Proteomics

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Native mass spectrometry of calmodulin binding to the plasma-membrane Ca2+-ATPase ACA8

ABSTRACT: Binding of two calmodoulin proteins to the integral membrane protein ACA8, a plasma-membrane Ca2+-ATPase von A. thaliana, was shown by native mass spectrometry.

INSTRUMENT(S): Q-Tof ultima

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

SUBMITTER: Johannes Heidemann  

LAB HEAD: Charlotte Uetrecht

PROVIDER: PXD011177 | Pride | 2018-12-05

REPOSITORIES: Pride

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Plasma-membrane Ca<sup>2+</sup>-ATPases expel Ca<sup>2+</sup> from the cytoplasm and are key regulators of Ca<sup>2+</sup> homeostasis in eukaryotes. They are autoinhibited under low Ca<sup>2+</sup> concentrations. Calmodulin (CaM)-binding to a unique regulatory domain releases the autoinhibition and activates the pump. However, the structural basis for this activation, including the overall structure of this calcium pump and its complex with calmodulin, is unknown. We previously determined the  ...[more]

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