Ankyrin domain of myosin 16 influences motor function and decreases protein phosphatase catalytic activity.

European Biophysics Journal : EBJ
Andras KengyelMiklós Nyitrai

Abstract

The unconventional myosin 16 (Myo16), which may have a role in regulation of cell cycle and cell proliferation, can be found in both the nucleus and the cytoplasm. It has a unique, eight ankyrin repeat containing pre-motor domain, the so-called ankyrin domain (My16Ank). Ankyrin repeats are present in several other proteins, e.g., in the regulatory subunit (MYPT1) of the myosin phosphatase holoenzyme, which binds to the protein phosphatase-1 catalytic subunit (PP1c). My16Ank shows sequence similarity to MYPT1. In this work, the interactions of recombinant and isolated My16Ank were examined in vitro. To test the effects of My16Ank on myosin motor function, we used skeletal muscle myosin or nonmuscle myosin 2B. The results showed that My16Ank bound to skeletal muscle myosin (K D ≈ 2.4 µM) and the actin-activated ATPase activity of heavy meromyosin (HMM) was increased in the presence of My16Ank, suggesting that the ankyrin domain can modulate myosin motor activity. My16Ank showed no direct interaction with either globular or filamentous actin. We found, using a surface plasmon resonance-based binding technique, that My16Ank bound to PP1cα (K D ≈ 540 nM) and also to PP1cδ (K D ≈ 600 nM) and decreased its phosphatase activity towards...Continue Reading

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Citations

Dec 19, 2015·Nursing Ethics·Lalit Kumar Radha KrishnaRavindran Kanesvaran
Sep 3, 2019·Frontiers in Cellular Neuroscience·Mona Katrin RoeslerWolfgang Wagner
Aug 23, 2020·Cells·Elek TelekBeáta Bugyi
Mar 23, 2019·International Journal of Molecular Sciences·Reina SasakiMitsuhiko Moriyama

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