HN1L/JPT2: A signaling protein that connects NAADP generation to Ca 2+ microdomain formation
NAADP-evoked Ca release through type 1 ryanodine receptors (RYR1) is a major mechanism underlying the earliest signals in T cell activation, which are the formation of Ca microdomains. In our characterization of the molecular machinery underlying NAADP action, we identified an NAADP-binding protein,...
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| Veröffentlicht in: | Science signaling 2021-03, Vol.14 (675) |
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| creator | Roggenkamp, Hannes G Khansahib, Imrankhan Hernandez C, Lola C Zhang, Yunpeng Lodygin, Dmitri Krüger, Aileen Gu, Feng Möckl, Franziska Löhndorf, Anke Wolters, Valerie Woike, Daniel Rosche, Anette Bauche, Andreas Schetelig, Daniel Werner, René Schlüter, Hartmut Failla, Antonio V Meier, Chris Fliegert, Ralf Walseth, Timothy F Flügel, Alexander Diercks, Björn-Philipp Guse, Andreas H |
| description | NAADP-evoked Ca
release through type 1 ryanodine receptors (RYR1) is a major mechanism underlying the earliest signals in T cell activation, which are the formation of Ca
microdomains. In our characterization of the molecular machinery underlying NAADP action, we identified an NAADP-binding protein, called hematological and neurological expressed 1-like protein (HN1L) [also known as Jupiter microtubule-associated homolog 2 (JPT2)]. Gene deletion of
in human Jurkat and primary rat T cells resulted in decreased numbers of initial Ca
microdomains and delayed the onset and decreased the amplitude of global Ca
signaling. Photoaffinity labeling demonstrated direct binding of NAADP to recombinant HN1L/JPT2. T cell receptor/CD3-dependent coprecipitation of HN1L/JPT2 with RYRs and colocalization of these proteins suggest that HN1L/JPT2 connects NAADP formation with the activation of RYR channels within the first seconds of T cell activation. Thus, HN1L/JPT2 enables NAADP to activate Ca
release from the endoplasmic reticulum through RYR. |
| doi_str_mv | 10.1126/scisignal.abd5647 |
| format | Article |
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release through type 1 ryanodine receptors (RYR1) is a major mechanism underlying the earliest signals in T cell activation, which are the formation of Ca
microdomains. In our characterization of the molecular machinery underlying NAADP action, we identified an NAADP-binding protein, called hematological and neurological expressed 1-like protein (HN1L) [also known as Jupiter microtubule-associated homolog 2 (JPT2)]. Gene deletion of
in human Jurkat and primary rat T cells resulted in decreased numbers of initial Ca
microdomains and delayed the onset and decreased the amplitude of global Ca
signaling. Photoaffinity labeling demonstrated direct binding of NAADP to recombinant HN1L/JPT2. T cell receptor/CD3-dependent coprecipitation of HN1L/JPT2 with RYRs and colocalization of these proteins suggest that HN1L/JPT2 connects NAADP formation with the activation of RYR channels within the first seconds of T cell activation. Thus, HN1L/JPT2 enables NAADP to activate Ca
release from the endoplasmic reticulum through RYR.</description><identifier>ISSN: 1945-0877</identifier><identifier>EISSN: 1937-9145</identifier><identifier>DOI: 10.1126/scisignal.abd5647</identifier><identifier>PMID: 33758062</identifier><language>eng</language><publisher>United States</publisher><subject>Animals ; Calcium - metabolism ; Calcium Signaling ; CD3 Complex - metabolism ; Endoplasmic Reticulum - metabolism ; Humans ; Jurkat Cells ; Lymphocyte Activation ; Membrane Microdomains - metabolism ; Microtubule-Associated Proteins - genetics ; Microtubule-Associated Proteins - metabolism ; NADP - analogs & derivatives ; NADP - metabolism ; Protein Binding ; Rats ; Receptors, Antigen, T-Cell - metabolism ; Ryanodine Receptor Calcium Release Channel - metabolism ; T-Lymphocytes - metabolism</subject><ispartof>Science signaling, 2021-03, Vol.14 (675)</ispartof><rights>Copyright © 2021 