Regulation of RIP1 kinase signalling at the crossroads of inflammation and cell death
Key Points Receptor-interacting protein 1 (RIP1) contains an amino-terminal kinase domain, a carboxy-terminal death domain and an intermediate domain with a receptor-interacting protein homotypic interaction motif (RHIM). RIP1 has emerged as a key upstream regulator that controls inflammatory signal...
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| Veröffentlicht in: | Nature reviews. Molecular cell biology 2013-11, Vol.14 (11), p.727-736 |
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| container_title | Nature reviews. Molecular cell biology |
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| creator | Ofengeim, Dimitry Yuan, Junying |
| description | Key Points
Receptor-interacting protein 1 (RIP1) contains an amino-terminal kinase domain, a carboxy-terminal death domain and an intermediate domain with a receptor-interacting protein homotypic interaction motif (RHIM).
RIP1 has emerged as a key upstream regulator that controls inflammatory signalling as well as the activation of multiple cell death pathways, including apoptosis and necroptosis.
The ability of RIP1 to modulate these key cellular events is tightly controlled by ubiquitylation, deubiquitylation and the interaction of RIP1 with a class of ubiquitin receptors.
Ubiquitylation of RIP1 might provide a unique 'ubiquitin code' that determines whether a cell activates cell survival through the nuclear factor-κB (NF-κB)-dependent or -independent pathways or induces cell death through necroptosis or apoptosis.
Targeting RIP1 kinase might provide novel therapeutics for the treatment of both acute and chronic human diseases.
Receptor-interacting protein (RIP1) is a key upstream regulator of signalling pathways that lead to either inflammation or cell death by apoptosis or necroptosis. Recent evidence indicates that the decision between these pathways is regulated by the ubiquitylation and deubiquitylation of RIP1, which determines its interaction with various ubiquitin-binding proteins.
Receptor-interacting protein 1 (RIP1) kinase has emerged as a key upstream regulator that controls inflammatory signalling as well as the activation of multiple cell death pathways, including apoptosis and necroptosis. The ability of RIP1 to modulate these key cellular events is tightly controlled by ubiquitylation, deubiquitylation and the interaction of RIP1 with a class of ubiquitin receptors. The modification of RIP1 may thus provide a unique 'ubiquitin code' that determines whether a cell activates nuclear factor-κB (NF-κB) to promote inflammatory signalling or induces cell death by apoptosis or necroptosis. Targeting RIP1 might be a novel therapeutic strategy for the treatment of both acute and chronic human diseases. |
| doi_str_mv | 10.1038/nrm3683 |
| format | Article |
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Receptor-interacting protein 1 (RIP1) contains an amino-terminal kinase domain, a carboxy-terminal death domain and an intermediate domain with a receptor-interacting protein homotypic interaction motif (RHIM).
RIP1 has emerged as a key upstream regulator that controls inflammatory signalling as well as the activation of multiple cell death pathways, including apoptosis and necroptosis.
The ability of RIP1 to modulate these key cellular events is tightly controlled by ubiquitylation, deubiquitylation and the interaction of RIP1 with a class of ubiquitin receptors.
Ubiquitylation of RIP1 might provide a unique 'ubiquitin code' that determines whether a cell activates cell survival through the nuclear factor-κB (NF-κB)-dependent or -independent pathways or induces cell death through necroptosis or apoptosis.
Targeting RIP1 kinase might provide novel therapeutics for the treatment of both acute and chronic human diseases.
Receptor-interacting protein (RIP1) is a key upstream regulator of signalling pathways that lead to either inflammation or cell death by apoptosis or necroptosis. Recent evidence indicates that the decision between these pathways is regulated by the ubiquitylation and deubiquitylation of RIP1, which determines its interaction with various ubiquitin-binding proteins.
