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α‐Synemin localizes to the M‐band of the sarcomere through interaction with the M10 region of titin
Author(s) -
Prudner Bethany C.,
Roy Pritam Sinha,
Damron Derek S.,
Russell Mary A.
Publication year - 2014
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.2014.11.001
Subject(s) - titin , sarcomere , immunoprecipitation , microbiology and biotechnology , gene isoform , chemistry , immunostaining , two hybrid screening , biology , biochemistry , yeast , myocyte , immunohistochemistry , gene , immunology
α‐Synemin contains a unique 312 amino acid insert near the end of its C‐terminal tail. Therefore we set out to determine if the insert is a site of protein–protein interaction that regulates the sub‐cellular localization of this large isoform of synemin. Yeast‐two hybrid analysis indicated that this region is a binding site for the M10 region of titin. This was confirmed with GST pull‐down assays. Co‐immunoprecipitation of endogenous proteins indicated close association of the two proteins in vivo and immunostaining of cardiomyocytes demonstrated co‐localization of the proteins at the M‐band of the sarcomere.