The Ligand of Ate1 is intrinsically disordered and participates in nucleolar phase separation regulated by Jumonji Domain Containing 6
The Ligand of Ate1 (Liat1) is a protein of unknown function that was originally discovered through its interaction with arginyltRNA protein transferase 1 (Ate1), a component of the Arg/N-degron pathway of protein degradation. Here, we characterized the functional domains of mouse Liat1 and found tha...
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description | The Ligand of Ate1 (Liat1) is a protein of unknown function that was originally discovered through its interaction with arginyltRNA protein transferase 1 (Ate1), a component of the Arg/N-degron pathway of protein degradation. Here, we characterized the functional domains of mouse Liat1 and found that its N-terminal half comprises an intrinsically disordered region (IDR) that facilitates its liquid–liquid phase separation (LLPS) in the nucleolus. Using bimolecular fluorescence complementation and immunocytochemistry, we found that Liat1 is targeted to the nucleolus by a low-complexity poly-K region within its IDR. We also found that the lysyl-hydroxylase activity of Jumonji Domain Containing 6 (Jmjd6) modifies Liat1, in a manner that requires the Liat1 poly-K region, and inhibits its nucleolar targeting and potential functions. In sum, this study reveals that Liat1 participates in nucleolar LLPS regulated by Jmjd6. |
doi_str_mv | 10.1073/pnas.2015887118 |
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Here, we characterized the functional domains of mouse Liat1 and found that its N-terminal half comprises an intrinsically disordered region (IDR) that facilitates its liquid–liquid phase separation (LLPS) in the nucleolus. Using bimolecular fluorescence complementation and immunocytochemistry, we found that Liat1 is targeted to the nucleolus by a low-complexity poly-K region within its IDR. We also found that the lysyl-hydroxylase activity of Jumonji Domain Containing 6 (Jmjd6) modifies Liat1, in a manner that requires the Liat1 poly-K region, and inhibits its nucleolar targeting and potential functions. In sum, this study reveals that Liat1 participates in nucleolar LLPS regulated by Jmjd6.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.2015887118</identifier><identifier>PMID: 33443146</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Aminoacyltransferases - metabolism ; Animals ; Biological Sciences ; Cell Nucleolus - metabolism ; Domains ; Fluorescence ; HEK293 Cells ; Humans ; Hydroxylase ; Immunocytochemistry ; Intrinsically Disordered Proteins - chemistry ; Intrinsically Disordered Proteins - metabolism ; Jumonji Domain-Containing Histone Demethylases - metabolism ; Ligands ; Liquid phases ; Liquid-Liquid Extraction - methods ; Mice ; Nuclear Proteins - metabolism ; Nucleoli ; Phase separation ; Phase Transition ; Protein Binding ; Protein Domains ; Proteins ; Proteolysis ; Receptors, Cell Surface - metabolism ; tRNA</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2021-01, Vol.118 (1), p.1-11</ispartof><rights>Copyright National Academy of Sciences Jan 5, 2021</rights><rights>2021</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c443t-1f75fc9799d22cd530088fec02d8471fd95357f2c2ef497da84313d9415acde63</citedby><cites>FETCH-LOGICAL-c443t-1f75fc9799d22cd530088fec02d8471fd95357f2c2ef497da84313d9415acde63</cites><orcidid>0000-0003-4836-7437 ; 0000-0002-1627-7261 ; 0000-0002-9057-1186 ; 0000-0003-2690-3729</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/27006438$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/27006438$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33443146$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Arva, Akshaya</creatorcontrib><creatorcontrib>Kasu, Yasar Arfat T.</creatorcontrib><creatorcontrib>Duncan, Jennifer</creatorcontrib><creatorcontrib>Alkhatatbeh, Mosleh A.