Nucleo-cytoplasmic shuttling of splicing factor SRSF1 is required for development and cilia function
Shuttling RNA-binding proteins coordinate nuclear and cytoplasmic steps of gene expression. The SR family proteins regulate RNA splicing in the nucleus and a subset of them, including SRSF1, shuttles between the nucleus and cytoplasm affecting post-splicing processes. However, the physiological sign...
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| creator | Haward, Fiona Maslon, Magdalena M Yeyati, Patricia L Bellora, Nicolas Hansen, Jan N Aitken, Stuart Lawson, Jennifer von Kriegsheim, Alex Wachten, Dagmar Mill, Pleasantine Adams, Ian R Caceres, Javier F |
| description | Shuttling RNA-binding proteins coordinate nuclear and cytoplasmic steps of gene expression. The SR family proteins regulate RNA splicing in the nucleus and a subset of them, including SRSF1, shuttles between the nucleus and cytoplasm affecting post-splicing processes. However, the physiological significance of this remains unclear. Here, we used genome editing to knock-in a nuclear retention signal (NRS) in
to create a mouse model harboring an SRSF1 protein that is retained exclusively in the nucleus.
mutants displayed small body size, hydrocephalus, and immotile sperm, all traits associated with ciliary defects. We observed reduced translation of a subset of mRNAs and decreased abundance of proteins involved in multiciliogenesis, with disruption of ciliary ultrastructure and motility in cells and tissues derived from this mouse model. These results demonstrate that SRSF1 shuttling is used to reprogram gene expression networks in the context of high cellular demands, as observed here, during motile ciliogenesis. |
| doi_str_mv | 10.7554/eLife.65104 |
| format | Article |
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to create a mouse model harboring an SRSF1 protein that is retained exclusively in the nucleus.
mutants displayed small body size, hydrocephalus, and immotile sperm, all traits associated with ciliary defects. We observed reduced translation of a subset of mRNAs and decreased abundance of proteins involved in multiciliogenesis, with disruption of ciliary ultrastructure and motility in cells and tissues derived from this mouse model. These results demonstrate that SRSF1 shuttling is used to reprogram gene expression networks in the context of high cellular demands, as observed here, during motile ciliogenesis.</description><identifier>ISSN: 2050-084X</identifier><identifier>EISSN: 2050-084X</identifier><identifier>DOI: 10.7554/eLife.65104</identifier><identifier>PMID: 34338635</identifier><language>eng</language><publisher>England: eLife Science Publications, Ltd</publisher><subject>alternative splicing ; Analysis ; Animals ; Binding proteins ; Biochemistry and Chemical Biology ; Body size ; Cell cycle ; Cell Nucleus - metabolism ; Chromosomes and Gene Expression ; Cilia ; Cilia - metabolism ; CRISPR ; Cytoplasm ; Cytoplasm - metabolism ; Gene expression ; Genome editing ; Genomes ; Genomics ; Hydrocephalus ; Kinases ; Localization ; Male ; Mice ; motile cilia ; mRNA translation ; Physiological aspects ; Protein binding ; Proteins ; RNA ; RNA polymerase ; RNA-binding protein ; RNA-binding proteins ; Serine-Arginine Splicing Factors - genetics ; Serine-Arginine Splicing Factors - metabolism ; Splicing factors ; SR proteins ; SRSF1 ; Stem cells ; Testes ; Ultrastructure</subject><ispartof>eLife, 2021-08, Vol.10</ispartof><rights>2021, Haward et al.</rights><rights>COPYRIGHT 2021 eLife Science Publications, Ltd.