Syntaxin1a variants lacking an N-peptide or bearing the LE mutation bind to Munc18a in a closed conformation
In neurons, soluble N -ethylmaleimide–sensitive factor attachment receptor (SNARE) proteins drive the fusion of synaptic vesicles to the plasma membrane through the formation of a four-helix SNARE complex. Members of the Sec1/Munc18 protein family regulate membrane fusion through interactions with t...
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Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2013-07, Vol.110 (31), p.12637-12642 |
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creator | Colbert, Karen N. Hattendorf, Douglas A. Weiss, Thomas M. Burkhardt, Pawel Fasshauer, Dirk Weis, William I. |
description | In neurons, soluble N -ethylmaleimide–sensitive factor attachment receptor (SNARE) proteins drive the fusion of synaptic vesicles to the plasma membrane through the formation of a four-helix SNARE complex. Members of the Sec1/Munc18 protein family regulate membrane fusion through interactions with the syntaxin family of SNARE proteins. The neuronal protein Munc18a interacts with a closed conformation of the SNARE protein syntaxin1a (Syx1a) and with an assembled SNARE complex containing Syx1a in an open conformation. The N-peptide of Syx1a (amino acids 1–24) has been implicated in the transition of Munc18a-bound Syx1a to Munc18a-bound SNARE complex, but the underlying mechanism is not understood. Here we report the X-ray crystal structures of Munc18a bound to Syx1a with and without its native N-peptide (Syx1aΔN), along with small-angle X-ray scattering (SAXS) data for Munc18a bound to Syx1a, Syx1aΔN, and Syx1a L165A/E166A (LE), a mutation thought to render Syx1a in a constitutively open conformation. We show that all three complexes adopt the same global structure, in which Munc18a binds a closed conformation of Syx1a. We also identify a possible structural connection between the Syx1a N-peptide and SNARE domain that might be important for the transition of closed-to-open Syx1a in SNARE complex assembly. Although the role of the N-peptide in Munc18a-mediated SNARE complex assembly remains unclear, our results demonstrate that the N-peptide and LE mutation have no effect on the global conformation of the Munc18a–Syx1a complex. |
doi_str_mv | 10.1073/pnas.1303753110 |
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Members of the Sec1/Munc18 protein family regulate membrane fusion through interactions with the syntaxin family of SNARE proteins. The neuronal protein Munc18a interacts with a closed conformation of the SNARE protein syntaxin1a (Syx1a) and with an assembled SNARE complex containing Syx1a in an open conformation. The N-peptide of Syx1a (amino acids 1–24) has been implicated in the transition of Munc18a-bound Syx1a to Munc18a-bound SNARE complex, but the underlying mechanism is not understood. Here we report the X-ray crystal structures of Munc18a bound to Syx1a with and without its native N-peptide (Syx1aΔN), along with small-angle X-ray scattering (SAXS) data for Munc18a bound to Syx1a, Syx1aΔN, and Syx1a L165A/E166A (LE), a mutation thought to render Syx1a in a constitutively open conformation. We show that all three complexes adopt the same global structure, in which Munc18a binds a closed conformation of Syx1a. We also identify a possible structural connection between the Syx1a N-peptide and SNARE domain that might be important for the transition of closed-to-open Syx1a in SNARE complex assembly. Although the role of the N-peptide in Munc18a-mediated SNARE complex assembly remains unclear, our results demonstrate that the N-peptide and LE mutation have no effect on the global conformation of the Munc18a–Syx1a complex.