</creatorcontrib><creatorcontrib>Brower, Christopher S.</creatorcontrib><title>The Ligand of Ate1 is intrinsically disordered and participates in nucleolar phase separation regulated by Jumonji Domain Containing 6</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The Ligand of Ate1 (Liat1) is a protein of unknown function that was originally discovered through its interaction with arginyltRNA protein transferase 1 (Ate1), a component of the Arg/N-degron pathway of protein degradation. Here, we characterized the functional domains of mouse Liat1 and found that its N-terminal half comprises an intrinsically disordered region (IDR) that facilitates its liquid–liquid phase separation (LLPS) in the nucleolus. Using bimolecular fluorescence complementation and immunocytochemistry, we found that Liat1 is targeted to the nucleolus by a low-complexity poly-K region within its IDR. We also found that the lysyl-hydroxylase activity of Jumonji Domain Containing 6 (Jmjd6) modifies Liat1, in a manner that requires the Liat1 poly-K region, and inhibits its nucleolar targeting and potential functions. In sum, this study reveals that Liat1 participates in nucleolar LLPS regulated by Jmjd6.</description><subject>Aminoacyltransferases - metabolism</subject><subject>Animals</subject><subject>Biological Sciences</subject><subject>Cell Nucleolus - metabolism</subject><subject>Domains</subject><subject>Fluorescence</subject><subject>HEK293 Cells</subject><subject>Humans</subject><subject>Hydroxylase</subject><subject>Immunocytochemistry</subject><subject>Intrinsically Disordered Proteins - chemistry</subject><subject>Intrinsically Disordered Proteins - metabolism</subject><subject>Jumonji Domain-Containing Histone Demethylases - metabolism</subject><subject>Ligands</subject><subject>Liquid phases</subject><subject>Liquid-Liquid Extraction - methods</subject><subject>Mice</subject><subject>Nuclear Proteins - metabolism</subject><subject>Nucleoli</subject><subject>Phase separation</subject><subject>Phase Transition</subject><subject>Protein Binding</subject><subject>Protein Domains</subject><subject>Proteins</subject><subject>Proteolysis</subject><subject>Receptors, Cell Surface - metabolism</subject><subject>tRNA</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkUtvEzEUhS0EoqGwZgWyxIbNtNePGdsbpCq8FYlNWVuu7UkcTezBnqmUP8DvxqOU8Fjdxf3O0Tk6CL0kcEVAsOsxmnJFgbRSCkLkI7QioEjTcQWP0QqAikZyyi_Qs1L2AKBaCU_RBWOcM8K7Ffp5u_N4E7YmOpx6fDN5gkPBIU45xBKsGYYjdqGk7Hz2Di_caPIUbBjN5BcSx9kOPg0m43FnisfFV8JMIUWc_XYeKufw3RF_nQ8p7gN-nw6mytYpTvWGuMXdc_SkN0PxLx7uJfr-8cPt-nOz-fbpy_pm09gaeGpIL9reKqGUo9S6lgFI2XsL1EkuSO9Uy1rRU0t9z5VwRtaazClOWmOd79glenfyHee7g3fW155m0GMOB5OPOpmg__3EsNPbdK-FJIJCWw3ePhjk9GP2ZdKHUKwfBhN9moumXEjgRBFV0Tf_ofs051jrLRTjVPJuSXR9omxOpWTfn8MQ0MvGetlY_9m4Kl7_3eHM_x61Aq9OwL5MKZ__VAB0nEn2C39xrpo</recordid><startdate>20210105</startdate><enddate>20210105</enddate><creator>Arva, Akshaya</creator><creator>Kasu, Yasar Arfat T.</creator><creator>Duncan, Jennifer</creator><creator>Alkhatatbeh, Mosleh A.</creator><creator>Brower, Christopher S.</creator><general>National Academy of Sciences</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0003-4836-7437</orcidid><orcidid>https://orcid.org/0000-0002-1627-7261</orcidid><orcidid>https://orcid.org/0000-0002-9057-1186</orcidid><orcidid>https://orcid.org/0000-0003-2690-3729</orcidid></search><sort><creationdate>20210105</creationdate><title>The Ligand of Ate1 is intrinsically disordered and participates in nucleolar phase separation regulated by Jumonji Domain Containing 6</title><author>Arva, Akshaya ; Kasu, Yasar Arfat T. ; Duncan, Jennifer ; Alkhatatbeh, Mosleh A. ; Brower, Christopher S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c443t-1f75fc9799d22cd530088fec02d8471fd95357f2c2ef497da84313d9415acde63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Aminoacyltransferases - metabolism</topic><topic>Animals</topic><topic>Biological Sciences</topic><topic>Cell Nucleolus - metabolism</topic><topic>Domains</topic><topic>Fluorescence</topic><topic>HEK293 Cells</topic><topic>Humans</topic><topic>Hydroxylase</topic><topic>Immunocytochemistry</topic><topic>Intrinsically Disordered Proteins - chemistry</topic><topic>Intrinsically Disordered Proteins - metabolism</topic><topic>Jumonji Domain-Containing Histone Demethylases - metabolism</topic><topic>Ligands</topic><topic>Liquid phases</topic><topic>Liquid-Liquid Extraction - methods</topic><topic>Mice</topic><topic>Nuclear Proteins - metabolism</topic><topic>Nucleoli</topic><topic>Phase separation</topic><topic>Phase Transition</topic><topic>Protein Binding</topic><topic>Protein Domains</topic><topic>Proteins</topic><topic>Proteolysis</topic><topic>Receptors, Cell Surface - metabolism</topic><topic>tRNA</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Arva, Akshaya</creatorcontrib><creatorcontrib>Kasu, Yasar Arfat T.</creatorcontrib><creatorcontrib>Duncan, Jennifer</creatorcontrib><creatorcontrib>Alkhatatbeh, Mosleh A.</creatorcontrib><creatorcontrib>Brower, Christopher S.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Arva, Akshaya</au><au>Kasu, Yasar Arfat T.</au><au>Duncan, Jennifer</au><au>Alkhatatbeh, Mosleh A.</au><au>Brower, Christopher S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Ligand of Ate1 is intrinsically disordered and participates in nucleolar phase separation regulated by Jumonji Domain Containing 6</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2021-01-05</date><risdate>2021</risdate><volume>118</volume><issue>1</issue><spage>1</spage><epage>11</epage><pages>1-11</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>The Ligand of Ate1 (Liat1) is a protein of unknown function that was originally discovered through its interaction with arginyltRNA protein transferase 1 (Ate1), a component of the Arg/N-degron pathway of protein degradation. Here, we characterized the functional domains of mouse Liat1 and found that its N-terminal half comprises an intrinsically disordered region (IDR) that facilitates its liquid–liquid phase separation (LLPS) in the nucleolus. Using bimolecular fluorescence complementation and immunocytochemistry, we found that Liat1 is targeted to the nucleolus by a low-complexity poly-K region within its IDR. We also found that the lysyl-hydroxylase activity of Jumonji Domain Containing 6 (Jmjd6) modifies Liat1, in a manner that requires the Liat1 poly-K region, and inhibits its nucleolar targeting and potential functions. In sum, this study reveals that Liat1 participates in nucleolar LLPS regulated by Jmjd6.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>33443146</pmid><doi>10.1073/pnas.2015887118</doi><tpages>11</tpages><orcidid>https://orcid.org/0000-0003-4836-7437</orcidid><orcidid>https://orcid.org/0000-0002-1627-7261</orcidid><orcidid>https://orcid.org/0000-0002-9057-1186</orcidid><orcidid>https://orcid.org/0000-0003-2690-3729</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | Aminoacyltransferases - metabolism Animals Biological Sciences Cell Nucleolus - metabolism Domains Fluorescence HEK293 Cells Humans Hydroxylase Immunocytochemistry Intrinsically Disordered Proteins - chemistry Intrinsically Disordered Proteins - metabolism Jumonji Domain-Containing Histone Demethylases - metabolism Ligands Liquid phases Liquid-Liquid Extraction - methods Mice Nuclear Proteins - metabolism Nucleoli Phase separation Phase Transition Protein Binding Protein Domains Proteins Proteolysis Receptors, Cell Surface - metabolism tRNA |
title | The Ligand of Ate1 is intrinsically disordered and participates in nucleolar phase separation regulated by Jumonji Domain Containing 6 |
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