</rights><rights>2021, Haward et al. This work is published under https://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2021, Haward et al 2021 Haward et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c576t-f87525298e9914cc58a96a17e48eeb0dd1c70a0f74885d691b88dd24d4ad97003</citedby><cites>FETCH-LOGICAL-c576t-f87525298e9914cc58a96a17e48eeb0dd1c70a0f74885d691b88dd24d4ad97003</cites><orcidid>0000-0001-8838-1271 ; 0000-0001-8025-6169 ; 0000-0001-9048-5600 ; 0000-0003-4800-6332 ; 0000-0002-1050-1306 ; 0000-0002-0489-7535 ; 0000-0001-6637-3465</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC8352595/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC8352595/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2102,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/34338635$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Haward, Fiona</creatorcontrib><creatorcontrib>Maslon, Magdalena M</creatorcontrib><creatorcontrib>Yeyati, Patricia L</creatorcontrib><creatorcontrib>Bellora, Nicolas</creatorcontrib><creatorcontrib>Hansen, Jan N</creatorcontrib><creatorcontrib>Aitken, Stuart</creatorcontrib><creatorcontrib>Lawson, Jennifer</creatorcontrib><creatorcontrib>von Kriegsheim, Alex</creatorcontrib><creatorcontrib>Wachten, Dagmar</creatorcontrib><creatorcontrib>Mill, Pleasantine</creatorcontrib><creatorcontrib>Adams, Ian R</creatorcontrib><creatorcontrib>Caceres, Javier F</creatorcontrib><title>Nucleo-cytoplasmic shuttling of splicing factor SRSF1 is required for development and cilia function</title><title>eLife</title><addtitle>Elife</addtitle><description>Shuttling RNA-binding proteins coordinate nuclear and cytoplasmic steps of gene expression. The SR family proteins regulate RNA splicing in the nucleus and a subset of them, including SRSF1, shuttles between the nucleus and cytoplasm affecting post-splicing processes. However, the physiological significance of this remains unclear. Here, we used genome editing to knock-in a nuclear retention signal (NRS) in
to create a mouse model harboring an SRSF1 protein that is retained exclusively in the nucleus.
mutants displayed small body size, hydrocephalus, and immotile sperm, all traits associated with ciliary defects. We observed reduced translation of a subset of mRNAs and decreased abundance of proteins involved in multiciliogenesis, with disruption of ciliary ultrastructure and motility in cells and tissues derived from this mouse model. These results demonstrate that SRSF1 shuttling is used to reprogram gene expression networks in the context of high cellular demands, as observed here, during motile ciliogenesis.</description><subject>alternative splicing</subject><subject>Analysis</subject><subject>Animals</subject><subject>Binding proteins</subject><subject>Biochemistry and Chemical Biology</subject><subject>Body size</subject><subject>Cell cycle</subject><subject>Cell Nucleus - metabolism</subject><subject>Chromosomes and Gene Expression</subject><subject>Cilia</subject><subject>Cilia - metabolism</subject><subject>CRISPR</subject><subject>Cytoplasm</subject><subject>Cytoplasm - metabolism</subject><subject>Gene expression</subject><subject>Genome editing</subject><subject>Genomes</subject><subject>Genomics</subject><subject>Hydrocephalus</subject><subject>Kinases</subject><subject>Localization</subject><subject>Male</subject><subject>Mice</subject><subject>motile cilia</subject><subject>mRNA translation</subject><subject>Physiological aspects</subject><subject>Protein binding</subject><subject>Proteins</subject><subject>RNA</subject><subject>RNA polymerase</subject><subject>RNA-binding protein</subject><subject>RNA-binding proteins</subject><subject>Serine-Arginine Splicing Factors - genetics</subject><subject>Serine-Arginine Splicing Factors - metabolism</subject><subject>Splicing factors</subject><subject>SR proteins</subject><subject>SRSF1</subject><subject>Stem