SUMO conjugation regulates immune signalling

Post-translational modifications (PTMs) are critical drivers and attenuators for proteins that regulate immune signalling cascades in host defence. In this review, we explore functional roles for one such PTM, the small ubiquitin-like modifier (SUMO). Very few of the SUMO conjugation targets identif...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Fly (Austin, Tex.) Tex.), 2020-10, Vol.14 (1-4), p.62-79
Hauptverfasser: Hegde, Sushmitha, Soory, Amarendranath, Kaduskar, Bhagyashree, Ratnaparkhi, Girish S.
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 79
container_issue 1-4
container_start_page 62
container_title Fly (Austin, Tex.)
container_volume 14
creator Hegde, Sushmitha
Soory, Amarendranath
Kaduskar, Bhagyashree
Ratnaparkhi, Girish S.
description Post-translational modifications (PTMs) are critical drivers and attenuators for proteins that regulate immune signalling cascades in host defence. In this review, we explore functional roles for one such PTM, the small ubiquitin-like modifier (SUMO). Very few of the SUMO conjugation targets identified by proteomic studies have been validated in terms of their roles in host defence. Here, we compare and contrast potential SUMO substrate proteins in immune signalling for flies and mammals, with an emphasis on NFκB pathways. We discuss, using the few mechanistic studies that exist for validated targets, the effect of SUMO conjugation on signalling and also explore current molecular models that explain regulation by SUMO. We also discuss in detail roles of evolutionary conservation of mechanisms, SUMO interaction motifs, crosstalk of SUMO with other PTMs, emerging concepts such as group SUMOylation and finally, the potentially transforming roles for genome-editing technologies in studying the effect of PTMs.
doi_str_mv 10.1080/19336934.2020.1808402
format Article
fullrecord <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmed_primary_32777975</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><doaj_id>oai_doaj_org_article_f5dcd2968af24cdf88a27f09027b06b6</doaj_id><sourcerecordid>2432854857</sourcerecordid><originalsourceid>FETCH-LOGICAL-c534t-603ef1cbfef5189bb480cbbaaa53c2ef6c1178e1b67880942b8570e325fdf46e3</originalsourceid><addsrcrecordid>eNp9kU9vEzEQxS0Eom3gI4By5ECK_9t7QaCKQqWiHqBna-y1F0deu9i7oH57NiSN6IWTrTdv3oz9Q-gVwecEa_yOdIzJjvFziukiaaw5pk_Q6U7fyI7Tp8c74yforLUtxkIJLJ6jE0aVUp0Sp-jtt9uvN2tX8nYeYIolr6sf5gSTb-s4jnP26xaHDCnFPLxAzwKk5l8ezhW6vfz0_eLL5vrm89XFx-uNE4xPG4mZD8TZ4IMgurOWa-ysBQDBHPVBOkKU9sRKpTVeVrVaKOwZFaEPXHq2Qlf73L7A1tzVOEK9NwWi-SuUOhioU3TJmyB619NOagiUuz5oDVQF3GGqLJZWLlnv91l3sx1973yeKqRHoY8rOf4wQ_lllCJcLD-4Qm8OAbX8nH2bzBib8ylB9mVuhnJGteDLExar2FtdLa1VH45jCDY7auaBmtlRMwdqS9_rf3c8dj1gWgwf9oaYQ6kj_C419WaC-1RqqJBdbIb9f8YfERenGQ</addsrcrecordid><sourcetype>Open Website</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2432854857</pqid></control><display><type>article</type><title>SUMO conjugation regulates immune signalling</title><source>MEDLINE</source><source>EZB-FREE-00999 freely available EZB journals</source><source>PubMed Central</source><creator>Hegde, Sushmitha ; Soory, Amarendranath ; Kaduskar, Bhagyashree ; Ratnaparkhi, Girish S.</creator><creatorcontrib>Hegde, Sushmitha ; Soory, Amarendranath ; Kaduskar, Bhagyashree ; Ratnaparkhi, Girish S.