ArticleEMBO reports2018
Myosin-1C uses a novel phosphoinositide-dependent pathway for nuclear localization.
Article in EMBO reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
12 citing papers in PubMed, 23 citations in OpenAlex.
- Long-tailed class I myosins rely on tail-mediated phosphoinositide recognition for specific membrane recruitment.Cell communication and signaling : CCS · 2025Article
- Non-Canonical Localization of Cardiac Troponins: Expanding Functions or Causing Pathologies?International journal of molecular sciences · 2024Review
- Article
- The Taspase1/Myosin1f-axis regulates filopodia dynamics.iScience · 2022Article
- Article
- Basic-hydrophobic sites are localized in conserved positions inside and outside of PH domains and affect localization ofMolecular biology of the cell · 2020Article
- Unconventional Myosins: How Regulation Meets Function.International journal of molecular sciences · 2019Review
- Landscape of heart proteome changes in a diet-induced obesity model.Scientific reports · 2019Article
- The motor protein Myo1c regulates transforming growth factor-β-signaling and fibrosis in podocytes.Kidney international · 2019Article
- Nuclear actin: ancient clue to evolution in eukaryotes?Histochemistry and cell biology · 2018Review
- Calcium and Nuclear Signaling in Prostate Cancer.International journal of molecular sciences · 2018Review
- Myosin-1C uses a novel phosphoinositide-dependent pathway for nuclear localization.EMBO reports · 2018Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.