Myosin-1C uses a novel phosphoinositide-dependent pathway for nuclear localization.

ABSTRACT: Accurate control of macromolecule transport between nucleus and cytoplasm underlines several essential biological processes, including gene expression. According to the canonical model, nuclear import of soluble proteins is based on nuclear localization signals and transport factors. We challenge this view by showing that nuclear localization of the actin-dependent motor protein Myosin-1C (Myo1C) resembles the diffusion-retention mechanism utilized by inner nuclear membrane proteins. We show that Myo1C constantly shuttles in and out of the nucleus and that its nuclear localization does not require soluble factors, but is dependent on phosphoinositide binding. Nuclear import of Myo1C is preceded by its interaction with the endoplasmic reticulum, and phosphoinositide binding is specifically

SUBMITTER: Nevzorov I 

PROVIDER: S-EPMC5797967 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature