Differential interactions of cerebellin precursor protein (Cbln) subtypes and neurexin variants for synapse formation of cortical neurons
► Cbln1 and Cbln2 induce presynaptic differentiation of cortical neurons. ► Synaptogenic activities of Cbln1 and Cbln2 require the interaction with neurexins. ► Cbln1, Cbln2 and Cbln4 selectively bind to neurexin variants with splice segment 4. ► Cbln subtypes show differential affinities to neurexi...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2011-03, Vol.406 (4), p.627-632 |
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| description | ► Cbln1 and Cbln2 induce presynaptic differentiation of cortical neurons. ► Synaptogenic activities of Cbln1 and Cbln2 require the interaction with neurexins. ► Cbln1, Cbln2 and Cbln4 selectively bind to neurexin variants with splice segment 4. ► Cbln subtypes show differential affinities to neurexin variants.
Trans-synaptic interaction of postsynaptic glutamate receptor δ2 and presynaptic neurexins (NRXNs) through cerebellin precursor protein (Cbln) 1 mediates synapse formation in the cerebellum [T. Uemura, S.J. Lee, M. Yasumura, T. Takeuchi, T. Yoshida, M. Ra, R. Taguchi, K. Sakimura, M. Mishina, Cell 141 (2010) 1068–1079]. This finding raises a question whether other Cbln family members interact with NRXNs to regulate synapse formation in the forebrain. Here, we showed that Cbln1 and Cbln2 induced presynaptic differentiation of cultured cortical neurons, while Cbln4 exhibited little activity. When compared with neuroligin 1, Cbln1 and Cbln2 induced preferentially inhibitory presynaptic differentiation rather than excitatory one in cortical cultures. The synaptogenic activities of Cbln1 and Cbln2 were suppressed by the addition of the extracellular domain of NRXN1β to the cortical neuron cultures. Consistently, Cbln1 and Cbln2 showed robust binding activities to NRXN1α and three β-NRXNs, while only weak interactions were observed between Cbln4 and NRXNs. The interactions of Cbln1, Cbln2 and Cbln4 were selective for NRXN variants containing splice segment (S) 4. Affinities for NRXNs estimated by surface plasmon resonance analysis were variable among Cbln subtypes. Cbln1 showed higher affinities to NRXNs than Cbln2, while the binding ability of Cbln4 was much lower than those of Cbln1 and Cbln2. The affinities of Cbln1 and Cbln2 were comparable between NRXN1α and NRXN1β, but those for NRXN2β and NRXN3β were lower. These results suggest that Cbln subtypes exert synaptogenic activities in cortical neurons by differentially interacting with NRXN variants containing S4. |
| doi_str_mv | 10.1016/j.bbrc.2011.02.108 |
| format | Article |
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Trans-synaptic interaction of postsynaptic glutamate receptor δ2 and presynaptic neurexins (NRXNs) through cerebellin precursor protein (Cbln) 1 mediates synapse formation in the cerebellum [T. Uemura, S.J. Lee, M. Yasumura, T. Takeuchi, T. Yoshida, M. Ra, R. Taguchi, K. Sakimura, M. Mishina, Cell 141 (2010) 1068–1079]. This finding raises a question whether other Cbln family members interact with NRXNs to regulate synapse formation in the forebrain. Here, we showed that Cbln1 and Cbln2 induced presynaptic differentiation of cultured cortical neurons, while Cbln4 exhibited little activity. When compared with neuroligin 1, Cbln1 and Cbln2 induced preferentially inhibitory presynaptic differentiation rather than excitatory one in cortical cultures. The synaptogenic activities of Cbln1 and Cbln2 were suppressed by the addition of the extracellular domain of NRXN1β to the cortical neuron cultures. Consistently, Cbln1 and Cbln2 showed robust binding activities to NRXN1α and three β-NRXNs, while only weak interactions were observed between Cbln4 and NRXNs. The interactions of Cbln1, Cbln2 and Cbln4 were selective for NRXN variants containing splice segment (S) 4. Affinities for NRXNs estimated by surface plasmon resonance analysis were variable among Cbln subtypes. Cbln1 showed higher affinities to NRXNs than Cbln2, while the binding ability of Cbln4 was much lower than those of Cbln1 and Cbln2. The affinities of Cbln1 and Cbln2 were comparable between NRXN1α and NRXN1β, but those for NRXN2β and NRXN3β were lower. These results suggest that Cbln subtypes exert synaptogenic activities in cortical neurons by differentially interacting with NRXN variants containing S4.