The carboxyl-terminal ahnak domain induces actin bundling and stabilizes muscle contraction 1 HANNELORE HAASE * ,2 , INES PAGEL † , YANA KHALINA * ,‡ , UDO ZACHARZOWSKY † , VERONIKA PERSON § , GUDRUN LUTSCH * , DARIA PETZHOLD * , MONIKA KOTT * , JUTTA SCHAPER § and INGO MORANO * ,†† * Max Delbrück Center for Molecular Medicine, Berlin, Germany; † Franz Volhard Clinic, Humboldt University (Charité), Berlin, Germany; ‡ Institute of Theoretical and Experimental Biophysics, Academy of Sciences of Russia, Pushchino, Russia; § Max Planck Inst. for Physiological and Clinical Research, Bad Nauheim, Germany; and †† Johannes Müller Institute for Physiology, Humboldt University (Charité), Berlin, Germany 2 Correspondence: Max Delbrück Center for Molecular Medicine, 13092 Berlin, Germany, E-mail: haase@mdc-berlin.de <h3>SPECIFIC AIMS</h3> Ahnak is encoded by an intronless gene located on human chromosome 11q12. It has been implicated in fundamental cellular processes as diverse as cell differentiation, signal transduction, and regulated exocytosis. However, no information is available about the existence of ahnak isoforms that serve different cell type-specific functions. In cardiomyocytes we identified ahnak as a 700 kDa protein that localized to the inner side of the sarcolemma membrane and interacted with the ß subunit
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The carboxyl-terminal ahnak domain induces actin bundling and stabilizes muscle contraction
HAASE, HANNELORE; PAGEL, INES; KHALINA, YANA; ZACHARZOWSKY, UDO; PERSON, VERONIKA; LUTSCH, GUDRUN; PETZHOLD, DARIA; KOTT, MONIKA; SCHAPER, JUTTA; MORANO, INGO
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, Volume 18 (7): 839
Fed of American Socs for Experimental Biology – May 1, 2004
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