[Phosphorylation of sarcomeric cytoskeletal proteins--an adaptive factor for inhibiting the contractile activity of muscle during hibernation].
The influence of phosphorylation in vitro of the sarcomere cytoskeletal proteins titin and X-protein of skeletal muscles as well as C-protein of cardiac muscle of ground squirrel Citellus undulatus on the actin-activated ATPase activity of myosin and its Ca2+ sensitivity was studied. It was shown that phosphorylation lowers the activating effect of titin and C-protein and increases the inhibitory effect of X-protein on the enzymatic properties of actomyosin. The phosphorylation of the proteins has the most pronounced influence on Ca2+ sensitivity of actomyosin: it drops to a greater extent in the presence of phosphorylated C-protein and titin and is completely inhibited by phosphorylated X-protein. The inhibitory influence of phosphorylation in vitro of sarcomere cytoskeletal proteins on the above functional properties of the actomyosin system as well as the increase in the extent of phosphorylation of titin in vivo upon hibernation allow one to conclude that this posttranslation modification contributes to adaptive mechanisms of suppression of the contractile ability of muscles in this period.
Vikhliantsev
I M
IM
Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Moscow Region, 142290 Russia.
Podlubnaia
Z A
ZA
D000818:Animals; D006605:Hibernation; D009124:Muscle Proteins / Q000378:metabolism*; D018482:Muscle, Skeletal / Q000378:metabolism* / Q000502:physiology; D010766:Phosphorylation; D012518:Sarcomeres / Q000378:metabolism* / Q000502:physiology; D012589:Sciuridae
D009124:Muscle Proteins