Loading…

Identification of novel proteins involved in P2X7-mediated signaling cascades

High concentration of extracellular ATP acts as a danger signal that is sensed by the P2X7 receptor (P2X7R). This ATP-gated ion channel has been shown to induce multiple metabotropic events such as changes in plasma membrane composition and morphology, ectodomain shedding, activation of lipases, kin...

Full description

Saved in:
Bibliographic Details
Published in:Purinergic signalling 2022-12, Vol.18 (4), p.495-498
Main Author: Sassenbach, Lukas
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c474t-8988dd8fac7cb8a76d3e597ba3e60a316950ec92bcb236b184f3d011193dc0b93
cites cdi_FETCH-LOGICAL-c474t-8988dd8fac7cb8a76d3e597ba3e60a316950ec92bcb236b184f3d011193dc0b93
container_end_page 498
container_issue 4
container_start_page 495
container_title Purinergic signalling
container_volume 18
creator Sassenbach, Lukas
description High concentration of extracellular ATP acts as a danger signal that is sensed by the P2X7 receptor (P2X7R). This ATP-gated ion channel has been shown to induce multiple metabotropic events such as changes in plasma membrane composition and morphology, ectodomain shedding, activation of lipases, kinases, and transcription factors as well as cytokine release. The specific signaling pathways and molecular mechanisms remain largely obscure. Using an unbiased genome-scale CRISPR/Cas9 screening approach in a murine T cell line, Ryoden et al. (2022, 2020) identified three proteins involved in P2X7 regulation and signaling: Essential for Reactive Oxygen Species (EROS) is essential for P2X7 folding and maturation, and Xk and Vsp13a are required for P2X7-mediated phosphatidyl serine exposure and cell lysis. They further provide evidence for an interaction of Xk and Vsp13a at the plasma membrane and confirm the role of Xk in ATP-induced cytolysis in primary CD25 + CD4 + T cells from Xk −/− mice.
doi_str_mv 10.1007/s11302-022-09893-z
format article
fullrecord <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_9832184</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2763451820</sourcerecordid><originalsourceid>FETCH-LOGICAL-c474t-8988dd8fac7cb8a76d3e597ba3e60a316950ec92bcb236b184f3d011193dc0b93</originalsourceid><addsrcrecordid>eNp9kUtLAzEQx4Motj6-gAdZ8Lyaxz6SiyDFR6GiBwVvIZtk15RtUpPtgv30RrdWvXgIGTL_-c1M_gCcIHiOICwvAkIE4hTieBhlJF3vgDHKS5KyPCt2tzGhI3AQwhzCPMOE7YMRyVkBM5yNwf1UaduZ2kjRGWcTVyfW9bpNlt512tiQGNu7ttcqBskjfinThVZGdPEhmMaK1tgmkSJIoXQ4Anu1aIM-3tyH4Pnm-mlyl84ebqeTq1kqszLrUsooVYrWQpayoqIsFNE5KytBdAEFQQXLoZYMV7LCpKgQzWqiIEKIESVhxcghuBy4y1UVx5FxBS9avvRmIfw7d8LwvxlrXnnjes4owREXAWcbgHdvKx06PncrH7cJHJcFyXJEMYwqPKikdyF4XW87IMg_LeCDBTxawL8s4OtYdPp7tm3J959HARkEIaZso_1P73-wH302k54</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2763451820</pqid></control><display><type>article</type><title>Identification of novel proteins involved in P2X7-mediated signaling cascades</title><source>Open Access: PubMed Central</source><source>Springer Nature</source><creator>Sassenbach, Lukas</creator><creatorcontrib>Sassenbach, Lukas</creatorcontrib><description>High concentration of extracellular ATP acts as a danger signal that is sensed by the P2X7 receptor (P2X7R). This ATP-gated ion channel has been shown to induce multiple metabotropic events such as changes in plasma membrane composition and morphology, ectodomain shedding, activation of lipases, kinases, and transcription factors as well as cytokine release. The specific signaling pathways and molecular mechanisms remain largely obscure. Using an unbiased genome-scale CRISPR/Cas9 screening approach in a murine T cell line, Ryoden et al. (2022, 2020) identified three proteins involved in P2X7 regulation and signaling: Essential for Reactive Oxygen Species (EROS) is essential for P2X7 folding and maturation, and Xk and Vsp13a are required for P2X7-mediated phosphatidyl serine exposure and cell lysis. They further provide evidence for an interaction of Xk and Vsp13a at the plasma membrane and confirm the role of Xk in ATP-induced cytolysis in primary CD25 + CD4 + T cells from Xk −/− mice.