Demonstration of different metal ion-induced calcineurin conformations using a monoclonal antibody.

  title={Demonstration of different metal ion-induced calcineurin conformations using a monoclonal antibody.},
  author={H. Matsui and C. Pallen and A. Adachi and J. Wang and P. H. Lam},
  journal={The Journal of biological chemistry},
  volume={260 7},
It has been suggested that calcineurin, a calmodulin-stimulated phosphatase, may exist in different metal ion-dependent conformational states (Pallen, C.J., and Wang, J. H. (1984) J. Biol. Chem. 259, 6134-6141). Evidence in favor of this hypothesis comes from studies involving a monoclonal antibody, VA1, which is specific for the small (beta) subunit of calcineurin. This antibody inhibits Ni2+-stimulated but not Mn2+-stimulated phosphatase activity against p-nitrophenyl phosphate and… Expand
Survey of calcineurin activity towards nonprotein compounds and identification of phosphoenol pyruvate as a substrate.
The results suggest that functional roles of calcineurin may include actions of the enzyme toward nonprotein phosphocompounds. Expand
Differences between Mg(2+) and transition metal ions in the activation of calcineurin.
Circular dichroism showed that metal ions increased the alpha-helical content of calcineurin, but little significant differences in the spectra were identified between using activating and nonactivating metal ions. Expand
Function and structure of recombinant single chain calcineurin.
The findings suggested that the fusion of A and B subunits of calcineurin does not affect their folding pathways and structural changes involved in their function, furthermore, they are bound to the correct binding site. Expand
Occurrence of a para-nitrophenyl phosphate-phosphatase with calcineurin-like characteristics in Paramecium tetraurelia.
The data support the existence of both subunits of a CaN-like phosphatase in Paramecium cells, and strongly suggests that, in the absence of Ca2+, both sub Units A and B were separated either before or during chromatographic processing. Expand
The role of the autoinhibitory domain in differential metal ion activation of calmodulin‐stimulated phosphatase
An autoinhibitory domain previously implicated in the conformation transition of CaM stimulation of the phosphatase is shown to participate in defining the differential metal ion activation. Expand
Calcineurin-mediated dephosphorylation of the human placental membrane receptor for epidermal growth factor urogastrone.
The enzymatic properties and comparative abundance of calcineurin in the placenta membranes suggest that this enzyme may play an important role in regulating the phosphorylation state of those receptors also known to be present in the membranes. Expand
Selective activation of calcineurin by dipicolinic acid.
  • B. Martin
  • Chemistry, Medicine
  • Archives of biochemistry and biophysics
  • 1997
Atomic absorption spectrometry analysis showed no loss of iron or zinc from calcineurin after activation (2 h) by dipicolinic acid, and incubated with 1.0 mM Mn2+ (saturating levels) also did not show any loss of intrinsic metal by atomic absorption analysis. Expand
Ca2+/calmodulin-dependent protein phosphatase in bovine parotid gland: purification and characterization.
Calmodulin-dependent protein phosphatase (CaM-PPase) was isolated from bovine parotid gland by sequential application of DEAE-52, Affi-gel blue and calmodulin-affinity chromatography followed by gelExpand
Resolution of bovine brain calcineurin subunits: stimulatory effect of subunit B on subunit A phosphatase activity
The results support the view that subunit B plays an important role in Mn2+/calmodulin regulation of subunit A phosphatase activity and lend further support to the earlier postulate that Mn2- is a powerful regulator of calcineurin phosphatases. Expand
High Activity of the Calcineurin A Subunit with a V314 Deletion
It is proposed that the change of the activity and function of V314 is due to conformational changes of calcineurin to benefit the binding of, or stimulation by, Mn2+, or to affect the interaction between the A and B subunits. Expand