• Biomedical Science Letters
• /
• v.16 no.4
• /
• pp.207-212
• /
• 2010

Archivillin, a muscle-specific isoform of supervillin, is a component of the costameric cytoskeleton of muscle cells. The purpose of this study was to determine which protein in the skeletal muscle collaborates with archvillin C-terminus. For this purpose, a yeast two-hybrid screening of human skeletal muscle cDNA library was performed using the C-terminal region of archvillin as bait. This study shows that seven human skeletal muscle proteins, namely, nebulin, xeplin, archvillin, GAPDH, TOX4, PITRM1, and YME1L1 interact with archvillin C-terminus. Especially, xeplin is a newly discovered protein interacts with archvillin C-terminus. These results indicate that archvillin C-terminus acts as a bridge between nebulin and xeplin at costameres. Archvillin C-terminal region interacts with nebulin C-terminal region at Z-discs and interacts with xeplin at the vicinity of sarcolemma. I propose that these interactions may contribute to formation of costameric structure and muscle contraction.

• Biomedical Science Letters
• /
• v.9 no.4
• /
• pp.231-240
• /
• 2003

Deciphering the molecular interactions of proteins forming Z-lines is pivotal for understanding the regulation of myofibril assembly, sarcomeric organization, and mechanical properties of striated muscle. The purpose of this study is to searched for potential novel ligands of the Z-line portion of nebulin. In this study interacting proteins with intra-Z-line region of nebulin were screened using a yeast two-hybrid approach. The interaction was conformed by GST pull-down assay. We identified 269 residues within villin/gelsolin homology domain of supervillin that intreacts with the serine rich region of nebulin. The specific interactions of nebulin and supervillin were confirmed in vitro by GST pull-down experiments. Our data suggest that supervillin attaches directly to the Z-line through its interaction with the serine rich domain of nebulin in skeletal muscles. This interaction may link myofibrillar Z-discs to the membrane-associated complexes, costameres.