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ATP5O — MYL6

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Intact Interaction: Complex of 185 proteins (association, cross-linking study) Humphries et al., Science signaling 2009
• IRef Intact Interaction: Complex of 177 proteins (association, cross-linking study) Byron et al., Proteomics 2012
• IRef Intact Interaction: Complex of 203 proteins (association, cross-linking study) Byron et al., Proteomics 2012
• IRef Intact Interaction: Complex of 156 proteins (association, anti tag coimmunoprecipitation) Lau et al., Cell 2012

Text-mined interactions from Literome

Levinson et al., Wound Repair Regen 2004 (Disease Models, Animal...) : It is proposed that CaM-MLCK phosphorylation of myosin light chain and subsequent myosin ATPase activation affects granulation tissue fibroblast behavior and contributes to wound contraction
Stephens et al., Can J Physiol Pharmacol 2007 (Asthma...) : On the other hand, we found that the state of activation of the ATPase by phosphorylation of smooth muscle myosin light chain ( molecular mass 20,000 Da ) was greater in the SASM
Kalapos et al., Acta Biochim Biophys Hung 1989 : Effects of skeletal muscle myosin light chain phosphorylation on synthetic actomyosin ATPase activity and superprecipitation
Chacko et al., Prog Clin Biol Res 1986 : The regulation of actin activated ATPase activity by myosin light chain phosphorylation is depicted in the schematic diagram
Levitsky et al., FEBS Lett 1987 : The effect of myosin light chain phosphorylation on the actin stimulated ATPase activity of myosin minifilaments
Tuazon et al., J Biol Chem 1984 : Activation of actin activated ATPase in smooth muscle by phosphorylation of myosin light chain with protease activated kinase I
Franks et al., J Mol Cell Cardiol 1984 : It also appears that the effect of myosin light chain phosphorylation on ATPase activity requires an ordered myofilament structure
Nishikawa et al., Nature 1980 : Phosphorylation of myosin light chain increases the activity of actin activated myosin ATPase and the resultant contraction of the actomyosin presumably mediates the release reaction
Higashihara et al., FEBS Lett 1995 : These results suggest that LC20 interacts with both LC17 and the heavy chain, and the interaction between LC20 and LC17 is involved in the activation of actin activated ATPase activity of smooth muscle myosin
Ford et al., Can J Physiol Pharmacol 1994 : It is known that myosin light chain phosphorylation activates the actomyosin ATPase , but this same phosphorylation also causes a structural change that facilitates filament formation
Katoh et al., J Biol Chem 1996 : However, LC17 was not essential for the phosphorylation dependent regulation of actin activated ATPase activity and superprecipitation but was required for full regulation