Distinct phosphorylation states of mammalian CaMKIIβ control the induction and maintenance of sleep
The reduced sleep duration previously observed in Camk2b knockout mice revealed a role for Ca 2+ /calmodulin-dependent protein kinase II (CaMKII)β as a sleep-promoting kinase. However, the underlying mechanism by which CaMKIIβ supports sleep regulation is largely unknown. Here, we demonstrate that a...
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| Veröffentlicht in: | PLoS biology 2022-10, Vol.20 (10), p.e3001813-e3001813 |
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| creator | Tone, Daisuke Ode, Koji L. Zhang, Qianhui Fujishima, Hiroshi Yamada, Rikuhiro G. Nagashima, Yoshiki Matsumoto, Katsuhiko Wen, Zhiqing Yoshida, Shota Y. Mitani, Tomoki T. Arisato, Yuki Ohno, Rei-ichiro Ukai-Tadenuma, Maki Yoshida Garçon, Junko Kaneko, Mari Shi, Shoi Ukai, Hideki Miyamichi, Kazunari Okada, Takashi Sumiyama, Kenta Kiyonari, Hiroshi Ueda, Hiroki R. |
| description | The reduced sleep duration previously observed in
Camk2b
knockout mice revealed a role for Ca
2+
/calmodulin-dependent protein kinase II (CaMKII)β as a sleep-promoting kinase. However, the underlying mechanism by which CaMKIIβ supports sleep regulation is largely unknown. Here, we demonstrate that activation or inhibition of CaMKIIβ can increase or decrease sleep duration in mice by almost 2-fold, supporting the role of CaMKIIβ as a core sleep regulator in mammals. Importantly, we show that this sleep regulation depends on the kinase activity of CaMKIIβ. A CaMKIIβ mutant mimicking the constitutive-active (auto)phosphorylation state promotes the transition from awake state to sleep state, while mutants mimicking subsequent multisite (auto)phosphorylation states suppress the transition from sleep state to awake state. These results suggest that the phosphorylation states of CaMKIIβ differently control sleep induction and maintenance processes, leading us to propose a “phosphorylation hypothesis of sleep” for the molecular control of sleep in mammals. |
| doi_str_mv | 10.1371/journal.pbio.3001813 |
| format | Article |
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Camk2b
knockout mice revealed a role for Ca
2+
/calmodulin-dependent protein kinase II (CaMKII)β as a sleep-promoting kinase. However, the underlying mechanism by which CaMKIIβ supports sleep regulation is largely unknown. Here, we demonstrate that activation or inhibition of CaMKIIβ can increase or decrease sleep duration in mice by almost 2-fold, supporting the role of CaMKIIβ as a core sleep regulator in mammals. Importantly, we show that this sleep regulation depends on the kinase activity of CaMKIIβ. A CaMKIIβ mutant mimicking the constitutive-active (auto)phosphorylation state promotes the transition from awake state to sleep state, while mutants mimicking subsequent multisite (auto)phosphorylation states suppress the transition from sleep state to awake state. These results suggest that the phosphorylation states of CaMKIIβ differently control sleep induction and maintenance processes, leading us to propose a “phosphorylation hypothesis of sleep” for the molecular control of sleep in mammals.</description><identifier>ISSN: 1545-7885</identifier><identifier>ISSN: 1544-9173</identifier><identifier>EISSN: 1545-7885</identifier><identifier>DOI: 10.1371/journal.pbio.3001813</identifier><identifier>PMID: 36194579</identifier><language>eng</language><publisher>San Francisco: Public Library of Science</publisher><subject>Biology and Life Sciences ; Ca2+/calmodulin-dependent protein kinase II ; Calcium ions ; Calcium-binding protein ; Calmodulin ; Efficiency ; Gene expression ; Hypotheses ; Kinases ; Maintenance ; Mammals ; Medicine and Health Sciences ; Mimicry ; Mutants ; Phosphorylation ; Physiology ; Proteins ; Research and Analysis Methods ; Sleep</subject><ispartof>PLoS biology, 2022-10, Vol.20 (10), p.e3001813-e3001813</ispartof><rights>2022 Tone et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2022 