The SDS22:PP1:I3 complex: SDS22 binding to PP1 loosens the active site metal to prime metal exchange
SDS22 and Inhibitor-3 (I3) are two ancient regulators of protein phosphatase 1 (PP1) that regulate multiple essential biological processes. Both SDS22 and I3 form stable dimeric complexes with PP1; however, and atypically for PP1 regulators, they also form a triple complex, where both proteins bind...
Gespeichert in:
| Veröffentlicht in: | The Journal of biological chemistry 2024-01, Vol.300 (1), p.105515-105515, Article 105515 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 105515 |
|---|---|
| container_issue | 1 |
| container_start_page | 105515 |
| container_title | The Journal of biological chemistry |
| container_volume | 300 |
| creator | Choy, Meng S Srivastava, Gautam Robinson, Lucy C Tatchell, Kelly Page, Rebecca Peti, Wolfgang |
| description | SDS22 and Inhibitor-3 (I3) are two ancient regulators of protein phosphatase 1 (PP1) that regulate multiple essential biological processes. Both SDS22 and I3 form stable dimeric complexes with PP1; however, and atypically for PP1 regulators, they also form a triple complex, where both proteins bind to PP1 simultaneously (SPI complex). Here we report the crystal structure of the SPI complex. While both regulators bind PP1 in conformations identical to those observed in their individual PP1 complexes, PP1 adopts the SDS22-bound conformation, which lacks its M1 metal. Unexpectedly, surface plasmon resonance (SPR) revealed that the affinity of I3 for the SDS22:PP1 complex is ∼10-fold lower than PP1 alone. We show that this change in binding affinity is solely due to the interaction of I3 with the PP1 active site, specifically PP1's M2 metal, demonstrating that SDS22 likely allows for PP1 M2 metal exchange and thus PP1 biogenesis. |
| doi_str_mv | 10.1016/j.jbc.2023.105515 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_10776994</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2896810971</sourcerecordid><originalsourceid>FETCH-LOGICAL-c3425-77c6152ba268a1caa6c93b2f3589a9518240d81957aadec92c699ba899b8b50a3</originalsourceid><addsrcrecordid>eNpVUcFu1DAQtRCIbgsfwAVZnLhk8dhxYu8FVaVApUpUapG4WRPHu-tVYi-xtyp_j1dpK5iDR-N5782MHiHvgC2BQfNpt9x1dskZF6WWEuQLsgCmRCUk_HpJFoxxqDSX6oScprRjJWoNr8mJUKzmtZYL0t9tHb39csv56uYGVleC2jjuB_ewmn9p50Pvw4bmSAuADjEmFxLNhYY2-3tHk8-Oji7jcATtJz8-le7BbjFs3Bvyao1Dcm8f8xn5-fXy7uJ7df3j29XF-XVlRc1l1ba2Ack75I1CsIiN1aLjayGVRi1B8Zr1CrRsEXtnNbeN1h2q8qhOMhRn5POsuz90o-utC3nCwRxXwumPiejN_53gt2YT7w2wti1adVH4MCvElL1JtpxmtzaG4Gw2vMQM-vg4Zoq_Dy5lM_pk3TBgcPGQDFe6UcB0CwUKM9ROMaXJrZ-XAWaOHpqdKR6ao4dm9rBw3v97xTPjyTTxF8PNlkg</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2896810971</pqid></control><display><type>article</type><title>The SDS22:PP1:I3 complex: SDS22 binding to PP1 loosens the active site metal to prime metal exchange</title><source>MEDLINE</source><source>DOAJ Directory of Open Access Journals</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><creator>Choy, Meng S ; Srivastava, Gautam ; Robinson, Lucy C ; Tatchell, Kelly ; Page, Rebecca ; Peti, Wolfgang</creator><creatorcontrib>Choy, Meng S ; Srivastava, Gautam ; Robinson, Lucy C ; Tatchell, Kelly ; Page, Rebecca ; Peti, Wolfgang</creatorcontrib><description>SDS22 and Inhibitor-3 (I3) are two ancient regulators of protein phosphatase 1 (PP1) that regulate multiple essential biological processes. Both SDS22 and I3 form stable dimeric complexes with PP1; however, and atypically for PP1 regulators, they also form a triple complex, where both proteins bind to PP1 simultaneously (SPI complex). Here we report the crystal structure of the SPI complex. While both regulators bind PP1 in conformations identical to those observed in their individual PP1 complexes, PP1 adopts the SDS22-bound conformation, which lacks its M1 metal. Unexpectedly, surface plasmon resonance (SPR) revealed that the affinity of I3 for the SDS22:PP1 complex is ∼10-fold lower than PP1 alone. We show that this change in binding affinity is solely due to the interaction of I3 with the PP1 active site, specifically PP1's M2 metal, demonstrating that SDS22 likely allows for PP1 M2 metal exchange and thus PP1 biogenesis.