</description><identifier>ISSN: 1573-9538</identifier><identifier>EISSN: 1573-9546</identifier><identifier>DOI: 10.1007/s11302-022-09893-z</identifier><identifier>PMID: 35960424</identifier><language>eng</language><publisher>Dordrecht: Springer Netherlands</publisher><subject>Adenosine Triphosphate - pharmacology ; Animals ; Biomedical and Life Sciences ; Biomedicine ; Cancer Research ; CD25 antigen ; CD4 antigen ; CRISPR ; Cytolysis ; Genomes ; Human Physiology ; Journal Club ; Lymphocyte Activation ; Lymphocytes T ; Lysis ; Membrane composition ; Metabotropic receptors ; Mice ; Molecular modelling ; Neurosciences ; Pharmacology/Toxicology ; Reactive oxygen species ; Receptors, Purinergic P2X7 ; Signal Transduction ; T-Lymphocytes ; Transcription factors</subject><ispartof>Purinergic signalling, 2022-12, Vol.18 (4), p.495-498</ispartof><rights>The Author(s) 2022</rights><rights>2022. The Author(s).</rights><rights>The Author(s) 2022. This work is published under http://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><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c474t-8988dd8fac7cb8a76d3e597ba3e60a316950ec92bcb236b184f3d011193dc0b93</citedby><cites>FETCH-LOGICAL-c474t-8988dd8fac7cb8a76d3e597ba3e60a316950ec92bcb236b184f3d011193dc0b93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC9832184/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC9832184/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/35960424$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sassenbach, Lukas</creatorcontrib><title>Identification of novel proteins involved in P2X7-mediated signaling cascades</title><title>Purinergic signalling</title><addtitle>Purinergic Signalling</addtitle><addtitle>Purinergic Signal</addtitle><description>High concentration of extracellular ATP acts as a danger signal that is sensed by the P2X7 receptor (P2X7R). This ATP-gated ion channel has been shown to induce multiple metabotropic events such as changes in plasma membrane composition and morphology, ectodomain shedding, activation of lipases, kinases, and transcription factors as well as cytokine release. The specific signaling pathways and molecular mechanisms remain largely obscure. Using an unbiased genome-scale CRISPR/Cas9 screening approach in a murine T cell line, Ryoden et al. (2022, 2020) identified three proteins involved in P2X7 regulation and signaling: Essential for Reactive Oxygen Species (EROS) is essential for P2X7 folding and maturation, and Xk and Vsp13a are required for P2X7-mediated phosphatidyl serine exposure and cell lysis. They further provide evidence for an interaction of Xk and Vsp13a at the plasma membrane and confirm the role of Xk in ATP-induced cytolysis in primary CD25 + CD4 + T cells from Xk −/− mice.</description><subject>Adenosine Triphosphate - pharmacology</subject><subject>Animals</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Cancer Research</subject><subject>CD25 antigen</subject><subject>CD4 antigen</subject><subject>CRISPR</subject><subject>Cytolysis</subject><subject>Genomes</subject><subject>Human Physiology</subject><subject>Journal Club</subject><subject>Lymphocyte Activation</subject><subject>Lymphocytes T</subject><subject>Lysis</subject><subject>Membrane composition</subject><subject>Metabotropic receptors</subject><subject>Mice</subject><subject>Molecular modelling</subject><subject>Neurosciences</subject><subject>Pharmacology/Toxicology</subject><subject>Reactive oxygen species</subject><subject>Receptors, Purinergic P2X7</subject><subject>Signal Transduction</subject><subject>T-Lymphocytes</subject><subject>Transcription factors</subject><issn>1573-9538</issn><issn>1573-9546</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><recordid>eNp9kUtLAzEQx4Motj6-gAdZ8Lyaxz6SiyDFR6GiBwVvIZtk15RtUpPtgv30RrdWvXgIGTL_-c1M_gCcIHiOICwvAkIE4hTieBhlJF3vgDHKS5KyPCt2tzGhI3AQwhzCPMOE7YMRyVkBM5yNwf1UaduZ2kjRGWcTVyfW9bpNlt512tiQGNu7ttcqBskjfinThVZGdPEhmMaK1tgmkSJIoXQ4Anu1aIM-3tyH4Pnm-mlyl84ebqeTq1kqszLrUsooVYrWQpayoqIsFNE5KytBdAEFQQXLoZYMV7LCpKgQzWqiIEKIESVhxcghuBy4y1UVx5FxBS9avvRmIfw7d8LwvxlrXnnjes4owREXAWcbgHdvKx06PncrH7cJHJcFyXJEMYwqPKikdyF4XW87IMg_LeCDBTxawL8s4OtYdPp7tm3J959HARkEIaZso_1P73-wH302k54</recordid><startdate>20221201</startdate><enddate>20221201</enddate><creator>Sassenbach, Lukas</creator><general>Springer Netherlands</general><general>Springer Nature B.V</general><scope>C6C</scope><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>5PM</scope></search><sort><creationdate>20221201</creationdate><title>Identification of novel proteins involved in P2X7-mediated signaling