کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1951799 | 1055791 | 2006 | 8 صفحه PDF | دانلود رایگان |
The EF-hand family of calcium-binding proteins regulates cellular signal transduction events via calcium-dependent interactions with target proteins. Here, we show that the COOH-terminal tail of the leech homolog of protein phosphatase 4 regulatory subunit 2 (PP4-R2) interacts with the small neuronal EF-hand calcium-binding protein, Calsensin, in a calcium-dependent manner. Using two-dimensional NMR spectroscopy and chemical shift perturbations we have identified and mapped the residues of Calsensin that form a binding surface for PP4-R2. We show that the binding groove is formed primarily of discontinuous hydrophobic residues located in helix 1, the hinge region, and helix 4 of the unicornate-type four helix structure of Calsensin. The findings suggest the possibility that calcium-dependent modulation of phosphatase complexes through interactions with small calcium-binding proteins may be a general mechanism for regulation of signal transduction pathways.
Journal: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research - Volume 1763, Issue 3, March 2006, Pages 322–329