Membrane binding of endocytic myosin-1s is inhibited by a class of ankyrin repeat proteins
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Abstract
Ank1 binds the myosin-1 (Myo1) and prevents its membrane and endocytic patch localization. Structural predications suggest that the (Ank1) ankyrin repeats bind the Myo1 motor while the Ank1 acidic C-terminus masks positive charges necessary for Myo1 membrane association. This regulatory mechanism appears to be evolutionarily conserved.
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n ank1Δ cells, Myo1-GFP was instead localized uniformly along the plasma membrane (PM) (Fig. 1C).
Such an exciting and striking effect!!!! This paper is a lot of fun! Thank you for sharing!
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In contrast, in myo1-mNG fim1-mCherry cells overproducing Ank1, while Fim1-mCherry was at patches, almost all Myo1-mNG was cytoplasmic (Fig. 3A).
There are still some faint myo1-mNG puncta visible. Do you think this would go away with higher expression of Ank1? or do you expect there is another mechanism that allows some Myo1 to get to the membrane / evade Ank1?
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This suggests that, in addition to inhibiting membrane binding, myosin-1 F-actin binding and/or motor activity may also be inhibited by Ank1/OSTF1.
This is super cool! I love the 3 species inclusion in this paper! I'd be interested to see if Ank1/OSTF1 are interchangeable between species (expressing OSTF1 in Ank1 delta pombe)! Given its small size it might be an easily purifiable myosin "inhibitor"!
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In accord, Myo1Δ(1-772)-mNG localized to endocytic patches in wildtype cells but in ank1Δ cells, Myo1Δ(1-772)-mNG localized along the PM (Fig. 2C), consistent with the Myo1 C-terminal domains being dispensable for Ank1 interaction.
Was the Myo1 mutant localized to the contractile ring in the ank1 delta strain? One of the representative max intensity projections in Fig 2C looks like it has the beautiful elliptical ring!!!
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