ReviewFrontiers in cell and developmental biology2021
New Family Members of FG Repeat Proteins and Their Unexplored Roles During Phase Separation.
Review in Frontiers in cell and developmental biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Building peroxisomes: perspectives on plant peroxins.Biochemical Society transactions · 2026Review
- Germ granule localization of nematode Argonaute WAGO-4 ensures fidelity in small RNA loading.The EMBO journal · 2025Article
- Molecular mechanisms mediated by liquid-liquid phase separation in chronic liver disease progression.iScience · 2025Review
- Identifying and characterizing a missing peroxin-PEX8-in Arabidopsis thaliana.The Plant cell · 2025Article
- An ER-associated structure sequesters misassembled FG-rich nucleoporins to help maintain nuclear pore complex function.Journal of cell science · 2025Article
- Biomolecular Condensates in Telomere Maintenance of ALT Cancer Cells.Journal of molecular biology · 2025Review
- The TEMPO integrator: accelerating molecular simulations by temporally multiscale force prediction.Bioinformatics advances · 2025Article
- A role for BYN-1/bystin in cellular uptake and clearance of residual bodies in the Caenorhabditis elegans germline.Development (Cambridge, England) · 2024Article
- NUP98 oncofusions in myeloid malignancies: An update on molecular mechanisms and therapeutic opportunities.HemaSphere · 2024Review
- Unlocking the Gateway: The Spatio-Temporal Dynamics of the p53 Family Driven by the Nuclear Pores and Its Implication for the Therapeutic Approach in Cancer.International journal of molecular sciences · 2024Review
- Proxiome assembly of the plant nuclear pore reveals an essential hub for gene expression regulation.Nature plants · 2024Article
- Review
- Two structural switches in HIV-1 capsid regulate capsid curvature and host factor binding.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Molecular interactions of FG nucleoporin repeats at high resolution.Nature chemistry · 2022Article
- New Activities of the Nuclear Pore Complexes.Cells · 2021Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The condensation and compartmentalization of biomacromolecules in the cell are driven by the process of phase separation. The main effectors of phase separation are intrinsically disordered proteins, which include proteins with a phenylalanine-glycine (FG) repeat domain. Our understanding of the biological function of FG repeat proteins during phase separation has been mainly derived from recent research on a member of the nuclear pore complex proteins, nucleoporins containing FG repeat domain (FG-NUPs). FG-NUPs form meshwork structures by inter- and intra-molecular FG domain interactions, which confine the nucleo-cytoplasmic exchange. Whereas FG-NUPs localize in the nuclear membrane, other FG repeat proteins reside in the cytoplasm and the nucleoplasm, and the biological function of the FG repeat domain of these proteins is not well described. In the present review, we list the FG repeat proteins that are known to phase separate in the cell, and review their biological functions. We extract the unraveled features of FG repeat proteins as an activator of barrier formation and homotypic cell-cell interactions. Understanding the regulatory mechanisms of FG repeat proteins will provide a potential delivery tool for therapeutic reagents.
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