Receptor-interacting protein 1 (RIP1) kinase has emerged as a key upstream regulator that controls inflammatory signalling as well as the activation of multiple cell death pathways, including apoptosis and necroptosis. The ability of RIP1 to modulate these key cellular events is tightly controlled by ubiquitylation, deubiquitylation and the interaction of RIP1 with a class of ubiquitin receptors. The modification of RIP1 may thus provide a unique 'ubiquitin code' that determines whether a cell activates nuclear factor-κB (NF-κB) to promote inflammatory signalling or induces cell death by apoptosis or necroptosis. Targeting RIP1 might be a novel therapeutic strategy for the treatment of both acute and chronic human diseases.</description><identifier>ISSN: 1471-0072</identifier><identifier>EISSN: 1471-0080</identifier><identifier>DOI: 10.1038/nrm3683</identifier><identifier>PMID: 24129419</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/80/458/582 ; 631/80/82/23 ; 631/80/82/2344 ; 631/80/86/2366 ; Animals ; Apoptosis ; Biochemistry ; Cancer Research ; Cell Biology ; Cell death ; Cell Death - physiology ; Cellular signal transduction ; Developmental Biology ; Humans ; Inflammation - genetics ; Inflammation - metabolism ; Life Sciences ; Models, Biological ; Mortality ; NF-kappa B - metabolism ; Observations ; Physiological aspects ; Protein kinases ; Receptor-Interacting Protein Serine-Threonine Kinases - genetics ; Receptor-Interacting Protein Serine-Threonine Kinases - metabolism ; review-article ; Stem Cells ; Testing ; Upstream</subject><ispartof>Nature reviews. Molecular cell biology, 2013-11, Vol.14 (11), p.727-736</ispartof><rights>Springer Nature Limited 2013</rights><rights>COPYRIGHT 2013 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Nov 2013</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c443t-321557b88ad7adb715d5ab5733447a64346dfa02a83a2aca8a631fa89bf128f33</citedby><cites>FETCH-LOGICAL-c443t-321557b88ad7adb715d5ab5733447a64346dfa02a83a2aca8a631fa89bf128f33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/nrm3683$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/nrm3683$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24129419$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ofengeim, Dimitry</creatorcontrib><creatorcontrib>Yuan, Junying</creatorcontrib><title>Regulation of RIP1 kinase signalling at the crossroads of inflammation and cell death</title><title>Nature reviews. Molecular cell biology</title><addtitle>Nat Rev Mol Cell Biol</addtitle><addtitle>Nat Rev Mol Cell Biol</addtitle><description>Key Points
Receptor-interacting protein 1 (RIP1) contains an amino-terminal kinase domain, a carboxy-terminal death domain and an intermediate domain with a receptor-interacting protein homotypic interaction motif (RHIM).
RIP1 has emerged as a key upstream regulator that controls inflammatory signalling as well as the activation of multiple cell death pathways, including apoptosis and necroptosis.
The ability of RIP1 to modulate these key cellular events is tightly controlled by ubiquitylation, deubiquitylation and the interaction of RIP1 with a class of ubiquitin receptors.
Ubiquitylation of RIP1 might provide a unique 'ubiquitin code' that determines whether a cell activates cell survival through the nuclear factor-κB (NF-κB)-dependent or -independent pathways or induces cell death through necroptosis or apoptosis.
Targeting RIP1 kinase might provide novel therapeutics for the treatment of both acute and chronic human diseases.
Receptor-interacting protein (RIP1) is a key upstream regulator of signalling pathways that lead to either inflammation or cell death by apoptosis or necroptosis. Recent evidence indicates that the decision between these pathways is regulated by the ubiquitylation and deubiquitylation of RIP1, which determines its interaction with various ubiquitin-binding proteins.