cells</subject><subject>Testes</subject><subject>Ultrastructure</subject><issn>2050-084X</issn><issn>2050-084X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>DOA</sourceid><recordid>eNptktFrFDEQxhex2NL2yXdZ8MUieyabZJN9EUqxenAo9BR8C9lkcs2xt9km2WL_e3N3tfbE5CHD5Ddf-CZTFK8xmnHG6AdYOAuzhmFEXxQnNWKoQoL-fPksPi7OY1yjvDgVArevimNCCRENYSeF-TrpHnylH5IfexU3Tpfxdkqpd8Oq9LaMY-_0NrZKJx_K5c3yGpculgHuJhfAlDZnDdxD78cNDKlUgym1650q7TTo5PxwVhxZ1Uc4fzxPix_Xn75ffakW3z7Pry4XlWa8SZUVnNWsbgW0LaZaM6HaRmEOVAB0yBisOVLIbm0w07S4E8KYmhqqTMsRIqfFfK9rvFrLMbiNCg_SKyd3CR9WUoXksmEpKLOIE5FfwhR3dYe5rWlDqOlaRJs6a33ca41TtwGjs7Og-gPRw5vB3cqVv5eCZBMtywLvHgWCv5sgJrlxUUPfqwH8FGXNGGeEMMEz-vYfdO2nMORWya1UjSlh7C-1UtmAG6zP7-qtqLxsOK4ZwghnavYfKm8D-W_9ANbl_EHBxUFBZhL8Sis1xSjny5tD9v2e1cHHGMA-9QMjuZ1HuZtHuZvHTL953sIn9s_0kd9COth_</recordid><startdate>20210802</startdate><enddate>20210802</enddate><creator>Haward, Fiona</creator><creator>Maslon, Magdalena M</creator><creator>Yeyati, Patricia L</creator><creator>Bellora, Nicolas</creator><creator>Hansen, Jan N</creator><creator>Aitken, Stuart</creator><creator>Lawson, Jennifer</creator><creator>von Kriegsheim, Alex</creator><creator>Wachten, Dagmar</creator><creator>Mill, Pleasantine</creator><creator>Adams, Ian R</creator><creator>Caceres, Javier F</creator><general>eLife Science Publications, Ltd</general><general>eLife Sciences Publications Ltd</general><general>eLife Sciences Publications, Ltd</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>ISR</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>88I</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope><orcidid>https://orcid.org/0000-0001-8838-1271</orcidid><orcidid>https://orcid.org/0000-0001-8025-6169</orcidid><orcidid>https://orcid.org/0000-0001-9048-5600</orcidid><orcidid>https://orcid.org/0000-0003-4800-6332</orcidid><orcidid>https://orcid.org/0000-0002-1050-1306</orcidid><orcidid>https://orcid.org/0000-0002-0489-7535</orcidid><orcidid>https://orcid.org/0000-0001-6637-3465</orcidid></search><sort><creationdate>20210802</creationdate><title>Nucleo-cytoplasmic shuttling of splicing factor SRSF1 is required for development and cilia function</title><author>Haward, Fiona ; Maslon, Magdalena M ; Yeyati, Patricia L ; Bellora, Nicolas ; Hansen, Jan N ; Aitken, Stuart ; Lawson, Jennifer ; von Kriegsheim, Alex ; Wachten, Dagmar ; Mill, Pleasantine ; Adams, Ian R ; Caceres, Javier F</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c576t-f87525298e9914cc58a96a17e48eeb0dd1c70a0f74885d691b88dd24d4ad97003</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>alternative splicing</topic><topic>Analysis</topic><topic>Animals</topic><topic>Binding proteins</topic><topic>Biochemistry and Chemical Biology</topic><topic>Body size</topic><topic>Cell cycle</topic><topic>Cell Nucleus - metabolism</topic><topic>Chromosomes and Gene Expression</topic><topic>Cilia</topic><topic>Cilia - metabolism</topic><topic>CRISPR</topic><topic>Cytoplasm</topic><topic>Cytoplasm - metabolism</topic><topic>Gene expression</topic><topic>Genome editing</topic><topic>Genomes</topic><topic>Genomics</topic><topic>Hydrocephalus</topic><topic>Kinases</topic><topic>Localization</topic><topic>Male</topic><topic>Mice</topic><topic>motile cilia</topic><topic>mRNA translation</topic><topic>Physiological aspects</topic><topic>Protein binding</topic><topic>Proteins</topic><topic>RNA</topic><topic>RNA polymerase</topic><topic>RNA-binding protein</topic><topic>RNA-binding proteins</topic><topic>Serine-Arginine Splicing Factors - genetics</topic><topic>Serine-Arginine Splicing Factors - metabolism</topic><topic>Splicing factors</topic><topic>SR proteins</topic><topic>SRSF1</topic><topic>Stem cells</topic><topic>Testes</topic><topic>Ultrastructure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Haward, Fiona</creatorcontrib><creatorcontrib>Maslon, Magdalena M</creatorcontrib><creatorcontrib>Yeyati, Patricia L</creatorcontrib><creatorcontrib>Bellora, Nicolas</creatorcontrib><creatorcontrib>Hansen, Jan N</creatorcontrib><creatorcontrib>Aitken, Stuart</creatorcontrib><creatorcontrib>Lawson, Jennifer</creatorcontrib><creatorcontrib>von