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.1303753110</identifier><identifier>PMID: 23858467</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Amino Acid Substitution ; Amino acids ; BASIC BIOLOGICAL SCIENCES ; Biological Sciences ; Cell membranes ; Crystal structure ; Electron density ; Evolutionary linguistics ; Exocytosis ; Humans ; Hydrogen bonds ; membrane fusion ; membrane trafficking ; Munc18 Proteins - chemistry ; Munc18 Proteins - genetics ; Munc18 Proteins - metabolism ; Mutation ; Neurons ; Peptides ; plasma membrane ; Protein Binding ; protein crystallography ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Proteins ; Sequence Deletion ; SM proteins ; SNARE proteins ; SNARE Proteins - chemistry ; SNARE Proteins - genetics ; SNARE Proteins - metabolism ; synaptic vesicles ; Syntaxin 1 - chemistry ; Syntaxin 1 - genetics ; Syntaxin 1 - metabolism ; X-radiation ; X-ray diffraction</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2013-07, Vol.110 (31), p.12637-12642</ispartof><rights>copyright © 1993-2008 National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Jul 30, 2013</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c552t-cca1e327187555b0d008830f6cb302b7512ec89ddd576b67c08dd31878f423833</citedby><cites>FETCH-LOGICAL-c552t-cca1e327187555b0d008830f6cb302b7512ec89ddd576b67c08dd31878f423833</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/110/31.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/42712659$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/42712659$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23858467$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/servlets/purl/1132335$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Colbert, Karen N.</creatorcontrib><creatorcontrib>Hattendorf, Douglas A.</creatorcontrib><creatorcontrib>Weiss, Thomas M.</creatorcontrib><creatorcontrib>Burkhardt, Pawel</creatorcontrib><creatorcontrib>Fasshauer, Dirk</creatorcontrib><creatorcontrib>Weis, William I.</creatorcontrib><creatorcontrib>SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States)</creatorcontrib><title>Syntaxin1a variants lacking an N-peptide or bearing the LE mutation bind to Munc18a in a closed conformation</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>In neurons, soluble N -ethylmaleimide–sensitive factor attachment receptor (SNARE) proteins drive the fusion of synaptic vesicles to the plasma membrane through the formation of a four-helix SNARE complex. Members of the Sec1/Munc18 protein family regulate membrane fusion through interactions with the syntaxin family of SNARE proteins. The neuronal protein Munc18a interacts with a closed conformation of the SNARE protein syntaxin1a (Syx1a) and with an assembled SNARE complex containing Syx1a in an open conformation. The N-peptide of Syx1a (amino acids 1–24) has been implicated in the transition of Munc18a-bound Syx1a to Munc18a-bound SNARE complex, but the underlying mechanism is not understood. Here we report the X-ray crystal structures of Munc18a bound to Syx1a with and without its native N-peptide (Syx1aΔN), along with small-angle X-ray scattering (SAXS) data for Munc18a bound to Syx1a, Syx1aΔN, and Syx1a L165A/E166A (LE), a mutation thought to render Syx1a in a constitutively open conformation. We show that all three complexes adopt the same global structure, in which Munc18a binds a closed conformation of Syx1a. We also identify a possible structural connection between the Syx1a N-peptide and SNARE domain that might be important for the transition of closed-to-open Syx1a in SNARE complex assembly. Although the role of the N-peptide in Munc18a-mediated SNARE complex assembly remains unclear, our results demonstrate that the N-peptide and LE mutation have no effect on the global conformation of the Munc18a–Syx1a complex.