The Presynaptic Particle Web: Ultrastructure, Composition, Dissolution, and Reconstitution
We report the purification of a presynaptic “particle web” consisting of ∼50 nm pyramidally shaped particles interconnected by ∼100 nm spaced fibrils. This is the “presynaptic grid” described in early EM studies. It is completely soluble above pH 8, but reconstitutes after dialysis against pH 6. Int...
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| Veröffentlicht in: | Neuron (Cambridge, Mass.) Mass.), 2001-10, Vol.32 (1), p.63-77 |
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| creator | Phillips, Greg R Huang, Jeffrey K Wang, Yun Tanaka, Hidekazu Shapiro, Lawrence Zhang, Wandong Shan, Wei-Song Arndt, Kirsten Frank, Marcus Gordon, Ronald E Gawinowicz, Mary Ann Zhao, Yingming Colman, David R |
| description | We report the purification of a presynaptic “particle web” consisting of ∼50 nm pyramidally shaped particles interconnected by ∼100 nm spaced fibrils. This is the “presynaptic grid” described in early EM studies. It is completely soluble above pH 8, but reconstitutes after dialysis against pH 6. Interestingly, reconstituted particles orient and bind PSDs asymmetrically. Mass spectrometry of purified web components reveals major proteins involved in the exocytosis of synaptic vesicles and in membrane retrieval. Our data support the idea that the CNS synaptic junction is organized by transmembrane adhesion molecules interlinked in the synaptic cleft, connected via their intracytoplasmic domains to the presynaptic web on one side and to the postsynaptic density on the other. The CNS synaptic junction may therefore be conceptualized as a complicated macromolecular scaffold that isostatically bridges two closely aligned plasma membranes. |
| doi_str_mv | 10.1016/S0896-6273(01)00450-0 |
| format | Article |
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This is the “presynaptic grid” described in early EM studies. It is completely soluble above pH 8, but reconstitutes after dialysis against pH 6. Interestingly, reconstituted particles orient and bind PSDs asymmetrically. Mass spectrometry of purified web components reveals major proteins involved in the exocytosis of synaptic vesicles and in membrane retrieval. Our data support the idea that the CNS synaptic junction is organized by transmembrane adhesion molecules interlinked in the synaptic cleft, connected via their intracytoplasmic domains to the presynaptic web on one side and to the postsynaptic density on the other. The CNS synaptic junction may therefore be conceptualized as a complicated macromolecular scaffold that isostatically bridges two closely aligned plasma membranes.</description><identifier>ISSN: 0896-6273</identifier><identifier>EISSN: 1097-4199</identifier><identifier>DOI: 10.1016/S0896-6273(01)00450-0</identifier><identifier>PMID: 11604139</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Antibodies ; Cadherins - analysis ; Cadherins - immunology ; Cell Membrane - chemistry ; Cell Membrane - metabolism ; Cell Membrane - ultrastructure ; Clathrin - analysis ; Clathrin - immunology ; Clathrin Heavy Chains ; Dynamins ; GTP Phosphohydrolases - analysis ; GTP Phosphohydrolases - immunology ; HSP70 Heat-Shock Proteins - analysis ; HSP70 Heat-Shock Proteins - immunology ; Male ; Membrane Proteins - analysis ; Membrane Proteins - immunology ; Microscopy, Immunoelectron ; Munc18 Proteins ; Myosin Heavy Chains - analysis ; Myosin Heavy Chains - immunology ; Nerve Tissue Proteins - analysis ; Nerve Tissue Proteins - immunology ; Neurofilament Proteins - analysis ; Neurofilament Proteins - immunology ; Presynaptic