Notch-Jagged complex structure implicates a catch bond in tuning ligand sensitivity
Notch receptor activation initiates cell fate decisions and is distinctive in its reliance on mechanical force and protein glycosylation. The 2.5-angstrom-resolution crystal structure of the extracellular interacting region of Notch1 complexed with an engineered, high-affinity variant of Jagged1 (Ja...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 2017-03, Vol.355 (6331), p.1320-1324 |
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| creator | Luca, Vincent C. Kim, Byoung Choul Ge, Chenghao Kakuda, Shinako Wu, Di Roein-Peikar, Mehdi Haltiwanger, Robert S. Zhu, Cheng Ha, Taekjip Garcia, K. Christopher |
| description | Notch receptor activation initiates cell fate decisions and is distinctive in its reliance on mechanical force and protein glycosylation. The 2.5-angstrom-resolution crystal structure of the extracellular interacting region of Notch1 complexed with an engineered, high-affinity variant of Jagged1 (Jag1) reveals a binding interface that extends ~120 angstroms along five consecutive domains of each protein. O-Linked fucose modifications on Notch1 epidermal growth factor–like (EGF) domains 8 and 12 engage the EGF3 and C2 domains of Jag1, respectively, and different Notch1 domains are favored in binding to Jag1 than those that bind to the Delta-like 4 ligand. Jag1 undergoes conformational changes upon Notch binding, exhibiting catch bond behavior that prolongs interactions in the range of forces required for Notch activation. This mechanism enables cellular forces to regulate binding, discriminate among Notch ligands, and potentiate Notch signaling. |
| doi_str_mv | 10.1126/science.aaf9739 |
| format | Article |
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Christopher</creator><creatorcontrib>Luca, Vincent C. ; Kim, Byoung Choul ; Ge, Chenghao ; Kakuda, Shinako ; Wu, Di ; Roein-Peikar, Mehdi ; Haltiwanger, Robert S. ; Zhu, Cheng ; Ha, Taekjip ; Garcia, K. Christopher ; Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><description>Notch receptor activation initiates cell fate decisions and is distinctive in its reliance on mechanical force and protein glycosylation. The 2.5-angstrom-resolution crystal structure of the extracellular interacting region of Notch1 complexed with an engineered, high-affinity variant of Jagged1 (Jag1) reveals a binding interface that extends ~120 angstroms along five consecutive domains of each protein. O-Linked fucose modifications on Notch1 epidermal growth factor–like (EGF) domains 8 and 12 engage the EGF3 and C2 domains of Jag1, respectively, and different Notch1 domains are favored in binding to Jag1 than those that bind to the Delta-like 4 ligand. Jag1 undergoes conformational changes upon Notch binding, exhibiting catch bond behavior that prolongs interactions in the range of forces required for Notch activation. This mechanism enables cellular forces to regulate binding, discriminate among Notch ligands, and potentiate Notch signaling.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.aaf9739</identifier><identifier>PMID: 28254785</identifier><language>eng</language><publisher>United States: American Association for the Advancement of Science</publisher><subject>Activation ; Affinity ; Animals ; Binding ; Bonding ; Cell activation ; Cell fate ; Crystal structure ; Crystallography, X-Ray ; Epidermal growth factor ; Fucose ; Fucose - chemistry ; Genetic Engineering ; Glycosylation ; Growth factors ; Intracellular Signaling Peptides and Proteins - chemistry ; Jagged-1 Protein - chemistry ; Jagged-1 Protein - genetics ; Jagged-1 Protein - ultrastructure ; Jagged1 protein ; Ligands ; Membrane Proteins - chemistry ; Notch sensitivity ; Notch1 protein ; Notches ; Polysaccharides ; Protein Binding ; Protein Domains ; Proteins ; Rats ; Receptor mechanisms ; Receptor, Notch1 - chemistry ; Receptor, Notch1 - genetics ; Receptor, Notch1 - ultrastructure ; Receptors ; Saccharomyces cerevisiae ; Signal Transduction ; Signaling</subject><ispartof>Science (American Association for the Advancement of Science), 2017-03, Vol.355 (6331), p.1320-1324</ispartof><rights>Copyright © 2017 American Association for the Advancement of Science</rights><rights>Copyright © 2017, American Association for the Advancement of Science.