A Critical Role for γCaMKII in Decoding NMDA Signaling to Regulate AMPA Receptors in Putative Inhibitory Interneurons
CaMKII is essential for long-term potentiation (LTP), a process in which synaptic strength is increased following the acquisition of information. Among the four CaMKII isoforms, γCaMKII is the one that mediates the LTP of excitatory synapses onto inhibitory interneurons (LTP E→I ). However, the mole...
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| Veröffentlicht in: | Neuroscience bulletin 2022-08, Vol.38 (8), p.916-926 |
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| creator | He, Xingzhi Wang, Yang Zhou, Guangjun Yang, Jing Li, Jiarui Li, Tao Hu, Hailan Ma, Huan |
| description | CaMKII is essential for long-term potentiation (LTP), a process in which synaptic strength is increased following the acquisition of information. Among the four CaMKII isoforms, γCaMKII is the one that mediates the LTP of excitatory synapses onto inhibitory interneurons (LTP
E→I
). However, the molecular mechanism underlying how γCaMKII mediates LTP
E→I
remains unclear. Here, we show that γCaMKII is highly enriched in cultured hippocampal inhibitory interneurons and opts to be activated by higher stimulating frequencies in the 10–30 Hz range. Following stimulation, γCaMKII is translocated to the synapse and becomes co-localized with the postsynaptic protein PSD-95. Knocking down γCaMKII prevents the chemical LTP-induced phosphorylation and trafficking of AMPA receptors (AMPARs) in putative inhibitory interneurons, which are restored by overexpression of γCaMKII but not its kinase-dead form. Taken together, these data suggest that γCaMKII decodes NMDAR-mediated signaling and in turn regulates AMPARs for expressing LTP in inhibitory interneurons. |
| doi_str_mv | 10.1007/s12264-022-00840-x |
| format | Article |
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E→I
). However, the molecular mechanism underlying how γCaMKII mediates LTP
E→I
remains unclear. Here, we show that γCaMKII is highly enriched in cultured hippocampal inhibitory interneurons and opts to be activated by higher stimulating frequencies in the 10–30 Hz range. Following stimulation, γCaMKII is translocated to the synapse and becomes co-localized with the postsynaptic protein PSD-95. Knocking down γCaMKII prevents the chemical LTP-induced phosphorylation and trafficking of AMPA receptors (AMPARs) in putative inhibitory interneurons, which are restored by overexpression of γCaMKII but not its kinase-dead form. Taken together, these data suggest that γCaMKII decodes NMDAR-mediated signaling and in turn regulates AMPARs for expressing LTP in inhibitory interneurons.</description><identifier>ISSN: 1673-7067</identifier><identifier>EISSN: 1995-8218</identifier><identifier>DOI: 10.1007/s12264-022-00840-x</identifier><identifier>PMID: 35290589</identifier><language>eng</language><publisher>Singapore: Springer Nature Singapore</publisher><subject>Anatomy ; Anesthesiology ; Biomedical and Life Sciences ; Biomedicine ; Calcium-Calmodulin-Dependent Protein Kinase Type 2 - metabolism ; Hippocampus - metabolism ; Human Physiology ; Interneurons - physiology ; Long-Term Potentiation - physiology ; N-Methylaspartate - metabolism ; Neurology ; Neurosciences ; Original ; Original Article ; Pain Medicine ; Receptors, AMPA - physiology ; Receptors, N-Methyl-D-Aspartate - metabolism ; Synapses - physiology</subject><ispartof>Neuroscience bulletin, 2022-08, Vol.38 (8), p.916-926</ispartof><rights>Center for Excellence in Brain Science and Intelligence Technology, Chinese Academy of Sciences 2022</rights><rights>2022. Center for Excellence in Brain Science and Intelligence Technology, Chinese Academy of Sciences.