Linked Life Data

17942410

Source:http://linkedlifedata.com/resource/pubmed/id/17942410

Statements in which the resource exists.
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pubmed-article:17942410pubmed:dateCreated2007-12-10lld:pubmed
pubmed-article:17942410pubmed:abstractTextThe 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.lld:pubmed
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pubmed-article:17942410pubmed:dateRevised2008-5-15lld:pubmed
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pubmed-article:17942410pubmed:year2007lld:pubmed
pubmed-article:17942410pubmed:articleTitleA novel calmodulin-Ca2+ target recognition activates the Bcl-2 regulator FKBP38.lld:pubmed
pubmed-article:17942410pubmed:affiliationMax Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, D-06120 Halle/Saale, Germany. edlich@enzyme-halle.mpg.delld:pubmed
pubmed-article:17942410pubmed:publicationTypeJournal Articlelld:pubmed
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