Tone et al 2022 Tone et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c503t-9af7c7fc979e65481ac2e23423e28386c8d9d82561cc496c3283834fe6e9371f3</citedby><cites>FETCH-LOGICAL-c503t-9af7c7fc979e65481ac2e23423e28386c8d9d82561cc496c3283834fe6e9371f3</cites><orcidid>0000-0001-8342-9176</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/PMC9531794/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC9531794/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2100,2926,23865,27923,27924,53790,53792,79371,79372</link.rule.ids></links><search><contributor>Kramer, Achim</contributor><creatorcontrib>Tone, Daisuke</creatorcontrib><creatorcontrib>Ode, Koji L.</creatorcontrib><creatorcontrib>Zhang, Qianhui</creatorcontrib><creatorcontrib>Fujishima, Hiroshi</creatorcontrib><creatorcontrib>Yamada, Rikuhiro G.</creatorcontrib><creatorcontrib>Nagashima, Yoshiki</creatorcontrib><creatorcontrib>Matsumoto, Katsuhiko</creatorcontrib><creatorcontrib>Wen, Zhiqing</creatorcontrib><creatorcontrib>Yoshida, Shota Y.</creatorcontrib><creatorcontrib>Mitani, Tomoki T.</creatorcontrib><creatorcontrib>Arisato, Yuki</creatorcontrib><creatorcontrib>Ohno, Rei-ichiro</creatorcontrib><creatorcontrib>Ukai-Tadenuma, Maki</creatorcontrib><creatorcontrib>Yoshida Garçon, Junko</creatorcontrib><creatorcontrib>Kaneko, Mari</creatorcontrib><creatorcontrib>Shi, Shoi</creatorcontrib><creatorcontrib>Ukai, Hideki</creatorcontrib><creatorcontrib>Miyamichi, Kazunari</creatorcontrib><creatorcontrib>Okada, Takashi</creatorcontrib><creatorcontrib>Sumiyama, Kenta</creatorcontrib><creatorcontrib>Kiyonari, Hiroshi</creatorcontrib><creatorcontrib>Ueda, Hiroki R.</creatorcontrib><title>Distinct phosphorylation states of mammalian CaMKIIβ control the induction and maintenance of sleep</title><title>PLoS biology</title><description>The reduced sleep duration previously observed in
Camk2b
knockout mice revealed a role for Ca
2+
/calmodulin-dependent protein kinase II (CaMKII)β as a sleep-promoting kinase. However, the underlying mechanism by which CaMKIIβ supports sleep regulation is largely unknown. Here, we demonstrate that activation or inhibition of CaMKIIβ can increase or decrease sleep duration in mice by almost 2-fold, supporting the role of CaMKIIβ as a core sleep regulator in mammals. Importantly, we show that this sleep regulation depends on the kinase activity of CaMKIIβ. A CaMKIIβ mutant mimicking the constitutive-active (auto)phosphorylation state promotes the transition from awake state to sleep state, while mutants mimicking subsequent multisite (auto)phosphorylation states suppress the transition from sleep state to awake state. These results suggest that the phosphorylation states of CaMKIIβ differently control sleep induction and maintenance processes, leading us to propose a “phosphorylation hypothesis of sleep” for the molecular control of sleep in mammals.</description><subject>Biology and Life Sciences</subject><subject>Ca2+/calmodulin-dependent protein kinase II</subject><subject>Calcium ions</subject><subject>Calcium-binding protein</subject><subject>Calmodulin</subject><subject>Efficiency</subject><subject>Gene expression</subject><subject>Hypotheses</subject><subject>Kinases</subject><subject>Maintenance</subject><subject>Mammals</subject><subject>Medicine and Health Sciences</subject><subject>Mimicry</subject><subject>Mutants</subject><subject>Phosphorylation</subject><subject>Physiology</subject><subject>Proteins</subject><subject>Research and Analysis Methods</subject><subject>Sleep</subject><issn>1545-7885</issn><issn>1544-9173</issn><issn>1545-7885</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>DOA</sourceid><recordid>eNptUtuKFDEQDeLirqN_INjgiy8z27l1khdBxtvgLr7oc6hJp3cypJM2SQv7W36I32T3TiuuLCGkqDrnVOVQCL3A9QZTgS-PcUwB_GbYu7ihdY0lpo_QBeaMr4WU_PE_8Tl6mvOxrglRRD5B57TBinGhLlD7zuXiginVcIh5uunWQ3ExVLlAsbmKXdVD34N3EKotXH_e7X79rEwMJUVflYOtXGhHc0eB0E5gF4oNEIydudlbOzxDZx34bJ8v7wp9-_D-6_bT-urLx9327dXa8JqWtYJOGNEZJZRtOJMYDLGEMkItkVQ2RraqlYQ32BimGkPnLGWdbayaHOnoCr086Q4-Zr0YlDURU5VyRumE2J0QbYSjHpLrId3qCE7fJWK60ZCKM97qPexrrjADjAkTtJUgWIdZI2pBWjoNvEJvlm7jvretsZMl4O-J3q8Ed9A38YdWnGKh2CTwehFI8ftoc9G9y8Z6D8HGcZ6bYNJMZ-716j_ow79jJ5RJMedku7_D4FrPS_OHpeel0cvS0N_IHLaP</recordid><startdate>20221001</startdate><enddate>20221001</enddate><creator>Tone, 