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1
Max Delbrück Center for Molecular Medicine, 13092 Berlin, Germany;
Max Planck Institute for Physiological and Clinical Research, 61231 Bad Nauheim, Germany;
* Institute of Physiology, Humboldt University (Charité), 10117 Berlin, Germany; and
# Franz Volhard Clinic, Humboldt University (Charité), 13125 Berlin, Germany
1Correspondence: Max Delbrück Center for Molecular Medicine (MDC), Robert-Rössle-Str. 10, D-13092 Berlin, Germany. E-mail: haase{at}mdc-berlin.de
Ahnak is a ubiquitously expressed giant protein of 5643 amino acids implicated in cell differentiation and signal transduction. In a recent study, we demonstrated the association of ahnak with the regulatory ß2 subunit of the cardiac L-type Ca2+ channel. Here we identify the most carboxyl-terminal ahnak region (aa 5262–5643) to interact with recombinant ß2a as well as with ß2 and ß1a isoforms of native muscle Ca2+ channels using a panel of GST fusion proteins. Equilibrium sedimentation analysis revealed Kd values of 55 ± 11 nM and 328 ± 24 nM for carboxyl-terminal (aa 195–606) and amino-terminal (aa 1–200) truncates of the ß2a subunit, respectively. The same carboxyl-terminal ahnak region (aa 5262–5643) bound to G-actin and cosedimented with F-actin. Confocal microscopy of human left ventricular tissue localized the carboxyl-terminal ahnak portion to the sarcolemma including the T-tubular system and the intercalated disks of cardiomyocytes. These results suggest that ahnak provides a structural basis for the subsarcolemmal cytoarchitecture and confers the regulatory role of the actin-based cytoskeleton to the L-type Ca2+ channel.—Hohaus, A., Person, V., Behlke, J., Schaper, J., Morano, I., Haase, H. The carboxyl-terminal region of ahnak provides a link between cardiac L-type Ca2+ channels and the actin-based cytoskeleton.
Key Words: L-type calcium channel • ß subunit • protein–protein interaction • cardiomyocytes
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