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Structurally and functionally unique complexins at retinal ribbon synapses
Ribbon synapses in retinal sensory neurons maintain large pools of readily releasable synaptic vesicles. This allows them to release several hundreds of vesicles per second at every presynaptic release site. The molecular components that cause this high transmitter release efficiency of ribbon synap...
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| Published in: | The Journal of cell biology 2005-05, Vol.169 (4), p.669-680 |
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| Main Authors: | , , , , , , , |
| Format: | Article |
| Language: | English |
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| cites | cdi_FETCH-LOGICAL-c554t-f5456337403680111efe049f39d0d9645a41d77fcd3bfe060f63e7dbd83df5d83 |
| container_end_page | 680 |
| container_issue | 4 |
| container_start_page | 669 |
| container_title | The Journal of cell biology |
| container_volume | 169 |
| creator | Reim, Kerstin Wegmeyer, Heike Brandstätter, Johann Helmut Xue, Mingshan Rosenmund, Christian Dresbach, Thomas Hofmann, Kay Brose, Nils |
| description | Ribbon synapses in retinal sensory neurons maintain large pools of readily releasable synaptic vesicles. This allows them to release several hundreds of vesicles per second at every presynaptic release site. The molecular components that cause this high transmitter release efficiency of ribbon synapses are unknown. In the present study, we identified and characterized two novel vertebrate complexins (CPXs), CPXs III and IV, that are the only CPX isoforms present in retinal ribbon synapses. CPXs III and IV are COOH-terminally farnesylated, and, like CPXs I and II, bind to SNAP receptor complexes. CPXs III and IV can functionally replace CPXs I and II, and their COOH-terminal farnesylation regulates their synaptic targeting and modulatory function in transmitter release. The novel CPXs III and IV may contribute to the unique release efficacy of retinal sensory neurons. |
| doi_str_mv | 10.1083/jcb.200502115 |
| format | article |
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This allows them to release several hundreds of vesicles per second at every presynaptic release site. The molecular components that cause this high transmitter release efficiency of ribbon synapses are unknown. In the present study, we identified and characterized two novel vertebrate complexins (CPXs), CPXs III and IV, that are the only CPX isoforms present in retinal ribbon synapses. CPXs III and IV are COOH-terminally farnesylated, and, like CPXs I and II, bind to SNAP receptor complexes. CPXs III and IV can functionally replace CPXs I and II, and their COOH-terminal farnesylation regulates their synaptic targeting and modulatory function in transmitter release. The novel CPXs III and IV may contribute to the unique release efficacy of retinal sensory neurons.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.200502115</identifier><identifier>PMID: 15911881</identifier><identifier>CODEN: JCLBA3</identifier><language>eng</language><publisher>United States: Rockefeller University Press</publisher><subject>Adaptor Proteins, Vesicular Transport ; Amacrine cells ; Animals ; Cell Line ; Cell membranes ; Cellular biology ; Complementary DNA ; Eye Proteins - genetics ; Eye Proteins - isolation & purification ; Eye Proteins - metabolism ; HEK293 cells ; Humans ; Membrane Proteins - genetics ; Membrane Proteins - isolation & purification ; Membrane Proteins - metabolism ; Messenger RNA ; Mice ; Molecular Sequence Data ; Nerve Tissue Proteins - genetics ; Nerve Tissue Proteins - isolation & purification ; Nerve Tissue Proteins - metabolism ; Neurons ; Organelles - metabolism ; Photoreceptor Cells - metabolism ; Photoreceptors ; Protein Binding - physiology ; Protein isoforms ; Protein Prenylation - physiology ; Protein Structure, Tertiary - physiology ; Retina ; Retina - metabolism ; Sequence Homology, Amino Acid ; Sequence Homology, Nucleic Acid ; SNARE Proteins ; Synapses ; Synapses - metabolism ; Synaptic Transmission - physiology ; Vesicular Transport Proteins - metabolism</subject><ispartof>The Journal of cell biology, 2005-05, Vol.169 (4), p.669-680</ispartof><rights>Copyright 2005 The Rockefeller University Press</rights><rights>Copyright Rockefeller University Press May 23, 2005</rights><rights>Copyright © 2005, The Rockefeller University Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c554t-f5456337403680111efe049f39d0d9645a41d77fcd3bfe060f63e7dbd83df5d83</citedby><cites>FETCH-LOGICAL-c554t-f5456337403680111efe049f39d0d9645a41d77fcd3bfe060f63e7dbd83df5d83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15911881$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Reim, Kerstin</creatorcontrib><creatorcontrib>Wegmeyer, Heike</creatorcontrib><creatorcontrib>Brandstätter, Johann Helmut</creatorcontrib><creatorcontrib>Xue, Mingshan</creatorcontrib><creatorcontrib>Rosenmund, Christian</creatorcontrib><creatorcontrib>Dresbach, Thomas</creatorcontrib><creatorcontrib>Hofmann, Kay</creatorcontrib><creatorcontrib>Brose, Nils</creatorcontrib><title>Structurally