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Updated: Oct 18, 2026

Measuring Spatial and Temporal Ca2+ Signals in Arabidopsis Plants
Published on: September 2, 2014
Dimerization of Arabidopsis 14-3-3 proteins: structural requirements within the N-terminal domain and effect of
D Abarca1, F Madueño, J M Martínez-Zapater
1Departamento de Mejora Genética y Biotecnología, INIA, Madrid, Spain.
Abstract:
The structural requirements for dimerization of RCI14A and RCI14B, two 14-3-3 isoforms from Arabidopsis thaliana, have been analyzed by testing truncated forms of RCI14A for dimerization with full-length RCI14A and RCI14B. The results show that only the fourth helix of the truncated partner is essential for dimerization, which represents a difference from what is known for animal isoforms. On the other hand, the effect of calcium has been tested in RCI14A homodimerization. Millimolar concentrations of calcium exert a negative, dose-dependent effect that involves the C-terminal domain of RCI14A and might modulate interactions with other cellular components or among Arabidopsis 14-3-3 isoforms.
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