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c495t-e9c66206c5e8e3806cca86878794cb0232f5915ebae92f861f69dd8f9c41e6dc3</citedby><cites>FETCH-LOGICAL-c495t-e9c66206c5e8e3806cca86878794cb0232f5915ebae92f861f69dd8f9c41e6dc3</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/PMC9352831/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC9352831/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,725,778,782,883,27907,27908,41471,42540,51302,53774,53776</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/35290589$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>He, Xingzhi</creatorcontrib><creatorcontrib>Wang, Yang</creatorcontrib><creatorcontrib>Zhou, Guangjun</creatorcontrib><creatorcontrib>Yang, Jing</creatorcontrib><creatorcontrib>Li, Jiarui</creatorcontrib><creatorcontrib>Li, Tao</creatorcontrib><creatorcontrib>Hu, Hailan</creatorcontrib><creatorcontrib>Ma, Huan</creatorcontrib><title>A Critical Role for γCaMKII in Decoding NMDA Signaling to Regulate AMPA Receptors in Putative Inhibitory Interneurons</title><title>Neuroscience bulletin</title><addtitle>Neurosci. Bull</addtitle><addtitle>Neurosci Bull</addtitle><description>CaMKII is essential for long-term potentiation (LTP), a process in which synaptic strength is increased following the acquisition of information. Among the four CaMKII isoforms, γCaMKII is the one that mediates the LTP of excitatory synapses onto inhibitory interneurons (LTP
E→I
). However, the molecular mechanism underlying how γCaMKII mediates LTP
E→I
remains unclear. Here, we show that γCaMKII is highly enriched in cultured hippocampal inhibitory interneurons and opts to be activated by higher stimulating frequencies in the 10–30 Hz range. Following stimulation, γCaMKII is translocated to the synapse and becomes co-localized with the postsynaptic protein PSD-95. Knocking down γCaMKII prevents the chemical LTP-induced phosphorylation and trafficking of AMPA receptors (AMPARs) in putative inhibitory interneurons, which are restored by overexpression of γCaMKII but not its kinase-dead form. Taken together, these data suggest that γCaMKII decodes NMDAR-mediated signaling and in turn regulates AMPARs for expressing LTP in inhibitory interneurons.</description><subject>Anatomy</subject><subject>Anesthesiology</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Calcium-Calmodulin-Dependent Protein Kinase Type 2 - metabolism</subject><subject>Hippocampus - metabolism</subject><subject>Human Physiology</subject><subject>Interneurons - physiology</subject><subject>Long-Term Potentiation - physiology</subject><subject>N-Methylaspartate - metabolism</subject><subject>Neurology</subject><subject>Neurosciences</subject><subject>Original</subject><subject>Original Article</subject><subject>Pain Medicine</subject><subject>Receptors, AMPA - physiology</subject><subject>Receptors, N-Methyl-D-Aspartate - metabolism</subject><subject>Synapses - physiology</subject><issn>1673-7067</issn><issn>1995-8218</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kc1u3CAUhVGVqvlpX6CLiGU2TgHbGDaRrEnbjJppo7RdIwZfO0QemAIeJc-V98gzhemkUbvpinu555yL-BB6T8kpJaT5ECljvCoIYwUhoiLF3St0QKWsC8Go2Ms1b8qiIbzZR4cx3hLCSVNWb9B-WTNJaiEP0KbFs2CTNXrE134E3PuAHx9mevFlPsfW4XMwvrNuwF8X5y3-bgenx22bPL6GYRp1AtwurtrcGVgnH-LWdTUlnewG8Nzd2KXN1_e5TBAcTMG7-Ba97vUY4d3zeYR-fvr4Y3ZRXH77PJ-1l4WpZJ0KkIZzRripQUApcmG04KIRjazMkrCS9bWkNSw1SNYLTnsuu0700lQUeGfKI3S2y11PyxV0BlwKelTrYFc63Cuvrfp34uyNGvxGyfxFoqQ54OQ5IPhfE8SkVjYaGEftwE9RZQCEVKJmWynbSU3wMQboX9ZQorbA1A6YysDUb2DqLpuO_37gi-UPoSwod4KYR26AoG79FDKE-L_YJ0Dro3Y</recordid><startdate>20220801</startdate><enddate>20220801</enddate><creator>He, Xingzhi</creator><creator>Wang, Yang</creator><creator>Zhou, Guangjun</creator><creator>Yang, Jing</creator><creator>Li, Jiarui</creator><creator>Li, Tao</creator><creator>Hu, Hailan</creator><creator>Ma, Huan</creator><general>Springer Nature Singapore</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>7X8</scope><scope>5PM</scope></search><sort><creationdate>20220801</creationdate><title>A Critical Role for γCaMKII in Decoding NMDA Signaling to Regulate AMPA Receptors in Putative Inhibitory Interneurons</title><author>He, Xingzhi ; Wang, Yang ; Zhou, Guangjun ; Yang, Jing ; Li, Jiarui ; Li, Tao ; Hu, Hailan ; Ma, Huan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c495t-e9c66206c5e8e3806cca86878794cb0232f5915ebae92f861f69dd8f9c41e6dc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Anatomy</topic><topic>Anesthesiology</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Calcium-Calmodulin-Dependent Protein Kinase Type 2 - metabolism</topic><topic>Hippocampus - metabolism</topic><topic>Human Physiology</topic><topic>Interneurons - physiology</topic><topic>Long-Term Potentiation - physiology</topic><topic>N-Methylaspartate - metabolism</topic><topic>Neurology</topic><topic>Neurosciences</topic><topic>Original</topic><topic>Original Article</topic><topic>Pain Medicine</topic><topic>Receptors, AMPA - physiology</topic><topic>Receptors, N-Methyl-D-Aspartate - metabolism</topic><topic>Synapses - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>He, Xingzhi</creatorcontrib><creatorcontrib>Wang, Yang</creatorcontrib><creatorcontrib>Zhou, Guangjun</creatorcontrib><creatorcontrib>Yang, Jing</creatorcontrib><creatorcontrib>Li, Jiarui</creatorcontrib><creatorcontrib>Li, Tao</creatorcontrib><creatorcontrib>Hu, Hailan</creatorcontrib><creatorcontrib>Ma, Huan</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Neuroscience bulletin</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>He, Xingzhi</au><au>Wang, Yang</au><au>Zhou, Guangjun</au><au>Yang, Jing</au><au>Li, Jiarui</au><au>Li, Tao</au><au>Hu, Hailan</au><au>Ma, Huan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Critical Role for γCaMKII in Decoding NMDA Signaling to Regulate AMPA Receptors in Putative Inhibitory Interneurons</atitle><jtitle>Neuroscience bulletin</jtitle><stitle>Neurosci. Bull</stitle><addtitle>Neurosci Bull</addtitle><date>2022-08-01</date><risdate>2022</risdate><volume>38</volume><issue>8</issue><spage>916</spage><epage>926</epage><pages>916-926</pages><issn>1673-7067</issn><eissn>1995-8218</eissn><abstract>CaMKII is essential for long-term potentiation (LTP), a process in which synaptic strength is increased following the acquisition of information. Among the four CaMKII isoforms, γCaMKII is the one that mediates the LTP of excitatory synapses onto inhibitory interneurons (LTP
E→I
). However, the molecular mechanism underlying how γCaMKII mediates LTP
E→I
remains unclear. Here, we show that γCaMKII is highly enriched in cultured hippocampal inhibitory interneurons and opts to be activated by higher stimulating frequencies in the 10–30 Hz range. Following stimulation, γCaMKII is translocated to the synapse and becomes co-localized with the postsynaptic protein PSD-95. Knocking down γCaMKII prevents the chemical LTP-induced phosphorylation and trafficking of AMPA receptors (AMPARs) in putative inhibitory interneurons, which are restored by overexpression of γCaMKII but not its kinase-dead form. Taken together, these data suggest that γCaMKII decodes NMDAR-mediated signaling and in turn regulates AMPARs for expressing LTP in inhibitory interneurons.</abstract><cop>Singapore</cop><pub>Springer Nature Singapore</pub><pmid>35290589</pmid><doi>10.1007/s12264-022-00840-x</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Springer Nature - Complete Springer Journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Anatomy Anesthesiology Biomedical and Life Sciences Biomedicine Calcium-Calmodulin-Dependent Protein Kinase Type 2 - metabolism Hippocampus - metabolism Human Physiology Interneurons - physiology Long-Term Potentiation - physiology N-Methylaspartate - metabolism Neurology Neurosciences Original Original Article Pain Medicine Receptors, AMPA - physiology Receptors, N-Methyl-D-Aspartate - metabolism Synapses - physiology |
| title | A Critical Role for γCaMKII in Decoding NMDA Signaling to Regulate AMPA Receptors in Putative Inhibitory Interneurons |
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