</rights><rights>Copyright © 2017, American Association for the Advancement of Science</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4849-12d48218ac7edeea84fc2751053bb1e9079b92f9014c1eb9cc842f233d92aecc3</citedby><cites>FETCH-LOGICAL-c4849-12d48218ac7edeea84fc2751053bb1e9079b92f9014c1eb9cc842f233d92aecc3</cites><orcidid>0000-0001-9273-0278 ; 0000-0002-1386-3177 ; 0000-0001-8409-7046 ; 0000-0001-9427-5520 ; 0000-0002-1718-565X ; 0000000184097046 ; 0000000194275520 ; 0000000192730278 ; 000000021718565X ; 0000000213863177</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/24918077$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/24918077$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,777,781,800,882,2871,2872,27905,27906,57998,58231</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28254785$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/1353229$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Luca, Vincent C.</creatorcontrib><creatorcontrib>Kim, Byoung Choul</creatorcontrib><creatorcontrib>Ge, Chenghao</creatorcontrib><creatorcontrib>Kakuda, Shinako</creatorcontrib><creatorcontrib>Wu, Di</creatorcontrib><creatorcontrib>Roein-Peikar, Mehdi</creatorcontrib><creatorcontrib>Haltiwanger, Robert S.</creatorcontrib><creatorcontrib>Zhu, Cheng</creatorcontrib><creatorcontrib>Ha, Taekjip</creatorcontrib><creatorcontrib>Garcia, K. Christopher</creatorcontrib><creatorcontrib>Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><title>Notch-Jagged complex structure implicates a catch bond in tuning ligand sensitivity</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>Notch receptor activation initiates cell fate decisions and is distinctive in its reliance on mechanical force and protein glycosylation. The 2.5-angstrom-resolution crystal structure of the extracellular interacting region of Notch1 complexed with an engineered, high-affinity variant of Jagged1 (Jag1) reveals a binding interface that extends ~120 angstroms along five consecutive domains of each protein. O-Linked fucose modifications on Notch1 epidermal growth factor–like (EGF) domains 8 and 12 engage the EGF3 and C2 domains of Jag1, respectively, and different Notch1 domains are favored in binding to Jag1 than those that bind to the Delta-like 4 ligand. Jag1 undergoes conformational changes upon Notch binding, exhibiting catch bond behavior that prolongs interactions in the range of forces required for Notch activation. This mechanism enables cellular forces to regulate binding, discriminate among Notch ligands, and potentiate Notch signaling.</description><subject>Activation</subject><subject>Affinity</subject><subject>Animals</subject><subject>Binding</subject><subject>Bonding</subject><subject>Cell activation</subject><subject>Cell fate</subject><subject>Crystal structure</subject><subject>Crystallography, X-Ray</subject><subject>Epidermal growth factor</subject><subject>Fucose</subject><subject>Fucose - chemistry</subject><subject>Genetic Engineering</subject><subject>Glycosylation</subject><subject>Growth factors</subject><subject>Intracellular Signaling Peptides and Proteins - chemistry</subject><subject>Jagged-1 Protein - chemistry</subject><subject>Jagged-1 Protein - genetics</subject><subject>Jagged-1 Protein - ultrastructure</subject><subject>Jagged1 protein</subject><subject>Ligands</subject><subject>Membrane Proteins - chemistry</subject><subject>Notch sensitivity</subject><subject>Notch1 protein</subject><subject>Notches</subject><subject>Polysaccharides</subject><subject>Protein Binding</subject><subject>Protein