New Family Members of FG Repeat Proteins and Their Unexplored Roles During Phase Separation
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 bio...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2021-07-01
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| Series: | Frontiers in Cell and Developmental Biology |
| Subjects: | |
| Online Access: | https://www.frontiersin.org/articles/10.3389/fcell.2021.708702/full |
| _version_ | 1819070710820110336 |
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| author | Yoichi Shinkai Masahiro Kuramochi Takamitsu Miyafusa |
| author_facet | Yoichi Shinkai Masahiro Kuramochi Takamitsu Miyafusa |
| author_sort | Yoichi Shinkai |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-21T17:10:16Z |
| format | Article |
| id | doaj.art-c1fc5064347c4b36b9766d128155fef0 |
| institution | Directory Open Access Journal |
| issn | 2296-634X |
| language | English |
| last_indexed | 2024-12-21T17:10:16Z |
| publishDate | 2021-07-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Cell and Developmental Biology |
| spelling | doaj.art-c1fc5064347c4b36b9766d128155fef02022-12-21T18:56:25ZengFrontiers Media S.A.Frontiers in Cell and Developmental Biology2296-634X2021-07-01910.3389/fcell.2021.708702708702New Family Members of FG Repeat Proteins and Their Unexplored Roles During Phase SeparationYoichi Shinkai0Masahiro Kuramochi1Takamitsu Miyafusa2Molecular Neurobiology Research Group, Biomedical Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, JapanGraduate School of Science and Engineering, Ibaraki University, Hitachi, JapanBio-System Research Group, Bioproduction Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, JapanThe 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.https://www.frontiersin.org/articles/10.3389/fcell.2021.708702/fullFG repeatphase separationintrinsically disordered proteinnuclear poreP granulekeratohyalin granule |
| spellingShingle | Yoichi Shinkai Masahiro Kuramochi Takamitsu Miyafusa New Family Members of FG Repeat Proteins and Their Unexplored Roles During Phase Separation Frontiers in Cell and Developmental Biology FG repeat phase separation intrinsically disordered protein nuclear pore P granule keratohyalin granule |
| title | New Family Members of FG Repeat Proteins and Their Unexplored Roles During Phase Separation |
| title_full | New Family Members of FG Repeat Proteins and Their Unexplored Roles During Phase Separation |
| title_fullStr | New Family Members of FG Repeat Proteins and Their Unexplored Roles During Phase Separation |
| title_full_unstemmed | New Family Members of FG Repeat Proteins and Their Unexplored Roles During Phase Separation |
| title_short | New Family Members of FG Repeat Proteins and Their Unexplored Roles During Phase Separation |
| title_sort | new family members of fg repeat proteins and their unexplored roles during phase separation |
| topic | FG repeat phase separation intrinsically disordered protein nuclear pore P granule keratohyalin granule |
| url | https://www.frontiersin.org/articles/10.3389/fcell.2021.708702/full |
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