Cysteine-string proteins as templates for membrane fusion: models of synaptic vesicle exocytosis
Cysteine-string proteins are relatively small, cysteine-rich components of synaptic vesicle membranes. Recent investigations demonstrated that at least 11 of the 13 cysteine residues of the Torpedo cysteine-string protein are fatty acylated. This exceptional level of fatty acylation occurs along a s...
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Veröffentlicht in: | Journal of theoretical biology 1995-02, Vol.172 (3), p.269-277 |
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creator | Gundersen, Cameron B. Mastrogiacomo, Alessandro Umbach, Joy A. |
description | Cysteine-string proteins are relatively small, cysteine-rich components of synaptic vesicle membranes. Recent investigations demonstrated that at least 11 of the 13 cysteine residues of the Torpedo cysteine-string protein are fatty acylated. This exceptional level of fatty acylation occurs along a short stretch (less than 25 residues) of amino acids which are flanked on either side by very polar amino and carboxy termini. This amphipathic structure may have unique capabilities to catalyze events at membrane interfaces. We propose two distinct pathways to explain how these capabilities might subserve membrane fusion and exocytosis. |
doi_str_mv | 10.1006/jtbi.1995.0023 |
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Recent investigations demonstrated that at least 11 of the 13 cysteine residues of the Torpedo cysteine-string protein are fatty acylated. This exceptional level of fatty acylation occurs along a short stretch (less than 25 residues) of amino acids which are flanked on either side by very polar amino and carboxy termini. This amphipathic structure may have unique capabilities to catalyze events at membrane interfaces. 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Recent investigations demonstrated that at least 11 of the 13 cysteine residues of the Torpedo cysteine-string protein are fatty acylated. This exceptional level of fatty acylation occurs along a short stretch (less than 25 residues) of amino acids which are flanked on either side by very polar amino and carboxy termini. This amphipathic structure may have unique capabilities to catalyze events at membrane interfaces. We propose two distinct pathways to explain how these capabilities might subserve membrane fusion and exocytosis.</description><subject>Animals</subject><subject>Exocytosis - physiology</subject><subject>HSP40 Heat-Shock Proteins</subject><subject>Membrane Fusion</subject><subject>Membrane Proteins</subject><subject>Models, Biological</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>Synaptic Vesicles - physiology</subject><issn>0022-5193</issn><issn>1095-8541</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kDFv2zAQhYkiheu4XbMF4JRNKilKopgtMJKmgIEu7cxS5LGgIYkujzbif18JNrJ1Oty9dw93HyF3nJWcsfbrPveh5Eo1JWOV-EDWnKmm6Jqa35D1PKqKhivxidwi7hljqhbtiqyk5PNYrsnv7RkzhAkKzClMf-ghxaVHapBmGA-DyYDUx0RHGPtkJqD-iCFOj3SMDgak0VM8T-aQg6UnwGAHoPAW7TlHDPiZfPRmQPhyrRvy6-X55_a12P349n37tCusECoXnjVVq5qaVa1rwCvedVyCaZuegRPGykrWSvXSeM68kyBqUXsuaut601fSiQ15uOTOD_w9AmY9BrQwDPPF8YhayoqLqhOzsbwYbYqICbw-pDCadNac6QWpXpDqBalekM4L99fkYz-Ce7dfGc56d9FnGHAKkDTaAJMFFxLYrF0M_4v-B8ywh0Y</recordid><startdate>19950207</startdate><enddate>19950207</enddate><creator>Gundersen, Cameron B.</creator><creator>Mastrogiacomo, Alessandro</creator><creator>Umbach, Joy A.</creator><general>Elsevier Ltd</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></search><sort><creationdate>19950207</creationdate><title>Cysteine-string proteins as templates for membrane fusion: models of synaptic vesicle exocytosis</title><author>Gundersen, Cameron B. ; Mastrogiacomo, Alessandro ; Umbach, Joy A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c339t-f0526954026d5ef918817ea65b0ed3ac727499b7af10fd7e3434f134cdbab27d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Animals</topic><topic>Exocytosis - physiology</topic><topic>HSP40 Heat-Shock Proteins</topic><topic>Membrane Fusion</topic><topic>Membrane Proteins</topic><topic>Models, Biological</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>Synaptic Vesicles - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gundersen, Cameron B.</creatorcontrib><creatorcontrib>Mastrogiacomo, Alessandro</creatorcontrib><creatorcontrib>Umbach, Joy A.</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><jtitle>Journal of theoretical biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gundersen, Cameron B.</au><au>Mastrogiacomo, Alessandro</au><au>Umbach, Joy A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cysteine-string proteins as templates for membrane fusion: models of synaptic vesicle exocytosis</atitle><jtitle>Journal of theoretical biology</jtitle><addtitle>J Theor Biol</addtitle><date>1995-02-07</date><risdate>1995</risdate><volume>172</volume><issue>3</issue><spage>269</spage><epage>277</epage><pages>269-277</pages><issn>0022-5193</issn><eissn>1095-8541</eissn><abstract>Cysteine-string proteins are relatively small, cysteine-rich components of synaptic vesicle membranes. 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subjects | Animals Exocytosis - physiology HSP40 Heat-Shock Proteins Membrane Fusion Membrane Proteins Models, Biological Nerve Tissue Proteins - metabolism Synaptic Vesicles - physiology |
title | Cysteine-string proteins as templates for membrane fusion: models of synaptic vesicle exocytosis |
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