Nebulin SH3 binds to proline-rich peptides PR2 of titin and myopalladin MyoP2 with micromolar affinity (31 and 3.4 microM, respectively), suggesting a role in sarcomere assembly.
Titin PEVK and myopalladin bind to nebulin SH3 with micromolar affinity, suggesting they play signaling roles in targeting and orientating nebulin to the Z-line during sarcomere assembly.
Skeletal muscle nebulin is thought to determine thin filament length and regulate actomyosin interaction in a calcium/calmodulin or S100 sensitive manner. We have investigated the binding of nebulin SH3 with proline-rich peptides derived from the 28-mer PEVK modules of titin and the Z-line protein myopalladin, using fluorescence, circular dichroism and nuclear magnetic resonance techniques. Of the six peptides studied, PR2 of titin (VPEKKAPVAPPK) and myopalladin MyoP2 (646VKEPPPVLAKPK657) bind to nebulin SH3 with micromolar affinity (approximately 31 and 3.4 microM, respectively), whereas the other four peptides bind weakly (>100 microM). Sequence analysis of titins reveals numerous SH3 binding motifs that are highly enriched in the PEVK segments of titin isoforms. Our findings suggest that titin PEVK and myopalladin may play signaling roles in targeting and orientating nebulin to the Z-line during sarcomere assembly.
Ma et al. (Fri,) reported a other. Nebulin SH3 domain was evaluated on Binding affinity to proline-rich peptides. Nebulin SH3 binds to proline-rich peptides PR2 of titin and myopalladin MyoP2 with micromolar affinity (31 and 3.4 microM, respectively), suggesting a role in sarcomere assembly.
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