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

EMBO reports (2018-01-14)
Ilja Nevzorov, Ekaterina Sidorenko, Weihuan Wang, Hongxia Zhao, Maria K Vartiainen
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 required for nuclear import, but not nuclear retention, of Myo1C. Our results therefore demonstrate, for the first time, that membrane association and binding to nuclear partners is sufficient to drive nuclear localization of also soluble proteins, opening new perspectives to evolution of cellular protein sorting mechanisms.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Magnesium acetate solution, BioUltra, for molecular biology, ~1 M in H2O
Sigma-Aldrich
Anti-Histone H3 antibody produced in rabbit, IgG fraction of antiserum, buffered aqueous solution
Sigma-Aldrich
Anti-MYO1C antibody produced in rabbit, Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution

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