Receptor-interacting protein 1 (RIP1) kinase has emerged as a key upstream regulator that controls inflammatory signalling as well as the activation of multiple cell death pathways, including apoptosis and necroptosis. The ability of RIP1 to modulate these key cellular events is tightly controlled by ubiquitylation, deubiquitylation and the interaction of RIP1 with a class of ubiquitin receptors. The modification of RIP1 may thus provide a unique 'ubiquitin code' that determines whether a cell activates nuclear factor-κB (NF-κB) to promote inflammatory signalling or induces cell death by apoptosis or necroptosis. Targeting RIP1 might be a novel therapeutic strategy for the treatment of both acute and chronic human diseases.</description><subject>631/80/458/582</subject><subject>631/80/82/23</subject><subject>631/80/82/2344</subject><subject>631/80/86/2366</subject><subject>Animals</subject><subject>Apoptosis</subject><subject>Biochemistry</subject><subject>Cancer Research</subject><subject>Cell Biology</subject><subject>Cell death</subject><subject>Cell Death - physiology</subject><subject>Cellular signal transduction</subject><subject>Developmental Biology</subject><subject>Humans</subject><subject>Inflammation - genetics</subject><subject>Inflammation - metabolism</subject><subject>Life Sciences</subject><subject>Models, Biological</subject><subject>Mortality</subject><subject>NF-kappa B - metabolism</subject><subject>Observations</subject><subject>Physiological aspects</subject><subject>Protein kinases</subject><subject>Receptor-Interacting Protein Serine-Threonine Kinases - genetics</subject><subject>Receptor-Interacting Protein Serine-Threonine Kinases - metabolism</subject><subject>review-article</subject><subject>Stem Cells</subject><subject>Testing</subject><subject>Upstream</subject><issn>1471-0072</issn><issn>1471-0080</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNptkV9rHCEUxSW05F9DvkER-tDkYVMddcZ9DKFpFwIt2-ZZ7ow6MZ3RVB1ov30cdptkQ_FB8f7O5Z57EDql5IISJj_5OLJasj10SHlDF4RI8ubp3VQH6Cile0JoTRuxjw4qTqslp8tDdLs2_TRAdsHjYPF69Z3iX85DMji53sMwON9jyDjfGdzFkFIMoNPMOm8HGMeNFrzGnRkGrA3ku3forYUhmZPtfYxurz__vPq6uPn2ZXV1ebPoOGd5wSoqRNNKCboB3TZUaAGtaBjjvIGaM15rC6QCyaCCDiTUjFqQy9bSSlrGjtHZpu9DDL8nk7IaXZrHAG_ClBTlnEtRc0oL-uEVeh-mWAzOlJB1QQR5pnoYjCoOQ47QzU3V5VxnddlboS7-Q5Wjzei64I115X9HcL4jKEw2f3IPU0pq9WO9y37csJttG6seohsh_lWUqDlstQ27kO-3lqZ2NPqJ-5fu83pSKfnexBeeX_V6BEKsrek</recordid><startdate>20131101</startdate><enddate>20131101</enddate><creator>Ofengeim, Dimitry</creator><creator>Yuan, Junying</creator><general>Nature Publishing Group UK</general><general>Nature Publishing 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>ISR</scope><scope>3V.</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7RV</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB0</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>NAPCQ</scope><scope>P64</scope><scope>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20131101</creationdate><title>Regulation of RIP1 kinase signalling at the crossroads of inflammation and cell death</title><author>Ofengeim, Dimitry ; Yuan, Junying</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c443t-321557b88ad7adb715d5ab5733447a64346dfa02a83a2aca8a631fa89bf128f33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>631/80/458/582</topic><topic>631/80/82/23</topic><topic>631/80/82/2344</topic><topic>631/80/86/2366</topic><topic>Animals</topic><topic>Apoptosis</topic><topic>Biochemistry</topic><topic>Cancer Research</topic><topic>Cell Biology</topic><topic>Cell death</topic><topic>Cell Death - physiology</topic><topic>Cellular signal transduction</topic><topic>Developmental Biology</topic><topic>Humans</topic><topic>Inflammation - genetics</topic><topic>Inflammation - metabolism</topic><topic>Life Sciences</topic><topic>Models, Biological</topic><topic>Mortality</topic><topic>NF-kappa B - metabolism</topic><topic>Observations</topic><topic>Physiological aspects</topic><topic>Protein kinases</topic><topic>Receptor-Interacting Protein Serine-Threonine Kinases - genetics</topic><topic>Receptor-Interacting Protein Serine-Threonine Kinases - metabolism</topic><topic>review-article</topic><topic>Stem Cells</topic><topic>Testing</topic><topic>Upstream</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ofengeim, Dimitry</creatorcontrib><creatorcontrib>Yuan, Junying</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Proquest Nursing & Allied Health Source</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Earth, Atmospheric & Aquatic Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Nursing & Allied Health Premium</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Earth, Atmospheric & Aquatic Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Nature reviews. Molecular cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ofengeim, Dimitry</au><au>Yuan, Junying</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Regulation of RIP1 kinase signalling at the crossroads of inflammation and cell death</atitle><jtitle>Nature reviews. Molecular cell biology</jtitle><stitle>Nat Rev Mol Cell Biol</stitle><addtitle>Nat Rev Mol Cell Biol</addtitle><date>2013-11-01</date><risdate>2013</risdate><volume>14</volume><issue>11</issue><spage>727</spage><epage>736</epage><pages>727-736</pages><issn>1471-0072</issn><eissn>1471-0080</eissn><abstract>Key Points
Receptor-interacting protein 1 (RIP1) contains an amino-terminal kinase domain, a carboxy-terminal death domain and an intermediate domain with a receptor-interacting protein homotypic interaction motif (RHIM).
RIP1 has emerged as a key upstream regulator that controls inflammatory signalling as well as the activation of multiple cell death pathways, including apoptosis and necroptosis.
The ability of RIP1 to modulate these key cellular events is tightly controlled by ubiquitylation, deubiquitylation and the interaction of RIP1 with a class of ubiquitin receptors.
Ubiquitylation of RIP1 might provide a unique 'ubiquitin code' that determines whether a cell activates cell survival through the nuclear factor-κB (NF-κB)-dependent or -independent pathways or induces cell death through necroptosis or apoptosis.
Targeting RIP1 kinase might provide novel therapeutics for the treatment of both acute and chronic human diseases.
Receptor-interacting protein (RIP1) is a key upstream regulator of signalling pathways that lead to either inflammation or cell death by apoptosis or necroptosis. Recent evidence indicates that the decision between these pathways is regulated by the ubiquitylation and deubiquitylation of RIP1, which determines its interaction with various ubiquitin-binding proteins.
Receptor-interacting protein 1 (RIP1) kinase has emerged as a key upstream regulator that controls inflammatory signalling as well as the activation of multiple cell death pathways, including apoptosis and necroptosis. The ability of RIP1 to modulate these key cellular events is tightly controlled by ubiquitylation, deubiquitylation and the interaction of RIP1 with a class of ubiquitin receptors. The modification of RIP1 may thus provide a unique 'ubiquitin code' that determines whether a cell activates nuclear factor-κB (NF-κB) to promote inflammatory signalling or induces cell death by apoptosis or necroptosis. Targeting RIP1 might be a novel therapeutic strategy for the treatment of both acute and chronic human diseases.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>24129419</pmid><doi>10.1038/nrm3683</doi><tpages>10</tpages></addata></record> |
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| subjects | 631/80/458/582 631/80/82/23 631/80/82/2344 631/80/86/2366 Animals Apoptosis Biochemistry Cancer Research Cell Biology Cell death Cell Death - physiology Cellular signal transduction Developmental Biology Humans Inflammation - genetics Inflammation - metabolism Life Sciences Models, Biological Mortality NF-kappa B - metabolism Observations Physiological aspects Protein kinases Receptor-Interacting Protein Serine-Threonine Kinases - genetics Receptor-Interacting Protein Serine-Threonine Kinases - metabolism review-article Stem Cells Testing Upstream |
| title | Regulation of RIP1 kinase signalling at the crossroads of inflammation and cell death |
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