Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C
Neurotransmitters are released at synapses by the Ca2(+)-regulated exocytosis of synaptic vesicles, which are specialized secretory organelles that store high concentrations of neurotransmitters. The rapid Ca2(+)-triggered fusion of synaptic vesicles is presumably mediated by specific proteins that...
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| Veröffentlicht in: | Nature (London) 1990-05, Vol.345 (6272), p.260-263 |
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| creator | Perin, Mark S Fried, Victor A Mignery, Gregory A Jahn, Reinhard Südhof, Thomas C |
| description | Neurotransmitters are released at synapses by the Ca2(+)-regulated exocytosis of synaptic vesicles, which are specialized secretory organelles that store high concentrations of neurotransmitters. The rapid Ca2(+)-triggered fusion of synaptic vesicles is presumably mediated by specific proteins that must interact with Ca2+ and the phospholipid bilayer. We now report that the cytoplasmic domain of p65, a synaptic vesicle-specific protein that binds calmodulin contains an internally repeated sequence that is homologous to the regulatory C2-region of protein kinase C (PKC). The cytoplasmic domain of recombinant p65 binds acidic phospholipids with a specificity indicating an interaction of p65 with the hydrophobic core as well as the headgroups of the phospholipids. The binding specificity resembles PKC, except that p65 also binds calmodulin, placing the C2-regions in a context of potential Ca2(+)-regulation that is different from PKC. This is a novel homology between a cellular protein and the regulatory domain of protein kinase C. The structure and properties of p65 suggest that it may have a role in mediating membrane interactions during synaptic vesicle exocytosis. |
| doi_str_mv | 10.1038/345260a0 |
| format | Article |
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The rapid Ca2(+)-triggered fusion of synaptic vesicles is presumably mediated by specific proteins that must interact with Ca2+ and the phospholipid bilayer. We now report that the cytoplasmic domain of p65, a synaptic vesicle-specific protein that binds calmodulin contains an internally repeated sequence that is homologous to the regulatory C2-region of protein kinase C (PKC). The cytoplasmic domain of recombinant p65 binds acidic phospholipids with a specificity indicating an interaction of p65 with the hydrophobic core as well as the headgroups of the phospholipids. The binding specificity resembles PKC, except that p65 also binds calmodulin, placing the C2-regions in a context of potential Ca2(+)-regulation that is different from PKC. This is a novel homology between a cellular protein and the regulatory domain of protein kinase C. The structure and properties of p65 suggest that it may have a role in mediating membrane interactions during synaptic vesicle exocytosis.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/345260a0</identifier><identifier>PMID: 2333096</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing</publisher><subject>Amino Acid Sequence ; Amino acids ; Animals ; Base Sequence ; Binding ; Binding sites ; Biological and medical sciences ; Calcium ions ; Calcium-binding protein ; Calmodulin ; Cellular structure ; Cloning, Molecular ; Deoxyribonucleic acid ; DNA ; Exocytosis ; Fundamental and applied biological sciences. Psychology ; Genes. Genome ; Hemagglutination Inhibition Tests ; Homology ; Hydrophobicity ; Kinases ; Lipids ; Molecular and cellular biology ; Molecular genetics ; Molecular Sequence Data ; Molecular Weight ; Nerve Tissue Proteins - genetics ; Nerve Tissue Proteins - metabolism ; Nervous system ; Neurotransmitters ; Organelles ; Phospholipids ; Phospholipids - metabolism ; Protein kinase C ; Protein Kinase C - genetics ; Protein structure ; Proteins ; Rabbits ; Rats ; Recombinant Proteins - metabolism ; Regulatory sequences ; RNA, Messenger - genetics ; Secretory vesicles ; Sequence Homology, Nucleic Acid ; Synapses ; Synaptic vesicles ; Synaptic Vesicles - metabolism ; Vesicle fusion ; Vesicles</subject><ispartof>Nature (London), 1990-05, Vol.345 (6272), p.260-263</ispartof><rights>1991 INIST-CNRS</rights><rights>Copyright Macmillan Journals Ltd. May 17, 1990</rights><rights>Copyright Nature Publishing Group May 17, 