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c1132-42ec4ccc20a553a3c2c78a1466c4fed9e73f14f31b4bd5cd3883a074d07580833</citedby><cites>FETCH-LOGICAL-c1132-42ec4ccc20a553a3c2c78a1466c4fed9e73f14f31b4bd5cd3883a074d07580833</cites><orcidid>0000-0002-9358-7036 ; 0000-0002-4172-2398 ; 0000-0001-8117-0287 ; 0000-0002-3972-401X ; 0000-0003-3592-6818 ; 0000-0002-7970-9834 ; 0000-0002-4374-673X ; 0000-0002-6635-1706 ; 0000-0002-2296-3305 ; 0000-0002-9565-2241 ; 0000-0002-3653-5504 ; 0000-0001-9356-5091 ; 0000-0002-5622-6549 ; 0000-0003-2558-7859 ; 0000-0001-5062-6499</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,2884,2885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33758062$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Roggenkamp, Hannes G</creatorcontrib><creatorcontrib>Khansahib, Imrankhan</creatorcontrib><creatorcontrib>Hernandez C, Lola C</creatorcontrib><creatorcontrib>Zhang, Yunpeng</creatorcontrib><creatorcontrib>Lodygin, Dmitri</creatorcontrib><creatorcontrib>Krüger, Aileen</creatorcontrib><creatorcontrib>Gu, Feng</creatorcontrib><creatorcontrib>Möckl, Franziska</creatorcontrib><creatorcontrib>Löhndorf, Anke</creatorcontrib><creatorcontrib>Wolters, Valerie</creatorcontrib><creatorcontrib>Woike, Daniel</creatorcontrib><creatorcontrib>Rosche, Anette</creatorcontrib><creatorcontrib>Bauche, Andreas</creatorcontrib><creatorcontrib>Schetelig, Daniel</creatorcontrib><creatorcontrib>Werner, René</creatorcontrib><creatorcontrib>Schlüter, Hartmut</creatorcontrib><creatorcontrib>Failla, Antonio V</creatorcontrib><creatorcontrib>Meier, Chris</creatorcontrib><creatorcontrib>Fliegert, Ralf</creatorcontrib><creatorcontrib>Walseth, Timothy F</creatorcontrib><creatorcontrib>Flügel, Alexander</creatorcontrib><creatorcontrib>Diercks, Björn-Philipp</creatorcontrib><creatorcontrib>Guse, Andreas H</creatorcontrib><title>HN1L/JPT2: A signaling protein that connects NAADP generation to Ca 2+ microdomain formation</title><title>Science signaling</title><addtitle>Sci Signal</addtitle><description>NAADP-evoked Ca
release through type 1 ryanodine receptors (RYR1) is a major mechanism underlying the earliest signals in T cell activation, which are the formation of Ca
microdomains. In our characterization of the molecular machinery underlying NAADP action, we identified an NAADP-binding protein, called hematological and neurological expressed 1-like protein (HN1L) [also known as Jupiter microtubule-associated homolog 2 (JPT2)]. Gene deletion of
in human Jurkat and primary rat T cells resulted in decreased numbers of initial Ca
microdomains and delayed the onset and decreased the amplitude of global Ca
signaling. Photoaffinity labeling demonstrated direct binding of NAADP to recombinant HN1L/JPT2. T cell receptor/CD3-dependent coprecipitation of HN1L/JPT2 with RYRs and colocalization of these proteins suggest that HN1L/JPT2 connects NAADP formation with the activation of RYR channels within the first seconds of T cell activation. Thus, HN1L/JPT2 enables NAADP to activate Ca
release from the endoplasmic reticulum through RYR.</description><subject>Animals</subject><subject>Calcium - metabolism</subject><subject>Calcium Signaling</subject><subject>CD3 Complex - metabolism</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>Humans</subject><subject>Jurkat Cells</subject><subject>Lymphocyte Activation</subject><subject>Membrane Microdomains - metabolism</subject><subject>Microtubule-Associated Proteins - genetics</subject><subject>Microtubule-Associated Proteins - metabolism</subject><subject>NADP - analogs & derivatives</subject><subject>NADP - metabolism</subject><subject>Protein Binding</subject><subject>Rats</subject><subject>Receptors, Antigen, T-Cell - metabolism</subject><subject>Ryanodine Receptor Calcium Release Channel - metabolism</subject><subject>T-Lymphocytes - metabolism</subject><issn>1945-0877</issn><issn>1937-9145</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kLFOwzAQhi0EoqXwACzIO0rrs504YYtaoKCodCgbUuRenGLUxJUdBt6elJZOd9Kv79fdR8gtsDEATyYBbbCbVm_Hel3FiVRnZAiZUFEGMj7f7zKOWKrUgFyF8MVYApxnl2QghIpTlvAh-ZgvoJi8Llf8geb00GbbDd151xnb0u5TdxRd2xrsAl3k-WxJN6Y1XnfW9bGjU035PW0sele5RvdM7XzzF1-Ti1pvg7k5zhF5f3pcTedR8fb8Ms2LCAEEjyQ3KBGRMx3HQgvkqFINMklQ1qbKjBI1yFrAWvZvYiXSVGimZMX2X6RCjAgcevsbQvCmLnfeNtr_lMDKvanyZKo8muqZuwOz-143pjoR_2rEL-roZoQ</recordid><startdate>20210323</startdate><enddate>20210323</enddate><creator>Roggenkamp, Hannes