Domains</subject><subject>Proteins</subject><subject>Rats</subject><subject>Receptor mechanisms</subject><subject>Receptor, Notch1 - chemistry</subject><subject>Receptor, Notch1 - genetics</subject><subject>Receptor, Notch1 - ultrastructure</subject><subject>Receptors</subject><subject>Saccharomyces cerevisiae</subject><subject>Signal Transduction</subject><subject>Signaling</subject><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkjtvFDEUhS0EIkugpgKNoKGZxM8du4mEIp6KoABqy3PnzqxXs_ZieyLy73G0S3hUuLnSPZ-v7eNDyFNGzxjj6_MMHgPgmXOj6YS5R1aMGtUaTsV9sqJUrFtNO3VCHuW8pbRqRjwkJ1xzJTutVuTLp1hg035004RDA3G3n_FHk0taoCwJG18bHlzB3LimVtg0fQxD40NTluDD1Mx-crWRMWRf_LUvN4_Jg9HNGZ8c6yn59vbN18v37dXndx8uX1-1ILU0LeOD1JxpBx0OiE7LEXinGFWi7xka2pne8NFQJoFhbwC05CMXYjDcIYA4JReHuful3-EAGEpys90nv3Ppxkbn7d9K8Bs7xWurpLo1og54cRgQc_G2elkQNhBDQCiWCSU4NxV6dTwlxe8L5mJ3PgPOswsYl2yZNsJQvabr_0A7WRfTtKIv_0G3cUmh2lUpLdZUKCMrdX6gIMWcE453j2PU3gbAHgNgjwGoO57_6ckd_-vHK_DsAGxziem3Lk29VteJn59QuGg</recordid><startdate>20170324</startdate><enddate>20170324</enddate><creator>Luca, Vincent C.</creator><creator>Kim, Byoung Choul</creator><creator>Ge, Chenghao</creator><creator>Kakuda, Shinako</creator><creator>Wu, Di</creator><creator>Roein-Peikar, Mehdi</creator><creator>Haltiwanger, Robert S.</creator><creator>Zhu, Cheng</creator><creator>Ha, Taekjip</creator><creator>Garcia, K. Christopher</creator><general>American Association for the Advancement of Science</general><general>The American Association for the Advancement of Science</general><general>AAAS</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>7QF</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QQ</scope><scope>7QR</scope><scope>7SC</scope><scope>7SE</scope><scope>7SN</scope><scope>7SP</scope><scope>7SR</scope><scope>7SS</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7TK</scope><scope>7TM</scope><scope>7U5</scope><scope>7U9</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>JG9</scope><scope>JQ2</scope><scope>K9.</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>OTOTI</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0001-9273-0278</orcidid><orcidid>https://orcid.org/0000-0002-1386-3177</orcidid><orcidid>https://orcid.org/0000-0001-8409-7046</orcidid><orcidid>https://orcid.org/0000-0001-9427-5520</orcidid><orcidid>https://orcid.org/0000-0002-1718-565X</orcidid><orcidid>https://orcid.org/0000000184097046</orcidid><orcidid>https://orcid.org/0000000194275520</orcidid><orcidid>https://orcid.org/0000000192730278</orcidid><orcidid>https://orcid.org/000000021718565X</orcidid><orcidid>https://orcid.org/0000000213863177</orcidid></search><sort><creationdate>20170324</creationdate><title>Notch-Jagged complex structure implicates a catch bond in tuning ligand sensitivity</title><author>Luca, Vincent C. ; Kim, Byoung Choul ; Ge, Chenghao ; Kakuda, Shinako ; Wu, Di ; Roein-Peikar, Mehdi ; Haltiwanger, Robert S. ; Zhu, Cheng ; Ha, Taekjip ; Garcia, K. Christopher</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4849-12d48218ac7edeea84fc2751053bb1e9079b92f9014c1eb9cc842f233d92aecc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Activation</topic><topic>Affinity</topic><topic>Animals</topic><topic>Binding</topic><topic>Bonding</topic><topic>Cell activation</topic><topic>Cell fate</topic><topic>Crystal structure</topic><topic>Crystallography, X-Ray</topic><topic>Epidermal growth factor</topic><topic>Fucose</topic><topic>Fucose - chemistry</topic><topic>Genetic Engineering</topic><topic>Glycosylation</topic><topic>Growth factors</topic><topic>Intracellular Signaling Peptides and Proteins - chemistry</topic><topic>Jagged-1 Protein - chemistry</topic><topic>Jagged-1 Protein - genetics</topic><topic>Jagged-1 Protein - ultrastructure</topic><topic>Jagged1 protein</topic><topic>Ligands</topic><topic>Membrane Proteins - chemistry</topic><topic>Notch sensitivity</topic><topic>Notch1 protein</topic><topic>Notches</topic><topic>Polysaccharides</topic><topic>Protein Binding</topic><topic>Protein Domains</topic><topic>Proteins</topic><topic>Rats</topic><topic>Receptor mechanisms</topic><topic>Receptor, Notch1 - chemistry</topic><topic>Receptor, Notch1 - genetics</topic><topic>Receptor, Notch1 - ultrastructure</topic><topic>Receptors</topic><topic>Saccharomyces cerevisiae</topic><topic>Signal Transduction</topic><topic>Signaling</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Luca, Vincent C.