</description><subject>Amino Acid Substitution</subject><subject>Amino acids</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>Biological Sciences</subject><subject>Cell membranes</subject><subject>Crystal structure</subject><subject>Electron density</subject><subject>Evolutionary linguistics</subject><subject>Exocytosis</subject><subject>Humans</subject><subject>Hydrogen bonds</subject><subject>membrane fusion</subject><subject>membrane trafficking</subject><subject>Munc18 Proteins - chemistry</subject><subject>Munc18 Proteins - genetics</subject><subject>Munc18 Proteins - metabolism</subject><subject>Mutation</subject><subject>Neurons</subject><subject>Peptides</subject><subject>plasma membrane</subject><subject>Protein Binding</subject><subject>protein crystallography</subject><subject>Protein Structure, Quaternary</subject><subject>Protein Structure, Secondary</subject><subject>Proteins</subject><subject>Sequence Deletion</subject><subject>SM proteins</subject><subject>SNARE proteins</subject><subject>SNARE Proteins - chemistry</subject><subject>SNARE Proteins - genetics</subject><subject>SNARE Proteins - metabolism</subject><subject>synaptic vesicles</subject><subject>Syntaxin 1 - chemistry</subject><subject>Syntaxin 1 - genetics</subject><subject>Syntaxin 1 - metabolism</subject><subject>X-radiation</subject><subject>X-ray diffraction</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpd0c9vFCEUB_CJ0dhaPXtSiV68TPvgDQxzMTFN_ZGseqg9E4ZhdllnYQWmsf-9rLuuP04kvA9feLyqekrhnEKLF1uv0zlFwJYjpXCvOqXQ0Vo0HdyvTgFYW8uGNSfVo5TWANBxCQ-rE4aSy0a0p9V0feez_uE81eRWR6d9TmTS5pvzS6I9-Vxv7Ta7wZIQSW-LKPt5ZcniimzmrLMLnvTODyQH8mn2hkpNnCeamCkkOxAT_Bji5hd8XD0Y9ZTsk8N6Vt28u_p6-aFefHn_8fLtojacs1wbo6lF1lLZcs57GACkRBiF6RFY33LKrJHdMAy8Fb1oDchhwKLl2JTOEM-qN_vc7dxv7GCsz1FPahvdRsc7FbRT_1a8W6lluFXYIuuwKQEv9wEhZaeScdmaVenEW5MVpcgQeUGvD7fE8H22KauNS8ZOk_Y2zElRCVho17SFvvqPrsMcffkDRRsqmeg4iKIu9srEkFK04_HFFNRu3Go3bvVn3OXE878bPfrf8y2AHMDu5DGu5CFVlAnckWd7sk45xKNpyv8zwbtSf7GvjzoovYwuqZtrBlQAUBSCIv4E9tPCEg</recordid><startdate>20130730</startdate><enddate>20130730</enddate><creator>Colbert, Karen N.</creator><creator>Hattendorf, Douglas A.</creator><creator>Weiss, Thomas M.</creator><creator>Burkhardt, Pawel</creator><creator>Fasshauer, Dirk</creator><creator>Weis, William I.</creator><general>National Academy of Sciences</general><general>National Acad Sciences</general><general>National Academy of Sciences, Washington, DC (United States)</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</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>7S9</scope><scope>L.6</scope><scope>OIOZB</scope><scope>OTOTI</scope><scope>5PM</scope></search><sort><creationdate>20130730</creationdate><title>Syntaxin1a variants lacking an N-peptide or bearing the LE mutation bind to Munc18a in a closed conformation</title><author>Colbert, Karen N. ; Hattendorf, Douglas A. ; Weiss, Thomas M. ; Burkhardt, Pawel ; Fasshauer, Dirk ; Weis, William I.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c552t-cca1e327187555b0d008830f6cb302b7512ec89ddd576b67c08dd31878f423833</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Amino Acid Substitution</topic><topic>Amino acids</topic><topic>BASIC BIOLOGICAL SCIENCES</topic><topic>Biological Sciences</topic><topic>Cell membranes</topic><topic>Crystal structure</topic><topic>Electron density</topic><topic>Evolutionary linguistics</topic><topic>Exocytosis</topic><topic>Humans</topic><topic>Hydrogen bonds</topic><topic>membrane fusion</topic><topic>membrane trafficking</topic><topic>Munc18 Proteins - chemistry</topic><topic>Munc18 Proteins - genetics</topic><topic>Munc18 Proteins - metabolism</topic><topic>Mutation</topic><topic>Neurons</topic><topic>Peptides</topic><topic>plasma membrane</topic><topic>Protein Binding</topic><topic>protein crystallography</topic><topic>Protein Structure, Quaternary</topic><topic>Protein Structure, Secondary</topic><topic>Proteins</topic><topic>Sequence Deletion</topic><topic>SM proteins</topic><topic>SNARE proteins</topic><topic>SNARE Proteins - chemistry</topic><topic>SNARE Proteins - genetics</topic><topic>SNARE Proteins - metabolism</topic><topic>synaptic vesicles</topic><topic>Syntaxin 1 - chemistry</topic><topic>Syntaxin 1 - genetics</topic><topic>Syntaxin 1 - metabolism</topic><topic>X-radiation</topic><topic>X-ray diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Colbert, Karen N.