Terminals - chemistry ; Presynaptic Terminals - metabolism ; Presynaptic Terminals - ultrastructure ; Qa-SNARE Proteins ; Rabbits ; Rats ; Spectrin - analysis ; Spectrin - immunology ; Synapsins - analysis ; Synapsins - immunology ; Synaptic Vesicles - chemistry ; Synaptic Vesicles - metabolism ; Synaptic Vesicles - ultrastructure ; Synaptosomal-Associated Protein 25 ; Vesicular Transport Proteins</subject><ispartof>Neuron (Cambridge, Mass.), 2001-10, Vol.32 (1), p.63-77</ispartof><rights>2001 Cell Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c348t-72f78031988987d7a8168b20a0a7e631a5eb4e71f08b06d1395d924cc31870e83</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0896627301004500$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11604139$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Phillips, Greg R</creatorcontrib><creatorcontrib>Huang, Jeffrey K</creatorcontrib><creatorcontrib>Wang, Yun</creatorcontrib><creatorcontrib>Tanaka, Hidekazu</creatorcontrib><creatorcontrib>Shapiro, Lawrence</creatorcontrib><creatorcontrib>Zhang, Wandong</creatorcontrib><creatorcontrib>Shan, Wei-Song</creatorcontrib><creatorcontrib>Arndt, Kirsten</creatorcontrib><creatorcontrib>Frank, Marcus</creatorcontrib><creatorcontrib>Gordon, Ronald E</creatorcontrib><creatorcontrib>Gawinowicz, Mary Ann</creatorcontrib><creatorcontrib>Zhao, Yingming</creatorcontrib><creatorcontrib>Colman, David R</creatorcontrib><title>The Presynaptic Particle Web: Ultrastructure, Composition, Dissolution, and Reconstitution</title><title>Neuron (Cambridge, Mass.)</title><addtitle>Neuron</addtitle><description>We report the purification of a presynaptic “particle web” consisting of ∼50 nm pyramidally shaped particles interconnected by ∼100 nm spaced fibrils. 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The CNS synaptic junction may therefore be conceptualized as a complicated macromolecular scaffold that isostatically bridges two closely aligned plasma membranes.</description><subject>Animals</subject><subject>Antibodies</subject><subject>Cadherins - analysis</subject><subject>Cadherins - immunology</subject><subject>Cell Membrane - chemistry</subject><subject>Cell Membrane - metabolism</subject><subject>Cell Membrane - ultrastructure</subject><subject>Clathrin - analysis</subject><subject>Clathrin - immunology</subject><subject>Clathrin Heavy Chains</subject><subject>Dynamins</subject><subject>GTP Phosphohydrolases - analysis</subject><subject>GTP Phosphohydrolases - immunology</subject><subject>HSP70 Heat-Shock Proteins - analysis</subject><subject>HSP70 Heat-Shock Proteins - immunology</subject><subject>Male</subject><subject>Membrane Proteins - analysis</subject><subject>Membrane Proteins - immunology</subject><subject>Microscopy, Immunoelectron</subject><subject>Munc18 Proteins</subject><subject>Myosin Heavy Chains - analysis</subject><subject>Myosin Heavy Chains - immunology</subject><subject>Nerve Tissue Proteins - analysis</subject><subject>Nerve Tissue Proteins - immunology</subject><subject>Neurofilament Proteins - analysis</subject><subject>Neurofilament Proteins - immunology</subject><subject>Presynaptic Terminals - chemistry</subject><subject>Presynaptic Terminals - metabolism</subject><subject>Presynaptic Terminals - ultrastructure</subject><subject>Qa-SNARE Proteins</subject><subject>Rabbits</subject><subject>Rats</subject><subject>Spectrin - analysis</subject><subject>Spectrin - immunology</subject><subject>Synapsins - analysis</subject><subject>Synapsins - immunology</subject><subject>Synaptic Vesicles - chemistry</subject><subject>Synaptic Vesicles - metabolism</subject><subject>Synaptic