Gene interactions and pathways from curated databases and text-mining
EMBO J 2005, PMID: 15990872

Bcl-2 regulator FKBP38 is activated by Ca2+/calmodulin.

Edlich, Frank; Weiwad, Matthias; Erdmann, Frank; Fanghänel, Jörg; Jarczowski, Franziska; Rahfeld, Jens-Ulrich; Fischer, Gunter

FKBP-type peptidyl prolyl cis/trans isomerases (PPIases) are folding helper enzymes involved in the control of functional regrowth of damaged sciatic, cortical cholinergic, dopaminergic and 5-HT neurones. Here, we show that the constitutively inactive human FK506-binding protein 38 (FKBP38) is capable of responding directly to intracellular Ca2+ rise through formation of a heterodimeric Ca2+/calmodulin/FKBP38 complex. Only complex formation creates an enzymatically active FKBP, displaying affinity for Bcl-2 mediated through the PPIase site. Association between Bcl-2 and the active site of Ca2+/calmodulin/FKBP38 regulates Bcl-2 function and thereby participates in the promotion of apoptosis in neuronal tissues. FKBP38 proapoptotic function mediated by this interaction is abolished by either potent inhibitors of the PPIase activity of the Ca2+/calmodulin/FKBP38 complex or RNA interference-mediated depletion of FKBP38, promoting neuronal cell survival.

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Text Mining Data

Bcl-2 → Ca2+/calmodulin: " Bcl-2 regulator FKBP38 is activated by Ca2+/calmodulin "

Bcl-2 → Ca2+/calmodulin: " Bcl-2 regulator FKBP38 is activated by Ca2+/calmodulin "

FKBP38 → Ca2+/calmodulin/FKBP38: " FKBP38 proapoptotic function mediated by this interaction is abolished by either potent inhibitors of the PPIase activity of the Ca2+/calmodulin/FKBP38 complex or RNA interference mediated depletion of FKBP38 , promoting neuronal cell survival "

FKBP38 → Ca2+/calmodulin/FKBP38: " FKBP38 proapoptotic function mediated by this interaction is abolished by either potent inhibitors of the PPIase activity of the Ca2+/calmodulin/FKBP38 complex or RNA interference mediated depletion of FKBP38 , promoting neuronal cell survival "

FKBP38 → PPIase: " FKBP38 proapoptotic function mediated by this interaction is abolished by either potent inhibitors of the PPIase activity of the Ca2+/calmodulin/FKBP38 complex or RNA interference mediated depletion of FKBP38 , promoting neuronal cell survival "

Manually curated Databases

  • IRef Bind Interaction: FKBP8 — CALM1
  • IRef Bind_translation Interaction: FKBP8 — CALM1 (coimmunoprecipitation)
  • IRef Bind_translation Interaction: FKBP8 — CALM1 (affinity chromatography technology)
  • IRef Bind_translation Interaction: FKBP8 — CALM1 (experimental interaction detection)
  • IRef Bind_translation Interaction: BAD — BCL2 (coimmunoprecipitation)
  • IRef Bind_translation Interaction: BAD — BCL2 (affinity chromatography technology)
  • IRef Biogrid Interaction: BCL2 — FKBP8 (physical association, affinity chromatography technology)
  • IRef Biogrid Interaction: BCL2 — FKBP8 (direct interaction, pull down)
  • IRef Biogrid Interaction: FKBP8 — CALM1 (direct interaction, pull down)
  • IRef Biogrid Interaction: FKBP8 — CALM1 (physical association, affinity chromatography technology)
  • IRef Biogrid Interaction: BAD — BCL2 (physical association, affinity chromatography technology)
  • MIPS CORUM CALM1-FKBP38-BCL2 complex: CALM1-FKBP38-BCL2 complex complex (BCL2-CALM2-CALM3-CALM1-FKBP8)
  • IRef Corum Interaction: Complex of BCL2-CALM1-FKBP8 (association, coimmunoprecipitation)
In total, 11 gene pairs are associated to this article in curated databases