1990</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c484t-72f6284441d26d8c9119a295d72df8b69a8c5e57cf25f646145753b0ea62645b3</citedby><cites>FETCH-LOGICAL-c484t-72f6284441d26d8c9119a295d72df8b69a8c5e57cf25f646145753b0ea62645b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,782,786,2731,27933,27934</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19493190$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2333096$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Perin, Mark S</creatorcontrib><creatorcontrib>Fried, Victor A</creatorcontrib><creatorcontrib>Mignery, Gregory A</creatorcontrib><creatorcontrib>Jahn, Reinhard</creatorcontrib><creatorcontrib>Südhof, Thomas C</creatorcontrib><title>Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C</title><title>Nature (London)</title><addtitle>Nature</addtitle><description>Neurotransmitters are released at synapses by the Ca2(+)-regulated exocytosis of synaptic vesicles, which are specialized secretory organelles that store high concentrations of neurotransmitters. 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The structure and properties of p65 suggest that it may have a role in mediating membrane interactions during synaptic vesicle exocytosis.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Binding</subject><subject>Binding sites</subject><subject>Biological and medical sciences</subject><subject>Calcium ions</subject><subject>Calcium-binding protein</subject><subject>Calmodulin</subject><subject>Cellular structure</subject><subject>Cloning, Molecular</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>Exocytosis</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes. 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Academic</collection><jtitle>Nature (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Perin, Mark S</au><au>Fried, Victor A</au><au>Mignery, Gregory A</au><au>Jahn, Reinhard</au><au>Südhof, Thomas C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C</atitle><jtitle>Nature (London)</jtitle><addtitle>Nature</addtitle><date>1990-05-17</date><risdate>1990</risdate><volume>345</volume><issue>6272</issue><spage>260</spage><epage>263</epage><pages>260-263</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><coden>NATUAS</coden><abstract>Neurotransmitters are released at synapses by the Ca2(+)-regulated exocytosis of synaptic vesicles, which are specialized secretory organelles that store high concentrations of neurotransmitters. The rapid Ca2(+)-triggered fusion of synaptic vesicles is presumably mediated by specific proteins that must interact with Ca2+ and the phospholipid bilayer. We now report that the cytoplasmic domain of p65, a synaptic vesicle-specific protein that binds calmodulin contains an internally repeated sequence that is homologous to the regulatory C2-region of protein kinase C (PKC). The cytoplasmic domain of recombinant p65 binds acidic phospholipids with a specificity indicating an interaction of p65 with the hydrophobic core as well as the headgroups of the phospholipids. The binding specificity resembles PKC, except that p65 also binds calmodulin, placing the C2-regions in a context of potential Ca2(+)-regulation that is different from PKC. This is a novel homology between a cellular protein and the regulatory domain of protein kinase C. The structure and properties of p65 suggest that it may have a role in mediating membrane interactions during synaptic vesicle exocytosis.</abstract><cop>London</cop><pub>Nature Publishing</pub><pmid>2333096</pmid><doi>10.1038/345260a0</doi><tpages>4</tpages></addata></record> |
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| ispartof | Nature (London), 1990-05, Vol.345 (6272), p.260-263 |
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| subjects | Amino Acid Sequence Amino acids Animals Base Sequence Binding Binding sites Biological and medical sciences Calcium ions Calcium-binding protein Calmodulin Cellular structure Cloning, Molecular Deoxyribonucleic acid DNA Exocytosis Fundamental and applied biological sciences. Psychology Genes. Genome Hemagglutination Inhibition Tests Homology Hydrophobicity Kinases Lipids Molecular and cellular biology Molecular genetics Molecular Sequence Data Molecular Weight Nerve Tissue Proteins - genetics Nerve Tissue Proteins - metabolism Nervous system Neurotransmitters Organelles Phospholipids Phospholipids - metabolism Protein kinase C Protein Kinase C - genetics Protein structure Proteins Rabbits Rats Recombinant Proteins - metabolism Regulatory sequences RNA, Messenger - genetics Secretory vesicles Sequence Homology, Nucleic Acid Synapses Synaptic vesicles Synaptic Vesicles - metabolism Vesicle fusion Vesicles |
| title | Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C |
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