressed FKBP38 by RNA interference ( RNAi ) of FKBP38
Edlich et al., J Biol Chem 2007 : The direct interaction between FKBP38 and Bcl-2 , however, requires a prior activation of FKBP38 by the Ca2+ sensor calmodulin (CaM) ... Only the latter interaction between the catalytic FKBP38 domain and the N-terminal CaM domain activates FKBP38 and, as a consequence, also regulates Bcl-2
Ma et al., J Biol Chem 2010 : In addition to the role in mTOR regulation, FKBP38 is also involved in binding and recruiting Bcl-2 and Bcl-X ( L ), two anti-apoptotic proteins, to mitochondria
Choi et al., J Biol Chem 2010 : We demonstrated that the FKBP38 mediated Bcl-2 stability is specific as the levels of other anti-apoptotic proteins such as Bcl-X ( L ) and Mcl-1 remained unaffected
Maestre-Martínez et al., Biol Chem 2010 : The human FK506 binding protein 38 (FKBP38) regulates Bcl-2 in neuronal apoptosis