CML36 interacts directly with the regulative N terminus of the Arabidopsis plasma membrane Ca(2+)-ATPase isoform 8 (ACA8) and this interaction stimulates ACA8 activity
This study indicates that ACA10/8 and BON1 physically interact on plasma membrane and function in the generation of cytosol calcium signatures that are critical for stomatal movement and impact plant immunity.
This study identifies ACA8 as a prominent in vivo regulator of cellular Ca2+ dynamics and reveal the existence of a Ca2+-dependent CBL-CIPK-mediated regulatory feedback mechanism which crucially functions in the termination of Ca2+ signals.
complex between calmodulin and the regulatory domain of the plasma-membrane Ca(2+)-ATPase ACA8 from Arabidopsis has been crystallized. Crystals belonged to space group C2 with unit-cell parameters a = 176.8 b = 70.0 c = 69.8 A beta = 113.2 degrees.
Category
Structure, Family & Domains, Interaction, Structure, Structure
the cytosolic face of ACA8 mediates early CaM recognition and CaM subsequently competes with the intramolecular autoinhibitor in binding to the other face of the helix
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.