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/j.jbc.2023.105515</identifier><identifier>PMID: 38042495</identifier><language>eng</language><publisher>United States: Elsevier</publisher><subject>Catalytic Domain ; Cryoelectron Microscopy ; Humans ; Metals - chemistry ; Protein Binding ; Protein Phosphatase 1 - chemistry ; Ubiquitin-Protein Ligases - chemistry</subject><ispartof>The Journal of biological chemistry, 2024-01, Vol.300 (1), p.105515-105515, Article 105515</ispartof><rights>Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved.</rights><rights>2023 The Authors 2023</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3425-77c6152ba268a1caa6c93b2f3589a9518240d81957aadec92c699ba899b8b50a3</citedby><cites>FETCH-LOGICAL-c3425-77c6152ba268a1caa6c93b2f3589a9518240d81957aadec92c699ba899b8b50a3</cites><orcidid>0000-0002-8703-8903 ; 0000-0002-5330-410X ; 0000-0002-7590-3031 ; 000000025330410X ; 0000000275903031 ; 0000000287038903</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/PMC10776994/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC10776994/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/38042495$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/2222994$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Choy, Meng S</creatorcontrib><creatorcontrib>Srivastava, Gautam</creatorcontrib><creatorcontrib>Robinson, Lucy C</creatorcontrib><creatorcontrib>Tatchell, Kelly</creatorcontrib><creatorcontrib>Page, Rebecca</creatorcontrib><creatorcontrib>Peti, Wolfgang</creatorcontrib><title>The SDS22:PP1:I3 complex: SDS22 binding to PP1 loosens the active site metal to prime metal exchange</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>SDS22 and Inhibitor-3 (I3) are two ancient regulators of protein phosphatase 1 (PP1) that regulate multiple essential biological processes. Both SDS22 and I3 form stable dimeric complexes with PP1; however, and atypically for PP1 regulators, they also form a triple complex, where both proteins bind to PP1 simultaneously (SPI complex). Here we report the crystal structure of the SPI complex. While both regulators bind PP1 in conformations identical to those observed in their individual PP1 complexes, PP1 adopts the SDS22-bound conformation, which lacks its M1 metal. Unexpectedly, surface plasmon resonance (SPR) revealed that the affinity of I3 for the SDS22:PP1 complex is ∼10-fold lower than PP1 alone. We show that this change in binding affinity is solely due to the interaction of I3 with the PP1 active site, specifically PP1's M2 metal, demonstrating that SDS22 likely allows for PP1 M2 metal exchange and thus PP1 biogenesis.</description><subject>Catalytic Domain</subject><subject>Cryoelectron Microscopy</subject><subject>Humans</subject><subject>Metals - chemistry</subject><subject>Protein Binding</subject><subject>Protein Phosphatase 1 - chemistry</subject><subject>Ubiquitin-Protein Ligases - chemistry</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVUcFu1DAQtRCIbgsfwAVZnLhk8dhxYu8FVaVApUpUapG4WRPHu-tVYi-xtyp_j1dpK5iDR-N5782MHiHvgC2BQfNpt9x1dskZF6WWEuQLsgCmRCUk_HpJFoxxqDSX6oScprRjJWoNr8mJUKzmtZYL0t9tHb39csv56uYGVleC2jjuB_ewmn9p50Pvw4bmSAuADjEmFxLNhYY2-3tHk8-Oji7jcATtJz8-le7BbjFs3Bvyao1Dcm8f8xn5-fXy7uJ7df3j29XF-XVlRc1l1ba2Ack75I1CsIiN1aLjayGVRi1B8Zr1CrRsEXtnNbeN1h2q8qhOMhRn5POsuz90o-utC3nCwRxXwumPiejN_53gt2YT7w2wti1adVH4MCvElL1JtpxmtzaG4Gw2vMQM-vg4Zoq_Dy5lM_pk3TBgcPGQDFe6UcB0CwUKM9ROMaXJrZ-XAWaOHpqdKR6ao4dm9rBw3v97xTPjyTTxF8PNlkg</recordid><startdate>20240101</startdate><enddate>20240101</enddate><creator>Choy, Meng S</creator><creator>Srivastava, Gautam</creator><creator>Robinson, Lucy C</creator><creator>Tatchell, Kelly</creator><creator>Page, Rebecca</creator><creator>Peti, Wolfgang</creator><general>Elsevier</general><general>American Society for Biochemistry and Molecular Biology</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>OTOTI</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-8703-8903</orcidid><orcidid>https://orcid.org/0000-0002-5330-410X</orcidid><orcidid>https://orcid.org/0000-0002-7590-3031</orcidid><orcidid>https://orcid.org/000000025330410X</orcidid><orcidid>https://orcid.org/0000000275903031</orcidid><orcidid>https://orcid.org/0000000287038903</orcidid></search><sort><creationdate>20240101</creationdate><title>The