</creatorcontrib><creatorcontrib>Hattendorf, Douglas A.</creatorcontrib><creatorcontrib>Weiss, Thomas M.</creatorcontrib><creatorcontrib>Burkhardt, Pawel</creatorcontrib><creatorcontrib>Fasshauer, Dirk</creatorcontrib><creatorcontrib>Weis, William I.</creatorcontrib><creatorcontrib>SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States)</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><collection>OSTI.GOV - Hybrid</collection><collection>OSTI.GOV</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Colbert, Karen N.</au><au>Hattendorf, Douglas A.</au><au>Weiss, Thomas M.</au><au>Burkhardt, Pawel</au><au>Fasshauer, Dirk</au><au>Weis, William I.</au><aucorp>SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Syntaxin1a variants lacking an N-peptide or bearing the LE mutation bind to Munc18a in a closed conformation</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2013-07-30</date><risdate>2013</risdate><volume>110</volume><issue>31</issue><spage>12637</spage><epage>12642</epage><pages>12637-12642</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>In neurons, soluble N -ethylmaleimide–sensitive factor attachment receptor (SNARE) proteins drive the fusion of synaptic vesicles to the plasma membrane through the formation of a four-helix SNARE complex. Members of the Sec1/Munc18 protein family regulate membrane fusion through interactions with the syntaxin family of SNARE proteins. The neuronal protein Munc18a interacts with a closed conformation of the SNARE protein syntaxin1a (Syx1a) and with an assembled SNARE complex containing Syx1a in an open conformation. The N-peptide of Syx1a (amino acids 1–24) has been implicated in the transition of Munc18a-bound Syx1a to Munc18a-bound SNARE complex, but the underlying mechanism is not understood. Here we report the X-ray crystal structures of Munc18a bound to Syx1a with and without its native N-peptide (Syx1aΔN), along with small-angle X-ray scattering (SAXS) data for Munc18a bound to Syx1a, Syx1aΔN, and Syx1a L165A/E166A (LE), a mutation thought to render Syx1a in a constitutively open conformation. We show that all three complexes adopt the same global structure, in which Munc18a binds a closed conformation of Syx1a. We also identify a possible structural connection between the Syx1a N-peptide and SNARE domain that might be important for the transition of closed-to-open Syx1a in SNARE complex assembly. Although the role of the N-peptide in Munc18a-mediated SNARE complex assembly remains unclear, our results demonstrate that the N-peptide and LE mutation have no effect on the global conformation of the Munc18a–Syx1a complex.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>23858467</pmid><doi>10.1073/pnas.1303753110</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Substitution Amino acids BASIC BIOLOGICAL SCIENCES Biological Sciences Cell membranes Crystal structure Electron density Evolutionary linguistics Exocytosis Humans Hydrogen bonds membrane fusion membrane trafficking Munc18 Proteins - chemistry Munc18 Proteins - genetics Munc18 Proteins - metabolism Mutation Neurons Peptides plasma membrane Protein Binding protein crystallography Protein Structure, Quaternary Protein Structure, Secondary Proteins Sequence Deletion SM proteins SNARE proteins SNARE Proteins - chemistry SNARE Proteins - genetics SNARE Proteins - metabolism synaptic vesicles Syntaxin 1 - chemistry Syntaxin 1 - genetics Syntaxin 1 - metabolism X-radiation X-ray diffraction |
title | Syntaxin1a variants lacking an N-peptide or bearing the LE mutation bind to Munc18a in a closed conformation |
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