</creatorcontrib><description>Post-translational modifications (PTMs) are critical drivers and attenuators for proteins that regulate immune signalling cascades in host defence. In this review, we explore functional roles for one such PTM, the small ubiquitin-like modifier (SUMO). Very few of the SUMO conjugation targets identified by proteomic studies have been validated in terms of their roles in host defence. Here, we compare and contrast potential SUMO substrate proteins in immune signalling for flies and mammals, with an emphasis on NFκB pathways. We discuss, using the few mechanistic studies that exist for validated targets, the effect of SUMO conjugation on signalling and also explore current molecular models that explain regulation by SUMO. We also discuss in detail roles of evolutionary conservation of mechanisms, SUMO interaction motifs, crosstalk of SUMO with other PTMs, emerging concepts such as group SUMOylation and finally, the potentially transforming roles for genome-editing technologies in studying the effect of PTMs.</description><identifier>ISSN: 1933-6934</identifier><identifier>EISSN: 1933-6942</identifier><identifier>DOI: 10.1080/19336934.2020.1808402</identifier><identifier>PMID: 32777975</identifier><language>eng</language><publisher>United States: Taylor &amp; Francis</publisher><subject>Animals ; CRISPR ; crosstalk ; Drosophila melanogaster ; Drosophila Proteins - genetics ; Drosophila Proteins - metabolism ; Gene Expression Regulation - immunology ; Immunity ; nfκb ; Protein Processing, Post-Translational - immunology ; ptm ; Review ; signal transduction ; Signal Transduction - immunology ; sim ; Small Ubiquitin-Related Modifier Proteins - genetics ; Small Ubiquitin-Related Modifier Proteins - metabolism ; transcriptional Activation/Repression ; ubiquitin</subject><ispartof>Fly (Austin, Tex.), 2020-10, Vol.14 (1-4), p.62-79</ispartof><rights>2020 Informa UK Limited, trading as Taylor &amp; Francis Group 2020</rights><rights>2020 Informa UK Limited, trading as Taylor &amp; Francis Group 2020 Informa UK Limited, trading as Taylor &amp; Francis Group</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c534t-603ef1cbfef5189bb480cbbaaa53c2ef6c1178e1b67880942b8570e325fdf46e3</citedby><cites>FETCH-LOGICAL-c534t-603ef1cbfef5189bb480cbbaaa53c2ef6c1178e1b67880942b8570e325fdf46e3</cites><orcidid>0000-0003-3023-6121 ; 0000-0001-7615-3140 ; 0000-0002-8506-1309 ; 0000-0003-0777-962X</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/PMC7714519/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7714519/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27903,27904,53770,53772</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32777975$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hegde, Sushmitha</creatorcontrib><creatorcontrib>Soory, Amarendranath</creatorcontrib><creatorcontrib>Kaduskar, Bhagyashree</creatorcontrib><creatorcontrib>Ratnaparkhi, Girish S.</creatorcontrib><title>SUMO conjugation regulates immune signalling</title><title>Fly (Austin, Tex.)</title><addtitle>Fly (Austin)</addtitle><description>Post-translational modifications (PTMs) are critical drivers and attenuators for proteins that regulate immune signalling cascades in host defence. In this review, we explore functional roles for one such PTM, the small ubiquitin-like modifier (SUMO). Very few of the SUMO conjugation targets identified by proteomic studies have been validated in terms of their roles in host defence. Here, we compare and contrast potential SUMO substrate proteins in immune signalling for flies and mammals, with an emphasis on NFκB pathways. We discuss, using the few mechanistic studies that exist for validated targets, the effect of SUMO conjugation on signalling and also explore current molecular models that explain regulation by SUMO. We also discuss in detail roles of evolutionary conservation of mechanisms, SUMO interaction motifs, crosstalk of SUMO with other PTMs, emerging concepts such as group SUMOylation and finally, the potentially transforming roles for genome-editing technologies in studying the effect of PTMs.