Calmodulin Interaction with hEAG1 Visualized by FRET Microscopy

Open Access

Peer-reviewed

Research Article

J. Tiago Gonçalves ,

* E-mail: goncalves@ucla.edu

Current address: Department of Neurology, David Geffen School of Medicine, University of California Los Angeles, Los Angeles, California, United States of America

Affiliation Molecular Biology of Neuronal Signals, Max-Planck Institute for Experimental Medicine, Göttingen, Germany
⨯
Walter Stühmer

Affiliations Molecular Biology of Neuronal Signals, Max-Planck Institute for Experimental Medicine, Göttingen, Germany, DFG Research Center for Molecular Physiology of the Brain, Göttingen, Germany
⨯

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http://plosone.org/article/info:doi/10.1371/journal.pone.0010873#article1.front1.article-meta1.abstract1.sec3.p1

The Conclusions/Significance should read:

"We demonstrated that the BD-N and BD-C2 binding domains are necessary for CaM binding to the native channel, and, therefore, that BD-C1 is unable to bind CaM independently."

No competing interests declared.

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Fluorescence imaging
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Cell binding
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Intracellular membranes
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Transfection
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Voltage-gated potassium channels
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