Vesicles - ultrastructure</subject><subject>Synaptosomal-Associated Protein 25</subject><subject>Vesicular Transport Proteins</subject><issn>0896-6273</issn><issn>1097-4199</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtLAzEQgIMotj5-grInUXB1Zl9JvIjUJwgWHwheQjY7xch2tyZZof_eta1encsww8cwMx9jewgnCFicPoGQRVwkPD0EPALIcohhjQ0RJI8zlHKdDf-QAdvy_gMAs1ziJhsgFpBhKofs7fmdorEjP2_0LFgTjbXrU03RK5Vn0UsdnPbBdSZ0jo6jUTudtd4G2zbH0aX1vq27ZaGbKnok0zY-2LDo7bCNia497a7yNnu5vnoe3cb3Dzd3o4v72KSZCDFPJlxAilIIKXjFtcBClAlo0JyKFHVOZUYcJyBKKKp-67ySSWZMioIDiXSbHSznzlz72ZEPamq9obrWDbWdVzxJoOjjXxBFAkkuZA_ur8CunFKlZs5OtZur37f1wPkSoP6uL0tOeWOpMVRZRyaoqrUKQf2IUgtR6seCAlQLUQrSbybHg5E</recordid><startdate>20011011</startdate><enddate>20011011</enddate><creator>Phillips, Greg R</creator><creator>Huang, Jeffrey K</creator><creator>Wang, Yun</creator><creator>Tanaka, Hidekazu</creator><creator>Shapiro, Lawrence</creator><creator>Zhang, Wandong</creator><creator>Shan, Wei-Song</creator><creator>Arndt, Kirsten</creator><creator>Frank, Marcus</creator><creator>Gordon, Ronald E</creator><creator>Gawinowicz, Mary Ann</creator><creator>Zhao, Yingming</creator><creator>Colman, David R</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7TK</scope><scope>7X8</scope></search><sort><creationdate>20011011</creationdate><title>The Presynaptic Particle Web: Ultrastructure, Composition, Dissolution, and Reconstitution</title><author>Phillips, Greg R ; Huang, Jeffrey K ; Wang, Yun ; Tanaka, Hidekazu ; Shapiro, Lawrence ; Zhang, Wandong ; Shan, Wei-Song ; Arndt, Kirsten ; Frank, Marcus ; Gordon, Ronald E ; Gawinowicz, Mary Ann ; Zhao, Yingming ; Colman, David R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c348t-72f78031988987d7a8168b20a0a7e631a5eb4e71f08b06d1395d924cc31870e83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Animals</topic><topic>Antibodies</topic><topic>Cadherins - analysis</topic><topic>Cadherins - immunology</topic><topic>Cell Membrane - chemistry</topic><topic>Cell Membrane - metabolism</topic><topic>Cell Membrane - ultrastructure</topic><topic>Clathrin - analysis</topic><topic>Clathrin - immunology</topic><topic>Clathrin Heavy Chains</topic><topic>Dynamins</topic><topic>GTP Phosphohydrolases - analysis</topic><topic>GTP Phosphohydrolases - immunology</topic><topic>HSP70 Heat-Shock Proteins - analysis</topic><topic>HSP70 Heat-Shock Proteins - immunology</topic><topic>Male</topic><topic>Membrane Proteins - analysis</topic><topic>Membrane Proteins - immunology</topic><topic>Microscopy, Immunoelectron</topic><topic>Munc18 Proteins</topic><topic>Myosin Heavy Chains - analysis</topic><topic>Myosin Heavy Chains - immunology</topic><topic>Nerve Tissue Proteins - analysis</topic><topic>Nerve Tissue Proteins - immunology</topic><topic>Neurofilament Proteins - analysis</topic><topic>Neurofilament Proteins - immunology</topic><topic>Presynaptic Terminals - chemistry</topic><topic>Presynaptic Terminals - metabolism</topic><topic>Presynaptic Terminals - ultrastructure</topic><topic>Qa-SNARE Proteins</topic><topic>Rabbits</topic><topic>Rats</topic><topic>Spectrin - analysis</topic><topic>Spectrin - immunology</topic><topic>Synapsins - analysis</topic><topic>Synapsins - immunology</topic><topic>Synaptic Vesicles - chemistry</topic><topic>Synaptic Vesicles - metabolism</topic><topic>Synaptic Vesicles - ultrastructure</topic><topic>Synaptosomal-Associated Protein 25</topic><topic>Vesicular Transport Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Phillips, Greg R</creatorcontrib><creatorcontrib>Huang, Jeffrey