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Am J Physiol Cell Physiol (March 10, 2004). doi:10.1152/ajpcell.00497.2003
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Submitted on November 10, 2003
Accepted on March 5, 2004

Obscurin Regulates the Organization of Myosin into A-Bands

Aikaterini Kontrogianni-Konstantopoulos1*, Dawn H Catino1, John C Strong1, William R Randall2, and Robert J Bloch1

1 Physiology, University of Maryland, Baltimore, Baltimore, MD, USA
2 Pharmacology and Experimental Therapeutics, University of Maryland, Baltimore, Baltimore, MD, USA

* To whom correspondence should be addressed. E-mail: akons001{at}umaryland.edu.

Obscurin is a giant sarcomeric protein, composed of adhesion modules and signaling domains, that surrounds myofibrils at the level of the Z-disk and M-line. To study the role of obscurin during myofibrillogenesis we used adenoviral-mediated gene delivery to overexpress part of its COOH-terminus in primary cultures of postnatal day 1 (P1) skeletal myotubes. Examination of the subcellular distribution of a number of sarcomeric proteins revealed that the organization of myosin into A-bands was dramatically reduced. Myosin assembled into A-bands normally in mock- or control-infected P1 myotubes. Overexpression of the COOH-terminus of obscurin did not affect the organization of other sarcomeric markers, including actin, alpha-actinin, titin and myomesin. Assembly of myomesin into nascent M-lines in treated myotubes suggests that these structures can form independently of A-bands. Immunoblot analysis indicated that there was a small (~20%) but consistent decrease in the amount of myosin expressed in cells infected with the COOH-terminus of obscurin. Co-immunoprecipitation experiments, using adult skeletal muscle homogenates demonstrated that obscurin exists in a complex with myosin. Thus, our findings suggest that the COOH-terminal region of obscurin interacts with sarcomeric myosin and may play a critical role in its ability to assemble into A-bands in striated muscle.




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