</description><subject>Animals</subject><subject>CRISPR</subject><subject>crosstalk</subject><subject>Drosophila melanogaster</subject><subject>Drosophila Proteins - genetics</subject><subject>Drosophila Proteins - metabolism</subject><subject>Gene Expression Regulation - immunology</subject><subject>Immunity</subject><subject>nfκb</subject><subject>Protein Processing, Post-Translational - immunology</subject><subject>ptm</subject><subject>Review</subject><subject>signal transduction</subject><subject>Signal Transduction - immunology</subject><subject>sim</subject><subject>Small Ubiquitin-Related Modifier Proteins - genetics</subject><subject>Small Ubiquitin-Related Modifier Proteins - metabolism</subject><subject>transcriptional Activation/Repression</subject><subject>ubiquitin</subject><issn>1933-6934</issn><issn>1933-6942</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>DOA</sourceid><recordid>eNp9kU9vEzEQxS0Eom3gI4By5ECK_9t7QaCKQqWiHqBna-y1F0deu9i7oH57NiSN6IWTrTdv3oz9Q-gVwecEa_yOdIzJjvFziukiaaw5pk_Q6U7fyI7Tp8c74yforLUtxkIJLJ6jE0aVUp0Sp-jtt9uvN2tX8nYeYIolr6sf5gSTb-s4jnP26xaHDCnFPLxAzwKk5l8ezhW6vfz0_eLL5vrm89XFx-uNE4xPG4mZD8TZ4IMgurOWa-ysBQDBHPVBOkKU9sRKpTVeVrVaKOwZFaEPXHq2Qlf73L7A1tzVOEK9NwWi-SuUOhioU3TJmyB619NOagiUuz5oDVQF3GGqLJZWLlnv91l3sx1973yeKqRHoY8rOf4wQ_lllCJcLD-4Qm8OAbX8nH2bzBib8ylB9mVuhnJGteDLExar2FtdLa1VH45jCDY7auaBmtlRMwdqS9_rf3c8dj1gWgwf9oaYQ6kj_C419WaC-1RqqJBdbIb9f8YfERenGQ</recordid><startdate>20201001</startdate><enddate>20201001</enddate><creator>Hegde, Sushmitha</creator><creator>Soory, Amarendranath</creator><creator>Kaduskar, Bhagyashree</creator><creator>Ratnaparkhi, Girish S.</creator><general>Taylor &amp; Francis</general><general>Taylor &amp; Francis Group</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>7X8</scope><scope>5PM</scope><scope>DOA</scope><orcidid>https://orcid.org/0000-0003-3023-6121</orcidid><orcidid>https://orcid.org/0000-0001-7615-3140</orcidid><orcidid>https://orcid.org/0000-0002-8506-1309</orcidid><orcidid>https://orcid.org/0000-0003-0777-962X</orcidid></search><sort><creationdate>20201001</creationdate><title>SUMO conjugation regulates immune signalling</title><author>Hegde, Sushmitha ; Soory, Amarendranath ; Kaduskar, Bhagyashree ; Ratnaparkhi, Girish S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c534t-603ef1cbfef5189bb480cbbaaa53c2ef6c1178e1b67880942b8570e325fdf46e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Animals</topic><topic>CRISPR</topic><topic>crosstalk</topic><topic>Drosophila melanogaster</topic><topic>Drosophila Proteins - genetics</topic><topic>Drosophila Proteins - metabolism</topic><topic>Gene Expression Regulation - immunology</topic><topic>Immunity</topic><topic>nfκb</topic><topic>Protein Processing, Post-Translational - immunology</topic><topic>ptm</topic><topic>Review</topic><topic>signal transduction</topic><topic>Signal Transduction - immunology</topic><topic>sim</topic><topic>Small Ubiquitin-Related Modifier Proteins - genetics</topic><topic>Small Ubiquitin-Related Modifier Proteins - metabolism</topic><topic>transcriptional Activation/Repression</topic><topic>ubiquitin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hegde, Sushmitha</creatorcontrib><creatorcontrib>Soory, Amarendranath</creatorcontrib><creatorcontrib>Kaduskar, Bhagyashree</creatorcontrib><creatorcontrib>Ratnaparkhi, Girish 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>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>Fly (Austin, Tex.