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phosphorylation states of mammalian CaMKIIβ control the induction and maintenance of sleep</title><author>Tone, Daisuke ; Ode, Koji L. ; Zhang, Qianhui ; Fujishima, Hiroshi ; Yamada, Rikuhiro G. ; Nagashima, Yoshiki ; Matsumoto, Katsuhiko ; Wen, Zhiqing ; Yoshida, Shota Y. ; Mitani, Tomoki T. ; Arisato, Yuki ; Ohno, Rei-ichiro ; Ukai-Tadenuma, Maki ; Yoshida Garçon, Junko ; Kaneko, Mari ; Shi, Shoi ; Ukai, Hideki ; Miyamichi, Kazunari ; Okada, Takashi ; Sumiyama, Kenta ; Kiyonari, Hiroshi ; Ueda, Hiroki R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c503t-9af7c7fc979e65481ac2e23423e28386c8d9d82561cc496c3283834fe6e9371f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Biology and Life Sciences</topic><topic>Ca2+/calmodulin-dependent protein kinase II</topic><topic>Calcium ions</topic><topic>Calcium-binding 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Katsuhiko</au><au>Wen, Zhiqing</au><au>Yoshida, Shota Y.</au><au>Mitani, Tomoki T.</au><au>Arisato, Yuki</au><au>Ohno, Rei-ichiro</au><au>Ukai-Tadenuma, Maki</au><au>Yoshida Garçon, Junko</au><au>Kaneko, Mari</au><au>Shi, Shoi</au><au>Ukai, Hideki</au><au>Miyamichi, Kazunari</au><au>Okada, Takashi</au><au>Sumiyama, Kenta</au><au>Kiyonari, Hiroshi</au><au>Ueda, Hiroki R.</au><au>Kramer, Achim</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Distinct phosphorylation states of mammalian CaMKIIβ control the induction and maintenance of sleep</atitle><jtitle>PLoS biology</jtitle><date>2022-10-01</date><risdate>2022</risdate><volume>20</volume><issue>10</issue><spage>e3001813</spage><epage>e3001813</epage><pages>e3001813-e3001813</pages><issn>1545-7885</issn><issn>1544-9173</issn><eissn>1545-7885</eissn><abstract>The reduced sleep duration previously observed in
Camk2b
knockout mice revealed a role for Ca
2+
/calmodulin-dependent protein kinase II (CaMKII)β as a sleep-promoting kinase. However, the underlying mechanism by which CaMKIIβ supports sleep regulation is largely unknown. Here, we demonstrate that activation or inhibition of CaMKIIβ can increase or decrease sleep duration in mice by almost 2-fold, supporting the role of CaMKIIβ as a core sleep regulator in mammals. Importantly, we show that this sleep regulation depends on the kinase activity of CaMKIIβ. A CaMKIIβ mutant mimicking the constitutive-active (auto)phosphorylation state promotes the transition from awake state to sleep state, while mutants mimicking subsequent multisite (auto)phosphorylation states suppress the transition from sleep state to awake state. These results suggest that the phosphorylation states of CaMKIIβ differently control sleep induction and maintenance processes, leading us to propose a “phosphorylation hypothesis of sleep” for the molecular control of sleep in mammals.</abstract><cop>San Francisco</cop><pub>Public Library of Science</pub><pmid>36194579</pmid><doi>10.1371/journal.pbio.3001813</doi><orcidid>https://orcid.org/0000-0001-8342-9176</orcidid><oa>free_for_read</oa></addata></record> |
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| source | DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Public Library of Science (PLoS); PubMed Central |
| subjects | Biology and Life Sciences Ca2+/calmodulin-dependent protein kinase II Calcium ions Calcium-binding protein Calmodulin Efficiency Gene expression Hypotheses Kinases Maintenance Mammals Medicine and Health Sciences Mimicry Mutants Phosphorylation Physiology Proteins Research and Analysis Methods Sleep |
| title | Distinct phosphorylation states of mammalian CaMKIIβ control the induction and maintenance of sleep |
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