Different obscurin isoforms localize to distinct sites at sarcomeres.
We used four antibodies to regions of obscurin isoforms A and B, encoded by the obscurin gene, to investigate the location of these proteins in skeletal myofibers at resting and stretched lengths. Obscurin A ( approximately 800 kDa) which was recognized by antibodies generated to the N-terminal, Rho-GEF, and the non-modular C-terminal domain that lacks the kinase-like domains, localizes at the level of the M-band. Obscurin B ( approximately 900 kDa) which has the N-terminal, Rho-GEF, and the C-terminal kinase-like domains, localizes at the level of the A/I junction. Additional isoforms, which lack one or more of these epitopes, are present at the Z-disk and Z/I junction.
Bowman
Amber L
AL
Department of Physiology, University of Maryland School of Medicine, 655 W. Baltimore St, MD 21201, USA.
Kontrogianni-Konstantopoulos
Aikaterini
A
Hirsch
Sara S
SS
Geisler
Sarah B
SB
Gonzalez-Serratos
Hugo
H
Russell
Mark W
MW
Bloch
Robert J
RJ
D000818:Animals; D009124:Muscle Proteins / Q000032:analysis*; D018482:Muscle, Skeletal / Q000737:chemistry*; D020033:Protein Isoforms / Q000032:analysis; D012518:Sarcomeres / Q000737:chemistry*
D009124:Muscle Proteins; D020033:Protein Isoforms