Gene interactions and pathways from curated databases and text-mining
J Biol Chem 2007, PMID: 17942410

A novel calmodulin-Ca2+ target recognition activates the Bcl-2 regulator FKBP38.

Edlich, Frank; Maestre-Martínez, Mitcheell; Jarczowski, Franziska; Weiwad, Matthias; Moutty, Marie-Christine; Malesević, Miroslav; Jahreis, Günther; Fischer, Gunter; Lücke, Christian

The FK506-binding protein 38 (FKBP38) affects neuronal apoptosis control by suppressing the anti-apoptotic function of Bcl-2. The direct interaction between FKBP38 and Bcl-2, however, requires a prior activation of FKBP38 by the Ca2+ sensor calmodulin (CaM). Here we demonstrate for the first time that the formation of a complex between FKBP38 and CaM-Ca2+ involves two separate interaction sites, thus revealing a novel scenario of target protein regulation by CaM-Ca2+. The C-terminal FKBP38 residues Ser290-Asn313 bind to the target protein-binding cleft of the Ca2+-coordinated C-terminal CaM domain, thereby enabling the N-terminal CaM domain to interact with the catalytic domain of FKBP38 in a Ca2+-independent manner. 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.

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Text Mining Data

FKBP38 → calmodulin-Ca2+: " A novel calmodulin-Ca2+ target recognition activates the Bcl-2 regulator FKBP38 "

FKBP38 → calmodulin-Ca2+: " A novel calmodulin-Ca2+ target recognition activates the Bcl-2 regulator FKBP38 "

calmodulin (CaM) → FKBP38: " The direct interaction between FKBP38 and Bcl-2, however, requires a prior activation of FKBP38 by the Ca2+ sensor calmodulin (CaM) "

calmodulin (CaM) → Bcl-2: " The direct interaction between FKBP38 and Bcl-2 , however, requires a prior activation of FKBP38 by the Ca2+ sensor calmodulin (CaM) "

FKBP38 → Bcl-2: " The direct interaction between FKBP38 and Bcl-2 , however, requires a prior activation of FKBP38 by the Ca2+ sensor calmodulin (CaM) "

Bcl-2 — FKBP38: " 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 "

Manually curated Databases

  • IRef Biogrid Interaction: BCL2 — FKBP8 (direct interaction, far western blotting)
  • IRef Biogrid Interaction: BCL2 — FKBP8 (physical association, affinity chromatography technology)
  • IRef Biogrid Interaction: FKBP8 — CALM1 (association, x-ray crystallography)
  • IRef Biogrid Interaction: FKBP8 — CALM1 (direct interaction, pull down)
  • IRef Innatedb Interaction: FKBP8 — BCL2 (unknown, -)
  • IRef Innatedb Interaction: FKBP8 — CALM1 (unknown, -)
In total, 2 gene pairs are associated to this article in curated databases