cascades</title><author>Sassenbach, Lukas</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c474t-8988dd8fac7cb8a76d3e597ba3e60a316950ec92bcb236b184f3d011193dc0b93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Adenosine Triphosphate - pharmacology</topic><topic>Animals</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Cancer Research</topic><topic>CD25 antigen</topic><topic>CD4 antigen</topic><topic>CRISPR</topic><topic>Cytolysis</topic><topic>Genomes</topic><topic>Human Physiology</topic><topic>Journal Club</topic><topic>Lymphocyte Activation</topic><topic>Lymphocytes T</topic><topic>Lysis</topic><topic>Membrane composition</topic><topic>Metabotropic receptors</topic><topic>Mice</topic><topic>Molecular modelling</topic><topic>Neurosciences</topic><topic>Pharmacology/Toxicology</topic><topic>Reactive oxygen species</topic><topic>Receptors, Purinergic P2X7</topic><topic>Signal Transduction</topic><topic>T-Lymphocytes</topic><topic>Transcription factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sassenbach, Lukas</creatorcontrib><collection>SpringerOpen</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Purinergic signalling</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sassenbach, Lukas</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of novel proteins involved in P2X7-mediated signaling cascades</atitle><jtitle>Purinergic signalling</jtitle><stitle>Purinergic Signalling</stitle><addtitle>Purinergic Signal</addtitle><date>2022-12-01</date><risdate>2022</risdate><volume>18</volume><issue>4</issue><spage>495</spage><epage>498</epage><pages>495-498</pages><issn>1573-9538</issn><eissn>1573-9546</eissn><abstract>High concentration of extracellular ATP acts as a danger signal that is sensed by the P2X7 receptor (P2X7R). This ATP-gated ion channel has been shown to induce multiple metabotropic events such as changes in plasma membrane composition and morphology, ectodomain shedding, activation of lipases, kinases, and transcription factors as well as cytokine release. The specific signaling pathways and molecular mechanisms remain largely obscure. Using an unbiased genome-scale CRISPR/Cas9 screening approach in a murine T cell line, Ryoden et al. (2022, 2020) identified three proteins involved in P2X7 regulation and signaling: Essential for Reactive Oxygen Species (EROS) is essential for P2X7 folding and maturation, and Xk and Vsp13a are required for P2X7-mediated phosphatidyl serine exposure and cell lysis. They further provide evidence for an interaction of Xk and Vsp13a at the plasma membrane and confirm the role of Xk in ATP-induced cytolysis in primary CD25 + CD4 + T cells from Xk −/− mice.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><pmid>35960424</pmid><doi>10.1007/s11302-022-09893-z</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 1573-9538
ispartof Purinergic signalling, 2022-12, Vol.18 (4), p.495-498
issn 1573-9538
1573-9546
language eng
recordid cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_9832184
source Open Access: PubMed Central; Springer Nature
subjects Adenosine Triphosphate - pharmacology
Animals
Biomedical and Life Sciences
Biomedicine
Cancer Research
CD25 antigen
CD4 antigen
CRISPR
Cytolysis
Genomes
Human Physiology
Journal Club
Lymphocyte Activation
Lymphocytes T
Lysis
Membrane composition
Metabotropic receptors
Mice
Molecular modelling
Neurosciences
Pharmacology/Toxicology
Reactive oxygen species
Receptors, Purinergic P2X7
Signal Transduction
T-Lymphocytes
Transcription factors
title Identification of novel proteins involved in P2X7-mediated signaling cascades
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-28T04%3A58%3A31IST&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=Identification%20of%20novel%20proteins%20involved%20in%20P2X7-mediated%20signaling%20cascades&rft.jtitle=Purinergic%20signalling&rft.au=Sassenbach,%20Lukas&rft.date=2022-12-01&rft.volume=18&rft.issue=4&rft.spage=495&rft.epage=498&rft.pages=495-498&rft.issn=1573-9538&rft.eissn=1573-9546&rft_id=info:doi/10.1007/s11302-022-09893-z&rft_dat=%3Cproquest_pubme%3E2763451820%3C/proquest_pubme%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c474t-8988dd8fac7cb8a76d3e597ba3e60a316950ec92bcb236b184f3d011193dc0b93%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=2763451820&rft_id=info:pmid/35960424&rfr_iscdi=true