SDS22:PP1:I3 complex: SDS22 binding to PP1 loosens the active site metal to prime metal exchange</title><author>Choy, Meng S ; Srivastava, Gautam ; Robinson, Lucy C ; Tatchell, Kelly ; Page, Rebecca ; Peti, Wolfgang</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3425-77c6152ba268a1caa6c93b2f3589a9518240d81957aadec92c699ba899b8b50a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>Catalytic Domain</topic><topic>Cryoelectron Microscopy</topic><topic>Humans</topic><topic>Metals - chemistry</topic><topic>Protein Binding</topic><topic>Protein Phosphatase 1 - chemistry</topic><topic>Ubiquitin-Protein Ligases - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Choy, Meng S</creatorcontrib><creatorcontrib>Srivastava, Gautam</creatorcontrib><creatorcontrib>Robinson, Lucy C</creatorcontrib><creatorcontrib>Tatchell, Kelly</creatorcontrib><creatorcontrib>Page, Rebecca</creatorcontrib><creatorcontrib>Peti, Wolfgang</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>OSTI.GOV</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Choy, Meng S</au><au>Srivastava, Gautam</au><au>Robinson, Lucy C</au><au>Tatchell, Kelly</au><au>Page, Rebecca</au><au>Peti, Wolfgang</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The SDS22:PP1:I3 complex: SDS22 binding to PP1 loosens the active site metal to prime metal exchange</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2024-01-01</date><risdate>2024</risdate><volume>300</volume><issue>1</issue><spage>105515</spage><epage>105515</epage><pages>105515-105515</pages><artnum>105515</artnum><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>SDS22 and Inhibitor-3 (I3) are two ancient regulators of protein phosphatase 1 (PP1) that regulate multiple essential biological processes. Both SDS22 and I3 form stable dimeric complexes with PP1; however, and atypically for PP1 regulators, they also form a triple complex, where both proteins bind to PP1 simultaneously (SPI complex). Here we report the crystal structure of the SPI complex. While both regulators bind PP1 in conformations identical to those observed in their individual PP1 complexes, PP1 adopts the SDS22-bound conformation, which lacks its M1 metal. Unexpectedly, surface plasmon resonance (SPR) revealed that the affinity of I3 for the SDS22:PP1 complex is ∼10-fold lower than PP1 alone. We show that this change in binding affinity is solely due to the interaction of I3 with the PP1 active site, specifically PP1's M2 metal, demonstrating that SDS22 likely allows for PP1 M2 metal exchange and thus PP1 biogenesis.</abstract><cop>United States</cop><pub>Elsevier</pub><pmid>38042495</pmid><doi>10.1016/j.jbc.2023.105515</doi><tpages>1</tpages><orcidid>https://orcid.org/0000-0002-8703-8903</orcidid><orcidid>https://orcid.org/0000-0002-5330-410X</orcidid><orcidid>https://orcid.org/0000-0002-7590-3031</orcidid><orcidid>https://orcid.org/000000025330410X</orcidid><orcidid>https://orcid.org/0000000275903031</orcidid><orcidid>https://orcid.org/0000000287038903</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 2024-01, Vol.300 (1), p.105515-105515, Article 105515 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_10776994 |
| source | MEDLINE; DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Catalytic Domain Cryoelectron Microscopy Humans Metals - chemistry Protein Binding Protein Phosphatase 1 - chemistry Ubiquitin-Protein Ligases - chemistry |
| title | The SDS22:PP1:I3 complex: SDS22 binding to PP1 loosens the active site metal to prime metal exchange |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-21T10%3A51%3A37IST&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=The%20SDS22:PP1:I3%20complex:%20SDS22%20binding%20to%20PP1%20loosens%20the%20active%20site%20metal%20to%20prime%20metal%20exchange&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=Choy,%20Meng%20S&rft.date=2024-01-01&rft.volume=300&rft.issue=1&rft.spage=105515&rft.epage=105515&rft.pages=105515-105515&rft.artnum=105515&rft.issn=0021-9258&rft.eissn=1083-351X&rft_id=info:doi/10.1016/j.jbc.2023.105515&rft_dat=%3Cproquest_pubme%3E2896810971%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=2896810971&rft_id=info:pmid/38042495&rfr_iscdi=true |