K</creatorcontrib><creatorcontrib>Wang, Yun</creatorcontrib><creatorcontrib>Tanaka, Hidekazu</creatorcontrib><creatorcontrib>Shapiro, Lawrence</creatorcontrib><creatorcontrib>Zhang, Wandong</creatorcontrib><creatorcontrib>Shan, Wei-Song</creatorcontrib><creatorcontrib>Arndt, Kirsten</creatorcontrib><creatorcontrib>Frank, Marcus</creatorcontrib><creatorcontrib>Gordon, Ronald E</creatorcontrib><creatorcontrib>Gawinowicz, Mary Ann</creatorcontrib><creatorcontrib>Zhao, Yingming</creatorcontrib><creatorcontrib>Colman, David R</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Neurosciences Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Neuron (Cambridge, Mass.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Phillips, Greg R</au><au>Huang, Jeffrey K</au><au>Wang, Yun</au><au>Tanaka, Hidekazu</au><au>Shapiro, Lawrence</au><au>Zhang, Wandong</au><au>Shan, Wei-Song</au><au>Arndt, Kirsten</au><au>Frank, Marcus</au><au>Gordon, Ronald E</au><au>Gawinowicz, Mary Ann</au><au>Zhao, Yingming</au><au>Colman, David R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Presynaptic Particle Web: Ultrastructure, Composition, Dissolution, and Reconstitution</atitle><jtitle>Neuron (Cambridge, Mass.)</jtitle><addtitle>Neuron</addtitle><date>2001-10-11</date><risdate>2001</risdate><volume>32</volume><issue>1</issue><spage>63</spage><epage>77</epage><pages>63-77</pages><issn>0896-6273</issn><eissn>1097-4199</eissn><abstract>We report the purification of a presynaptic “particle web” consisting of ∼50 nm pyramidally shaped particles interconnected by ∼100 nm spaced fibrils. This is the “presynaptic grid” described in early EM studies. It is completely soluble above pH 8, but reconstitutes after dialysis against pH 6. Interestingly, reconstituted particles orient and bind PSDs asymmetrically. Mass spectrometry of purified web components reveals major proteins involved in the exocytosis of synaptic vesicles and in membrane retrieval. Our data support the idea that the CNS synaptic junction is organized by transmembrane adhesion molecules interlinked in the synaptic cleft, connected via their intracytoplasmic domains to the presynaptic web on one side and to the postsynaptic density on the other. The CNS synaptic junction may therefore be conceptualized as a complicated macromolecular scaffold that isostatically bridges two closely aligned plasma membranes.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>11604139</pmid><doi>10.1016/S0896-6273(01)00450-0</doi><tpages>15</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Antibodies Cadherins - analysis Cadherins - immunology Cell Membrane - chemistry Cell Membrane - metabolism Cell Membrane - ultrastructure Clathrin - analysis Clathrin - immunology Clathrin Heavy Chains Dynamins GTP Phosphohydrolases - analysis GTP Phosphohydrolases - immunology HSP70 Heat-Shock Proteins - analysis HSP70 Heat-Shock Proteins - immunology Male Membrane Proteins - analysis Membrane Proteins - immunology Microscopy, Immunoelectron Munc18 Proteins Myosin Heavy Chains - analysis Myosin Heavy Chains - immunology Nerve Tissue Proteins - analysis Nerve Tissue Proteins - immunology Neurofilament Proteins - analysis Neurofilament Proteins - immunology Presynaptic Terminals - chemistry Presynaptic Terminals - metabolism Presynaptic Terminals - ultrastructure Qa-SNARE Proteins Rabbits Rats Spectrin - analysis Spectrin - immunology Synapsins - analysis Synapsins - immunology Synaptic Vesicles - chemistry Synaptic Vesicles - metabolism Synaptic Vesicles - ultrastructure Synaptosomal-Associated Protein 25 Vesicular Transport Proteins |
| title | The Presynaptic Particle Web: Ultrastructure, Composition, Dissolution, and Reconstitution |
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