</creatorcontrib><creatorcontrib>Kim, Byoung Choul</creatorcontrib><creatorcontrib>Ge, Chenghao</creatorcontrib><creatorcontrib>Kakuda, Shinako</creatorcontrib><creatorcontrib>Wu, Di</creatorcontrib><creatorcontrib>Roein-Peikar, Mehdi</creatorcontrib><creatorcontrib>Haltiwanger, Robert S.</creatorcontrib><creatorcontrib>Zhu, Cheng</creatorcontrib><creatorcontrib>Ha, Taekjip</creatorcontrib><creatorcontrib>Garcia, K. Christopher</creatorcontrib><creatorcontrib>Argonne National Laboratory (ANL), Argonne, IL (United States). 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Christopher</au><aucorp>Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Notch-Jagged complex structure implicates a catch bond in tuning ligand sensitivity</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><addtitle>Science</addtitle><date>2017-03-24</date><risdate>2017</risdate><volume>355</volume><issue>6331</issue><spage>1320</spage><epage>1324</epage><pages>1320-1324</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><abstract>Notch receptor activation initiates cell fate decisions and is distinctive in its reliance on mechanical force and protein glycosylation. The 2.5-angstrom-resolution crystal structure of the extracellular interacting region of Notch1 complexed with an engineered, high-affinity variant of Jagged1 (Jag1) reveals a binding interface that extends ~120 angstroms along five consecutive domains of each protein. O-Linked fucose modifications on Notch1 epidermal growth factor–like (EGF) domains 8 and 12 engage the EGF3 and C2 domains of Jag1, respectively, and different Notch1 domains are favored in binding to Jag1 than those that bind to the Delta-like 4 ligand. Jag1 undergoes conformational changes upon Notch binding, exhibiting catch bond behavior that prolongs interactions in the range of forces required for Notch activation. This mechanism enables cellular forces to regulate binding, discriminate among Notch ligands, and potentiate Notch signaling.</abstract><cop>United States</cop><pub>American Association for the Advancement of Science</pub><pmid>28254785</pmid><doi>10.1126/science.aaf9739</doi><tpages>5</tpages><orcidid>https://orcid.org/0000-0001-9273-0278</orcidid><orcidid>https://orcid.org/0000-0002-1386-3177</orcidid><orcidid>https://orcid.org/0000-0001-8409-7046</orcidid><orcidid>https://orcid.org/0000-0001-9427-5520</orcidid><orcidid>https://orcid.org/0000-0002-1718-565X</orcidid><orcidid>https://orcid.org/0000000184097046</orcidid><orcidid>https://orcid.org/0000000194275520</orcidid><orcidid>https://orcid.org/0000000192730278</orcidid><orcidid>https://orcid.org/000000021718565X</orcidid><orcidid>https://orcid.org/0000000213863177</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Activation Affinity Animals Binding Bonding Cell activation Cell fate Crystal structure Crystallography, X-Ray Epidermal growth factor Fucose Fucose - chemistry Genetic Engineering Glycosylation Growth factors Intracellular Signaling Peptides and Proteins - chemistry Jagged-1 Protein - chemistry Jagged-1 Protein - genetics Jagged-1 Protein - ultrastructure Jagged1 protein Ligands Membrane Proteins - chemistry Notch sensitivity Notch1 protein Notches Polysaccharides Protein Binding Protein Domains Proteins Rats Receptor mechanisms Receptor, Notch1 - chemistry Receptor, Notch1 - genetics Receptor, Notch1 - ultrastructure Receptors Saccharomyces cerevisiae Signal Transduction Signaling |
| title | Notch-Jagged complex structure implicates a catch bond in tuning ligand sensitivity |
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