and functionally unique complexins at retinal ribbon synapses</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>Ribbon synapses in retinal sensory neurons maintain large pools of readily releasable synaptic vesicles. This allows them to release several hundreds of vesicles per second at every presynaptic release site. The molecular components that cause this high transmitter release efficiency of ribbon synapses are unknown. In the present study, we identified and characterized two novel vertebrate complexins (CPXs), CPXs III and IV, that are the only CPX isoforms present in retinal ribbon synapses. CPXs III and IV are COOH-terminally farnesylated, and, like CPXs I and II, bind to SNAP receptor complexes. CPXs III and IV can functionally replace CPXs I and II, and their COOH-terminal farnesylation regulates their synaptic targeting and modulatory function in transmitter release. The novel CPXs III and IV may contribute to the unique release efficacy of retinal sensory neurons.</description><subject>Adaptor Proteins, Vesicular Transport</subject><subject>Amacrine cells</subject><subject>Animals</subject><subject>Cell Line</subject><subject>Cell membranes</subject><subject>Cellular biology</subject><subject>Complementary DNA</subject><subject>Eye Proteins - genetics</subject><subject>Eye Proteins - isolation & purification</subject><subject>Eye Proteins - metabolism</subject><subject>HEK293 cells</subject><subject>Humans</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - isolation & purification</subject><subject>Membrane Proteins - metabolism</subject><subject>Messenger RNA</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Nerve Tissue Proteins - genetics</subject><subject>Nerve Tissue Proteins - isolation & purification</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>Neurons</subject><subject>Organelles - metabolism</subject><subject>Photoreceptor Cells - metabolism</subject><subject>Photoreceptors</subject><subject>Protein Binding - physiology</subject><subject>Protein isoforms</subject><subject>Protein Prenylation - physiology</subject><subject>Protein Structure, Tertiary - physiology</subject><subject>Retina</subject><subject>Retina - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>SNARE Proteins</subject><subject>Synapses</subject><subject>Synapses - metabolism</subject><subject>Synaptic Transmission - physiology</subject><subject>Vesicular Transport Proteins - metabolism</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><recordid>eNqFkbtvFDEQxi0EIpdASYdgRUG3YWb9bpBQRHgoEkVIbXl37eDTnn3Yu4j773Fyp-PR0NjSfD_NfDMfIc8QzhEUfbMe-vMOgEOHyB-QFXIGrUIGD8kKarHVvOMn5LSUNQAwyehjcoJcIyqFK_L5es7LMC_ZTtOusXFs_BKHOaR4X1hi-L64Zkib7eR-hlgaOzfZzaHKTQ59n2JTdtFuiytPyCNvp-KeHv4zcnP5_uvFx_bqy4dPF--u2oFzNreeMy4olQyoUICIzjtg2lM9wqgF45bhKKUfRtpXRYAX1MmxHxUdPa_vGXm777td-o0bBxfn6t5sc9jYvDPJBvO3EsM3c5t-mA4lSsDa4PWhQU51uzKbTSiDmyYbXVqKEVJxLrj6L4iSMiVBVPDVP-A6LbneqNwPRan13dh2Dw05lZKdP1pGMHdZmpqlOWZZ-Rd_7vmbPoRXged7YF3mlI86rdZR6Cq_3MveJmNvcyjm5rqr-wNozaUS9BfYc63Q</recordid><startdate>20050523</startdate><enddate>20050523</enddate><creator>Reim, Kerstin</creator><creator>Wegmeyer, Heike</creator><creator>Brandstätter, Johann Helmut</creator><creator>Xue, Mingshan</creator><creator>Rosenmund, Christian</creator><creator>Dresbach, Thomas</creator><creator>Hofmann, Kay</creator><creator>Brose, Nils</creator><general>Rockefeller University Press</general><general>The Rockefeller University Press</general><scope>FBQ</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>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20050523</creationdate><title>Structurally and functionally unique complexins at retinal ribbon synapses</title><author>Reim, Kerstin ; 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| ispartof | The Journal of cell biology, 2005-05, Vol.169 (4), p.669-680 |
| issn | 0021-9525 1540-8140 |
| language | eng |
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| source | Alma/SFX Local Collection |
| subjects | Adaptor Proteins, Vesicular Transport Amacrine cells Animals Cell Line Cell membranes Cellular biology Complementary DNA Eye Proteins - genetics Eye Proteins - isolation & purification Eye Proteins - metabolism HEK293 cells Humans Membrane Proteins - genetics Membrane Proteins - isolation & purification Membrane Proteins - metabolism Messenger RNA Mice Molecular Sequence Data Nerve Tissue Proteins - genetics Nerve Tissue Proteins - isolation & purification Nerve Tissue Proteins - metabolism Neurons Organelles - metabolism Photoreceptor Cells - metabolism Photoreceptors Protein Binding - physiology Protein isoforms Protein Prenylation - physiology Protein Structure, Tertiary - physiology Retina Retina - metabolism Sequence Homology, Amino Acid Sequence Homology, Nucleic Acid SNARE Proteins Synapses Synapses - metabolism Synaptic Transmission - physiology Vesicular Transport Proteins - metabolism |
| title | Structurally and functionally unique complexins at retinal ribbon synapses |
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