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- W2028108889 abstract "Calcineurin (CaN) is a heterodimeric Ser/Thr phosphatase. Calcineurin regulates diverse biological functions, from T-cell activation to critical events in early heart development. The enzymatic activity of the A subunit (CaNA) is regulated by direct binding of Ca2+ to its B subunit (CaNB), and Ca2+ binding of the two-domain calcium-binding protein calmodulin (CaM) that is required for full activity. CaNA contains an auto-inhibitory domain that prevents full activation of CaN even when CaNB is Ca2+ saturated. Interactions between CaM and CaN occur through a CaM-binding domain (CaMBD). This sequence (391-414 of α CaNA) is a BAA-motif (basic amphipathic alpha-helix) in a region that becomes disordered when CaNB binds calcium. (Ca2+)4-CaM has picomolar affinity for CaN, as determined by thermodynamic linkage (O'Donnell et al, Proteins 2011). The Creamer Lab (Rumi-Masante et al, JMB 2012) has shown that CaM-binding induces secondary structuring of the full regulatory region of CaNA that extends beyond this CaMBD. We have also determined that calcium binding to CaM bound to the CaMBD is sequential, with the C-domain sites saturating at lower calcium than the N-domain sites. Thus, we are investigating a hypothesis that the mechanism of calcium-induced activation of CaN requires at least three steps that utilize the two domains of CaM (N and C) differently. We are using “knockout” mutants of CaM with modifications in one or more calcium-binding sites, and monitoring their binding to biosensor proteins containing the CaMBD embedded between auto-fluorescent proteins. Without CaM binding the fluorescent proteins undergo FRET, while CaM binding to the BAA motif reduces FRET efficiency and allows calculations to be made on CaM-biosensor interaction kinetics. We will report domain-specific effects of these mutations on recognition of this region. Support: NIH R01 GM57001, UI Helen Johnson Scholar Award, American Heart Association 12GRNT12050395." @default.
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- W2028108889 date "2013-01-01" @default.
- W2028108889 modified "2023-09-28" @default.
- W2028108889 title "Regulation of Calcineurin by Domain-Specific Interactions with Calmodulin" @default.
- W2028108889 doi "https://doi.org/10.1016/j.bpj.2012.11.590" @default.
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