Interaction of nebulin SH3 domain with titin PEVK and myopalladin: implications for the signaling and assembly role of titin and nebulin
Copyright policy )Interaction of nebulin SH3 domain with titin PEVK and myopalladin: implications for the signaling and assembly role of titin and nebulin
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 (∼31 and 3.4 μM, respectively), whereas the other four peptides bind weakly (>100 μM). 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.
- National Institute of Health Pakistan
- National Institutes of Health United States
- National Institute of Health (NIH/NICHD) United States
- National Institute of Arthritis and Musculoskeletal and Skin Diseases United States
- National Institutes of Health, National Institute of Arthritis and Musculoskeletal and Skin Diseases United States
Peptide Biosynthesis, Sarcomeres, Magnetic Resonance Spectroscopy, SH3 domain of nebulin, PEVK, Amino Acid Motifs, Muscle Proteins, Circular dichroism, Models, Biological, Fluorescence, Nuclear magnetic resonance, Humans, Protein Isoforms, Connectin, Muscle, Skeletal, Binding Sites, Dose-Response Relationship, Drug, Circular Dichroism, Protein Structure, Tertiary, Spectrometry, Fluorescence, Peptides, Protein Kinases, Myopalladin, Protein Binding, Signal Transduction
Peptide Biosynthesis, Sarcomeres, Magnetic Resonance Spectroscopy, SH3 domain of nebulin, PEVK, Amino Acid Motifs, Muscle Proteins, Circular dichroism, Models, Biological, Fluorescence, Nuclear magnetic resonance, Humans, Protein Isoforms, Connectin, Muscle, Skeletal, Binding Sites, Dose-Response Relationship, Drug, Circular Dichroism, Protein Structure, Tertiary, Spectrometry, Fluorescence, Peptides, Protein Kinases, Myopalladin, Protein Binding, Signal Transduction
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