Kriegsheim, Alex</creatorcontrib><creatorcontrib>Wachten, Dagmar</creatorcontrib><creatorcontrib>Mill, Pleasantine</creatorcontrib><creatorcontrib>Adams, Ian R</creatorcontrib><creatorcontrib>Caceres, Javier F</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>ProQuest Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection (Proquest) (PQ_SDU_P3)</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biological Sciences</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>ProQuest Science Journals</collection><collection>Biological Science Database</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>eLife</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Haward, Fiona</au><au>Maslon, Magdalena M</au><au>Yeyati, Patricia L</au><au>Bellora, Nicolas</au><au>Hansen, Jan N</au><au>Aitken, Stuart</au><au>Lawson, Jennifer</au><au>von Kriegsheim, Alex</au><au>Wachten, Dagmar</au><au>Mill, Pleasantine</au><au>Adams, Ian R</au><au>Caceres, Javier F</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Nucleo-cytoplasmic shuttling of splicing factor SRSF1 is required for development and cilia function</atitle><jtitle>eLife</jtitle><addtitle>Elife</addtitle><date>2021-08-02</date><risdate>2021</risdate><volume>10</volume><issn>2050-084X</issn><eissn>2050-084X</eissn><abstract>Shuttling RNA-binding proteins coordinate nuclear and cytoplasmic steps of gene expression. The SR family proteins regulate RNA splicing in the nucleus and a subset of them, including SRSF1, shuttles between the nucleus and cytoplasm affecting post-splicing processes. However, the physiological significance of this remains unclear. Here, we used genome editing to knock-in a nuclear retention signal (NRS) in
to create a mouse model harboring an SRSF1 protein that is retained exclusively in the nucleus.
mutants displayed small body size, hydrocephalus, and immotile sperm, all traits associated with ciliary defects. We observed reduced translation of a subset of mRNAs and decreased abundance of proteins involved in multiciliogenesis, with disruption of ciliary ultrastructure and motility in cells and tissues derived from this mouse model. These results demonstrate that SRSF1 shuttling is used to reprogram gene expression networks in the context of high cellular demands, as observed here, during motile ciliogenesis.</abstract><cop>England</cop><pub>eLife Science Publications, Ltd</pub><pmid>34338635</pmid><doi>10.7554/eLife.65104</doi><orcidid>https://orcid.org/0000-0001-8838-1271</orcidid><orcidid>https://orcid.org/0000-0001-8025-6169</orcidid><orcidid>https://orcid.org/0000-0001-9048-5600</orcidid><orcidid>https://orcid.org/0000-0003-4800-6332</orcidid><orcidid>https://orcid.org/0000-0002-1050-1306</orcidid><orcidid>https://orcid.org/0000-0002-0489-7535</orcidid><orcidid>https://orcid.org/0000-0001-6637-3465</orcidid><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; DOAJ Directory of Open Access Journals; PubMed Central; EZB Electronic Journals Library; PubMed Central Open Access |
| subjects | alternative splicing Analysis Animals Binding proteins Biochemistry and Chemical Biology Body size Cell cycle Cell Nucleus - metabolism Chromosomes and Gene Expression Cilia Cilia - metabolism CRISPR Cytoplasm Cytoplasm - metabolism Gene expression Genome editing Genomes Genomics Hydrocephalus Kinases Localization Male Mice motile cilia mRNA translation Physiological aspects Protein binding Proteins RNA RNA polymerase RNA-binding protein RNA-binding proteins Serine-Arginine Splicing Factors - genetics Serine-Arginine Splicing Factors - metabolism Splicing factors SR proteins SRSF1 Stem cells Testes Ultrastructure |
| title | Nucleo-cytoplasmic shuttling of splicing factor SRSF1 is required for development and cilia function |
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