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Different obscurin isoforms localize to distinct sites at sarcomeres
Author(s) -
Bowman Amber L.,
Kontrogianni-Konstantopoulos Aikaterini,
Hirsch Sara S.,
Geisler Sarah B.,
Gonzalez-Serratos Hugo,
Russell Mark W.,
Bloch Robert J.
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.03.011
Subject(s) - sarcomere , gene isoform , obscurin , titin , microbiology and biotechnology , biology , chemistry , computational biology , myocyte , genetics , gene
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 (∼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 (∼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.
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