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Myosin‐1C uses a novel phosphoinositide‐dependent pathway for nuclear localization
Author(s) -
Nevzorov Ilja,
Sidorenko Ekaterina,
Wang Weihuan,
Zhao Hongxia,
Vartiainen Maria K
Publication year - 2018
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.15252/embr.201744296
Subject(s) - nuclear transport , nuclear localization sequence , nuclear pore , myosin , endoplasmic reticulum , nuclear protein , nuclear export signal , microbiology and biotechnology , biology , cytoplasm , cell nucleus , nucleus , nucleoporin , protein targeting , inner membrane , nuclear membrane , gene , biochemistry , membrane protein , transcription factor , membrane , mitochondrion
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.