High impact information on MYPN

• The myopathic changes in the nebulin KO model include depressed contractility, loss of myopalladin from the Z-disk, and dysregulation of genes involved in calcium homeostasis and glycogen metabolism; features potentially relevant for understanding human NM [1].
• This suggests that palladin and myopalladin may have conserved roles in stress fiber and Z-line assembly [2].
• The NH(2)-terminal region of myopalladin specifically binds to the cardiac ankyrin repeat protein (CARP), a nuclear protein involved in control of muscle gene expression [2].
• The palladin/myotilin/myopalladin family of actin-associated scaffolds [3].

Anatomical context of MYPN

• While myotilin and myopalladin are most abundant in skeletal and cardiac muscle, palladin is ubiquitously expressed in the organs of developing vertebrates [3].
• Our findings suggest that titin PEVK and myopalladin may play signaling roles in targeting and orientating nebulin to the Z-line during sarcomere assembly [4].

Physical interactions of MYPN

• 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) [4].

References