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2011.02.108</identifier><identifier>PMID: 21356198</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Cblns ; Cell culture ; Cerebellum ; Cerebral Cortex - cytology ; Cerebral Cortex - physiology ; Cortex ; Differentiation ; Forebrain ; Glutamic acid receptors ; Mice ; Mice, Inbred ICR ; Nerve Tissue Proteins - genetics ; Nerve Tissue Proteins - metabolism ; Neurexin ; Neurons - cytology ; Neurons - physiology ; Protein Binding ; Protein Precursors - genetics ; Protein Precursors - metabolism ; surface plasmon resonance ; Synapse formation ; Synapses - metabolism ; Synapses - physiology ; Synaptogenesis</subject><ispartof>Biochemical and biophysical research communications, 2011-03, Vol.406 (4), p.627-632</ispartof><rights>2011 Elsevier Inc.</rights><rights>Copyright © 2011 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c454t-14f63a812411c70aa1f3713d2595e71f7b6df7d41e15e6dfdf28c627ca2963403</citedby><cites>FETCH-LOGICAL-c454t-14f63a812411c70aa1f3713d2595e71f7b6df7d41e15e6dfdf28c627ca2963403</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006291X11003135$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21356198$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Joo, Jae-Yeol</creatorcontrib><creatorcontrib>Lee, Sung-Jin</creatorcontrib><creatorcontrib>Uemura, Takeshi</creatorcontrib><creatorcontrib>Yoshida, Tomoyuki</creatorcontrib><creatorcontrib>Yasumura, Misato</creatorcontrib><creatorcontrib>Watanabe, Masahiko</creatorcontrib><creatorcontrib>Mishina, Masayoshi</creatorcontrib><title>Differential interactions of cerebellin precursor protein (Cbln) subtypes and neurexin variants for synapse formation of cortical neurons</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>► Cbln1 and Cbln2 induce presynaptic differentiation of cortical neurons. ► Synaptogenic activities of Cbln1 and Cbln2 require the interaction with neurexins. ► Cbln1, Cbln2 and Cbln4 selectively bind to neurexin variants with splice segment 4. ► Cbln subtypes show differential affinities to neurexin variants.
Trans-synaptic interaction of postsynaptic glutamate receptor δ2 and presynaptic neurexins (NRXNs) through cerebellin precursor protein (Cbln) 1 mediates synapse formation in the cerebellum [T. Uemura, S.J. Lee, M. Yasumura, T. Takeuchi, T. Yoshida, M. Ra, R. Taguchi, K. Sakimura, M. Mishina, Cell 141 (2010) 1068–1079]. This finding raises a question whether other Cbln family members interact with NRXNs to regulate synapse formation in the forebrain. Here, we showed that Cbln1 and Cbln2 induced presynaptic differentiation of cultured cortical neurons, while Cbln4 exhibited little activity. When compared with neuroligin 1, Cbln1 and Cbln2 induced preferentially inhibitory presynaptic differentiation rather than excitatory one in cortical cultures. The synaptogenic activities of Cbln1 and Cbln2 were suppressed by the addition of the extracellular domain of NRXN1β to the cortical neuron cultures. Consistently, Cbln1 and Cbln2 showed robust binding activities to NRXN1α and three β-NRXNs, while only weak interactions were observed between Cbln4 and NRXNs. The interactions of Cbln1, Cbln2 and Cbln4 were selective for NRXN variants containing splice segment (S) 4. Affinities for NRXNs estimated by surface plasmon resonance analysis were variable among Cbln subtypes. Cbln1 showed higher affinities to NRXNs than Cbln2, while the binding ability of Cbln4 was much lower than those of Cbln1 and Cbln2. The affinities of Cbln1 and Cbln2 were comparable between NRXN1α and NRXN1β, but those for NRXN2β and NRXN3β were lower. These results suggest that Cbln subtypes exert synaptogenic activities in cortical neurons by differentially interacting with NRXN variants containing S4.