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hegde, Sushmitha</au><au>Soory, Amarendranath</au><au>Kaduskar, Bhagyashree</au><au>Ratnaparkhi, Girish S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>SUMO conjugation regulates immune signalling</atitle><jtitle>Fly (Austin, Tex.)</jtitle><addtitle>Fly (Austin)</addtitle><date>2020-10-01</date><risdate>2020</risdate><volume>14</volume><issue>1-4</issue><spage>62</spage><epage>79</epage><pages>62-79</pages><issn>1933-6934</issn><eissn>1933-6942</eissn><abstract>Post-translational modifications (PTMs) are critical drivers and attenuators for proteins that regulate immune signalling cascades in host defence. In this review, we explore functional roles for one such PTM, the small ubiquitin-like modifier (SUMO). Very few of the SUMO conjugation targets identified by proteomic studies have been validated in terms of their roles in host defence. Here, we compare and contrast potential SUMO substrate proteins in immune signalling for flies and mammals, with an emphasis on NFκB pathways. We discuss, using the few mechanistic studies that exist for validated targets, the effect of SUMO conjugation on signalling and also explore current molecular models that explain regulation by SUMO. We also discuss in detail roles of evolutionary conservation of mechanisms, SUMO interaction motifs, crosstalk of SUMO with other PTMs, emerging concepts such as group SUMOylation and finally, the potentially transforming roles for genome-editing technologies in studying the effect of PTMs.</abstract><cop>United States</cop><pub>Taylor &amp; Francis</pub><pmid>32777975</pmid><doi>10.1080/19336934.2020.1808402</doi><tpages>18</tpages><orcidid>https://orcid.org/0000-0003-3023-6121</orcidid><orcidid>https://orcid.org/0000-0001-7615-3140</orcidid><orcidid>https://orcid.org/0000-0002-8506-1309</orcidid><orcidid>https://orcid.org/0000-0003-0777-962X</orcidid><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 1933-6934
ispartof Fly (Austin, Tex.), 2020-10, Vol.14 (1-4), p.62-79
issn 1933-6934
1933-6942
language eng
recordid cdi_pubmed_primary_32777975
source MEDLINE; EZB-FREE-00999 freely available EZB journals; PubMed Central
subjects Animals
CRISPR
crosstalk
Drosophila melanogaster
Drosophila Proteins - genetics
Drosophila Proteins - metabolism
Gene Expression Regulation - immunology
Immunity
nfκb
Protein Processing, Post-Translational - immunology
ptm
Review
signal transduction
Signal Transduction - immunology
sim
Small Ubiquitin-Related Modifier Proteins - genetics
Small Ubiquitin-Related Modifier Proteins - metabolism
transcriptional Activation/Repression
ubiquitin
title SUMO conjugation regulates immune signalling
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-21T15%3A01%3A32IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=SUMO%20conjugation%20regulates%20immune%20signalling&rft.jtitle=Fly%20(Austin,%20Tex.)&rft.au=Hegde,%20Sushmitha&rft.date=2020-10-01&rft.volume=14&rft.issue=1-4&rft.spage=62&rft.epage=79&rft.pages=62-79&rft.issn=1933-6934&rft.eissn=1933-6942&rft_id=info:doi/10.1080/19336934.2020.1808402&rft_dat=%3Cproquest_pubme%3E2432854857%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2432854857&rft_id=info:pmid/32777975&rft_doaj_id=oai_doaj_org_article_f5dcd2968af24cdf88a27f09027b06b6&rfr_iscdi=true