G</creator><creator>Khansahib, Imrankhan</creator><creator>Hernandez C, Lola C</creator><creator>Zhang, Yunpeng</creator><creator>Lodygin, Dmitri</creator><creator>Krüger, Aileen</creator><creator>Gu, Feng</creator><creator>Möckl, Franziska</creator><creator>Löhndorf, Anke</creator><creator>Wolters, Valerie</creator><creator>Woike, Daniel</creator><creator>Rosche, Anette</creator><creator>Bauche, Andreas</creator><creator>Schetelig, Daniel</creator><creator>Werner, René</creator><creator>Schlüter, Hartmut</creator><creator>Failla, Antonio V</creator><creator>Meier, Chris</creator><creator>Fliegert, Ralf</creator><creator>Walseth, Timothy F</creator><creator>Flügel, Alexander</creator><creator>Diercks, Björn-Philipp</creator><creator>Guse, Andreas H</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><orcidid>https://orcid.org/0000-0002-9358-7036</orcidid><orcidid>https://orcid.org/0000-0002-4172-2398</orcidid><orcidid>https://orcid.org/0000-0001-8117-0287</orcidid><orcidid>https://orcid.org/0000-0002-3972-401X</orcidid><orcidid>https://orcid.org/0000-0003-3592-6818</orcidid><orcidid>https://orcid.org/0000-0002-7970-9834</orcidid><orcidid>https://orcid.org/0000-0002-4374-673X</orcidid><orcidid>https://orcid.org/0000-0002-6635-1706</orcidid><orcidid>https://orcid.org/0000-0002-2296-3305</orcidid><orcidid>https://orcid.org/0000-0002-9565-2241</orcidid><orcidid>https://orcid.org/0000-0002-3653-5504</orcidid><orcidid>https://orcid.org/0000-0001-9356-5091</orcidid><orcidid>https://orcid.org/0000-0002-5622-6549</orcidid><orcidid>https://orcid.org/0000-0003-2558-7859</orcidid><orcidid>https://orcid.org/0000-0001-5062-6499</orcidid></search><sort><creationdate>20210323</creationdate><title>HN1L/JPT2: A signaling protein that connects NAADP generation to Ca 2+ microdomain formation</title><author>Roggenkamp, Hannes G ; 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release through type 1 ryanodine receptors (RYR1) is a major mechanism underlying the earliest signals in T cell activation, which are the formation of Ca
microdomains. In our characterization of the molecular machinery underlying NAADP action, we identified an NAADP-binding protein, called hematological and neurological expressed 1-like protein (HN1L) [also known as Jupiter microtubule-associated homolog 2 (JPT2)]. Gene deletion of
in human Jurkat and primary rat T cells resulted in decreased numbers of initial Ca
microdomains and delayed the onset and decreased the amplitude of global Ca
signaling. Photoaffinity labeling demonstrated direct binding of NAADP to recombinant HN1L/JPT2. T cell receptor/CD3-dependent coprecipitation of HN1L/JPT2 with RYRs and colocalization of these proteins suggest that HN1L/JPT2 connects NAADP formation with the activation of RYR channels within the first seconds of T cell activation. Thus, HN1L/JPT2 enables NAADP to activate Ca
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| fulltext | fulltext |
| identifier | ISSN: 1945-0877 |
| ispartof | Science signaling, 2021-03, Vol.14 (675) |
| issn | 1945-0877 1937-9145 |
| language | eng |
| recordid | cdi_crossref_primary_10_1126_scisignal_abd5647 |
| source | MEDLINE; American Association for the Advancement of Science |
| subjects | Animals Calcium - metabolism Calcium Signaling CD3 Complex - metabolism Endoplasmic Reticulum - metabolism Humans Jurkat Cells Lymphocyte Activation Membrane Microdomains - metabolism Microtubule-Associated Proteins - genetics Microtubule-Associated Proteins - metabolism NADP - analogs & derivatives NADP - metabolism Protein Binding Rats Receptors, Antigen, T-Cell - metabolism Ryanodine Receptor Calcium Release Channel - metabolism T-Lymphocytes - metabolism |
| title | HN1L/JPT2: A signaling protein that connects NAADP generation to Ca 2+ microdomain formation |
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