</description><subject>Animals</subject><subject>Cblns</subject><subject>Cell culture</subject><subject>Cerebellum</subject><subject>Cerebral Cortex - cytology</subject><subject>Cerebral Cortex - physiology</subject><subject>Cortex</subject><subject>Differentiation</subject><subject>Forebrain</subject><subject>Glutamic acid receptors</subject><subject>Mice</subject><subject>Mice, Inbred ICR</subject><subject>Nerve Tissue Proteins - genetics</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>Neurexin</subject><subject>Neurons - cytology</subject><subject>Neurons - physiology</subject><subject>Protein Binding</subject><subject>Protein Precursors - genetics</subject><subject>Protein Precursors - metabolism</subject><subject>surface plasmon resonance</subject><subject>Synapse formation</subject><subject>Synapses - metabolism</subject><subject>Synapses - physiology</subject><subject>Synaptogenesis</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kcFq3DAQhkVpSTZpXqCH4lvTg7ca2ZJt6CVsmqQQ6KWF3oQsj0CLV95Kcsg-Qt66426aY04aZr7_H0Y_Yx-Ar4GD-rJd9320a8EB1lxQr33DVsA7Xgrg9Vu24pyrUnTw-5SdpbTlBNaqO2GnAiqpoGtX7OnaO4cRQ_ZmLHzIGI3NfgqpmFxhadLjOPpQ7CPaOaYpUjVlpM7lph_D5yLNfT7sMRUmDEXAOeIjDR9M9CbkVDhSpEMw-4RLvTOL-T_vKWZvaemioX3v2TtnxoQXz-85-3Xz7efmrrz_cft9c3Vf2lrWuYTaqcq0IGoA23BjwFUNVIOQncQGXNOrwTVDDQgSqRycaK0SjTWiU1XNq3P26ehLd_yZMWW988nSkSbgNCfdyo7LFiQQefkqSSE0nQIFklBxRG2cUoro9D76nYkHghZO6a1ewtJLWJoL6rUk-vjsP_c7HF4k_9Mh4OsRQPqPB49RJ-sxWBw8pZH1MPnX_P8CqxyoLQ</recordid><startdate>20110325</startdate><enddate>20110325</enddate><creator>Joo, Jae-Yeol</creator><creator>Lee, Sung-Jin</creator><creator>Uemura, Takeshi</creator><creator>Yoshida, Tomoyuki</creator><creator>Yasumura, Misato</creator><creator>Watanabe, Masahiko</creator><creator>Mishina, Masayoshi</creator><general>Elsevier Inc</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>7TK</scope><scope>7X8</scope></search><sort><creationdate>20110325</creationdate><title>Differential interactions of cerebellin precursor protein (Cbln) subtypes and neurexin variants for synapse formation of cortical neurons</title><author>Joo, Jae-Yeol ; Lee, Sung-Jin ; Uemura, Takeshi ; Yoshida, Tomoyuki ; Yasumura, Misato ; Watanabe, Masahiko ; Mishina, Masayoshi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c454t-14f63a812411c70aa1f3713d2595e71f7b6df7d41e15e6dfdf28c627ca2963403</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Animals</topic><topic>Cblns</topic><topic>Cell culture</topic><topic>Cerebellum</topic><topic>Cerebral Cortex - cytology</topic><topic>Cerebral Cortex - physiology</topic><topic>Cortex</topic><topic>Differentiation</topic><topic>Forebrain</topic><topic>Glutamic acid receptors</topic><topic>Mice</topic><topic>Mice, Inbred ICR</topic><topic>Nerve Tissue Proteins - genetics</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>Neurexin</topic><topic>Neurons - cytology</topic><topic>Neurons - physiology</topic><topic>Protein Binding</topic><topic>Protein Precursors - genetics</topic><topic>Protein Precursors - metabolism</topic><topic>surface plasmon resonance</topic><topic>Synapse formation</topic><topic>Synapses - metabolism</topic><topic>Synapses - physiology</topic><topic>Synaptogenesis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Joo, Jae-Yeol</creatorcontrib><creatorcontrib>Lee, Sung-Jin</creatorcontrib><creatorcontrib>Uemura, Takeshi</creatorcontrib><creatorcontrib>Yoshida, Tomoyuki</creatorcontrib><creatorcontrib>Yasumura, Misato</creatorcontrib><creatorcontrib>Watanabe, Masahiko</creatorcontrib><creatorcontrib>Mishina, Masayoshi</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Neurosciences Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Joo, Jae-Yeol</au><au>Lee, Sung-Jin</au><au>Uemura, Takeshi</au><au>Yoshida, Tomoyuki</au><au>Yasumura, Misato</au><au>Watanabe, Masahiko</au><au>Mishina, Masayoshi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Differential interactions of cerebellin precursor protein (Cbln) subtypes and neurexin variants for synapse formation of cortical neurons</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2011-03-25</date><risdate>2011</risdate><volume>406</volume><issue>4</issue><spage>627</spage><epage>632</epage><pages>627-632</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>► Cbln1 and Cbln2 induce presynaptic differentiation of cortical neurons. ► Synaptogenic activities of Cbln1 and Cbln2 require the interaction with neurexins. ► Cbln1, Cbln2 and Cbln4 selectively bind to neurexin variants with splice segment 4. ► Cbln subtypes show differential affinities to neurexin variants.
Trans-synaptic interaction of postsynaptic glutamate receptor δ2 and presynaptic neurexins (NRXNs) through cerebellin precursor protein (Cbln) 1 mediates synapse formation in the cerebellum [T. Uemura, S.J. Lee, M. Yasumura, T. Takeuchi, T. Yoshida, M. Ra, R. Taguchi, K. Sakimura, M. Mishina, Cell 141 (2010) 1068–1079]. This finding raises a question whether other Cbln family members interact with NRXNs to regulate synapse formation in the forebrain. Here, we showed that Cbln1 and Cbln2 induced presynaptic differentiation of cultured cortical neurons, while Cbln4 exhibited little activity. When compared with neuroligin 1, Cbln1 and Cbln2 induced preferentially inhibitory presynaptic differentiation rather than excitatory one in cortical cultures. The synaptogenic activities of Cbln1 and Cbln2 were suppressed by the addition of the extracellular domain of NRXN1β to the cortical neuron cultures. Consistently, Cbln1 and Cbln2 showed robust binding activities to NRXN1α and three β-NRXNs, while only weak interactions were observed between Cbln4 and NRXNs. The interactions of Cbln1, Cbln2 and Cbln4 were selective for NRXN variants containing splice segment (S) 4. Affinities for NRXNs estimated by surface plasmon resonance analysis were variable among Cbln subtypes. Cbln1 showed higher affinities to NRXNs than Cbln2, while the binding ability of Cbln4 was much lower than those of Cbln1 and Cbln2. The affinities of Cbln1 and Cbln2 were comparable between NRXN1α and NRXN1β, but those for NRXN2β and NRXN3β were lower. These results suggest that Cbln subtypes exert synaptogenic activities in cortical neurons by differentially interacting with NRXN variants containing S4.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>21356198</pmid><doi>10.1016/j.bbrc.2011.02.108</doi><tpages>6</tpages></addata></record> |
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| subjects | Animals Cblns Cell culture Cerebellum Cerebral Cortex - cytology Cerebral Cortex - physiology Cortex Differentiation Forebrain Glutamic acid receptors Mice Mice, Inbred ICR Nerve Tissue Proteins - genetics Nerve Tissue Proteins - metabolism Neurexin Neurons - cytology Neurons - physiology Protein Binding Protein Precursors - genetics Protein Precursors - metabolism surface plasmon resonance Synapse formation Synapses - metabolism Synapses - physiology Synaptogenesis |
| title | Differential interactions of cerebellin precursor protein (Cbln) subtypes and neurexin variants for synapse formation of cortical neurons |
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