Nectin: An Adhesion Molecule Involved in Formation of Synapses
The nectin-afadin system is a novel cell-cell adhesion system that organizes adherens junctions cooperatively with the cadherin-catenin system in epithelial cells. Nectin is an immunoglobulin-like adhesion molecule, and afadin is an actin filament-binding protein that connects nectin to the actin cy...
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| Veröffentlicht in: | The Journal of cell biology 2002-02, Vol.156 (3), p.555-565 |
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| creator | Mizoguchi, Akira Nakanishi, Hiroyuki Kimura, Kazushi Matsubara, Kaho Ozaki-Kuroda, Kumi Katata, Tatsuo Honda, Tomoyuki Kiyohara, Yoshimoto Heo, Kyun Higashi, Mikito Tsutsumi, Tomonari Sonoda, Satomi Ide, Chizuka Takai, Yoshimi |
| description | The nectin-afadin system is a novel cell-cell adhesion system that organizes adherens junctions cooperatively with the cadherin-catenin system in epithelial cells. Nectin is an immunoglobulin-like adhesion molecule, and afadin is an actin filament-binding protein that connects nectin to the actin cytoskeleton. Nectin has four isoforms (-1, -2, -3, and -4). Each nectin forms a homo-cis-dimer followed by formation of a homo-trans-dimer, but nectin-3 furthermore forms a hetero-trans-dimer with nectin-1 or -2, and the formation of each hetero-trans-dimer is stronger than that of each homo-trans-dimer. We show here that at the synapses between the mossy fiber terminals and dendrites of pyramidal cells in the CA3 area of adult mouse hippocampus, the nectin-afadin system colocalizes with the cadherin-catenin system, and nectin-1 and -3 asymmetrically localize at the pre- and postsynaptic sides of puncta adherentia junctions, respectively. During development, nectin-1 and -3 asymmetrically localize not only at puncta adherentia junctions but also at synaptic junctions. Inhibition of the nectin-based adhesion by an inhibitor of nectin-1 in cultured rat hippocampal neurons results in a decrease in synapse size and a concomitant increase in synapse number. These results indicate an important role of the nectin-afadin system in the formation of synapses. |
| doi_str_mv | 10.1083/jcb.200103113 |
| format | Article |
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Nectin is an immunoglobulin-like adhesion molecule, and afadin is an actin filament-binding protein that connects nectin to the actin cytoskeleton. Nectin has four isoforms (-1, -2, -3, and -4). Each nectin forms a homo-cis-dimer followed by formation of a homo-trans-dimer, but nectin-3 furthermore forms a hetero-trans-dimer with nectin-1 or -2, and the formation of each hetero-trans-dimer is stronger than that of each homo-trans-dimer. We show here that at the synapses between the mossy fiber terminals and dendrites of pyramidal cells in the CA3 area of adult mouse hippocampus, the nectin-afadin system colocalizes with the cadherin-catenin system, and nectin-1 and -3 asymmetrically localize at the pre- and postsynaptic sides of puncta adherentia junctions, respectively. During development, nectin-1 and -3 asymmetrically localize not only at puncta adherentia junctions but also at synaptic junctions. Inhibition of the nectin-based adhesion by an inhibitor of nectin-1 in cultured rat hippocampal neurons results in a decrease in synapse size and a concomitant increase in synapse number. These results indicate an important role of the nectin-afadin system in the formation of synapses.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.200103113</identifier><identifier>PMID: 11827984</identifier><language>eng</language><publisher>United States: Rockefeller University Press</publisher><subject>Adherens junctions ; Adherens Junctions - drug effects ; Adherens Junctions - metabolism ; Adherens Junctions - ultrastructure ; Animals ; Cadherins ; Cell Adhesion - drug effects ; Cell Adhesion - physiology ; Cell Adhesion Molecules - antagonists & inhibitors ; Cell Adhesion Molecules - metabolism ; Cell Differentiation - drug effects ; Cell Differentiation - physiology ; Dendrites ; Dendrites - metabolism ; Dendrites - ultrastructure ; Dose-Response Relationship, Drug ; Epithelial cells ; Fetus ; Hippocampus ; Immunohistochemistry ; Kinesin ; Microfilament Proteins - metabolism ; Microscopy ; Microscopy, Electron ; Mossy Fibers, Hippocampal - embryology ; Mossy Fibers, Hippocampal - metabolism ; Mossy Fibers, Hippocampal - ultrastructure ; Myosins ; Nectins ; Neurons ; Protein Structure, Tertiary - physiology ; Pyramidal cells ; Pyramidal Cells - metabolism ; Pyramidal Cells - ultrastructure ; Rats ; Receptors ; Synapses ; Synapses - drug effects ; Synapses - metabolism ; Synapses - ultrastructure ; Synaptic Membranes - metabolism ; Synaptic Membranes - ultrastructure ; Synaptophysin - pharmacology ; Viral Envelope Proteins - pharmacology</subject><ispartof>The Journal of cell biology, 2002-02, Vol.156 (3), p.555-565</ispartof><rights>Copyright 2002 The Rockefeller University Press</rights><rights>Copyright © 2002, The Rockefeller University Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11827984$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mizoguchi, Akira</creatorcontrib><creatorcontrib>Nakanishi, Hiroyuki</creatorcontrib><creatorcontrib>Kimura, Kazushi</creatorcontrib><creatorcontrib>Matsubara, Kaho</creatorcontrib><creatorcontrib>Ozaki-Kuroda, Kumi</creatorcontrib><creatorcontrib>Katata, Tatsuo</creatorcontrib><creatorcontrib>Honda, Tomoyuki</creatorcontrib><creatorcontrib>Kiyohara, Yoshimoto</creatorcontrib><creatorcontrib>Heo, Kyun</creatorcontrib><creatorcontrib>Higashi, Mikito</creatorcontrib><creatorcontrib>Tsutsumi, Tomonari</creatorcontrib><creatorcontrib>Sonoda, Satomi</creatorcontrib><creatorcontrib>Ide, Chizuka</creatorcontrib><creatorcontrib>Takai, Yoshimi</creatorcontrib><title>Nectin: An Adhesion Molecule Involved in Formation of Synapses</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>The nectin-afadin system is a novel cell-cell adhesion system that organizes adherens junctions cooperatively with the cadherin-catenin system in epithelial cells. Nectin is an immunoglobulin-like adhesion molecule, and afadin is an actin filament-binding protein that connects nectin to the actin cytoskeleton. Nectin has four isoforms (-1, -2, -3, and -4). Each nectin forms a homo-cis-dimer followed by formation of a homo-trans-dimer, but nectin-3 furthermore forms a hetero-trans-dimer with nectin-1 or -2, and the formation of each hetero-trans-dimer is stronger than that of each homo-trans-dimer. We show here that at the synapses between the mossy fiber terminals and dendrites of pyramidal cells in the CA3 area of adult mouse hippocampus, the nectin-afadin system colocalizes with the cadherin-catenin system, and nectin-1 and -3 asymmetrically localize at the pre- and postsynaptic sides of puncta adherentia junctions, respectively. During development, nectin-1 and -3 asymmetrically localize not only at puncta adherentia junctions but also at synaptic junctions. Inhibition of the nectin-based adhesion by an inhibitor of nectin-1 in cultured rat hippocampal neurons results in a decrease in synapse size and a concomitant increase in synapse number. These results indicate an important role of the nectin-afadin system in the formation of synapses.</description><subject>Adherens junctions</subject><subject>Adherens Junctions - drug effects</subject><subject>Adherens Junctions - metabolism</subject><subject>Adherens Junctions - ultrastructure</subject><subject>Animals</subject><subject>Cadherins</subject><subject>Cell Adhesion - drug effects</subject><subject>Cell Adhesion - physiology</subject><subject>Cell Adhesion Molecules - antagonists & inhibitors</subject><subject>Cell Adhesion Molecules - metabolism</subject><subject>Cell Differentiation - drug effects</subject><subject>Cell Differentiation - physiology</subject><subject>Dendrites</subject><subject>Dendrites - metabolism</subject><subject>Dendrites - ultrastructure</subject><subject>Dose-Response Relationship, Drug</subject><subject>Epithelial cells</subject><subject>Fetus</subject><subject>Hippocampus</subject><subject>Immunohistochemistry</subject><subject>Kinesin</subject><subject>Microfilament Proteins - metabolism</subject><subject>Microscopy</subject><subject>Microscopy, Electron</subject><subject>Mossy Fibers, Hippocampal - embryology</subject><subject>Mossy Fibers, Hippocampal - metabolism</subject><subject>Mossy Fibers, Hippocampal - ultrastructure</subject><subject>Myosins</subject><subject>Nectins</subject><subject>Neurons</subject><subject>Protein Structure, Tertiary - physiology</subject><subject>Pyramidal cells</subject><subject>Pyramidal Cells - metabolism</subject><subject>Pyramidal Cells - ultrastructure</subject><subject>Rats</subject><subject>Receptors</subject><subject>Synapses</subject><subject>Synapses - drug effects</subject><subject>Synapses - metabolism</subject><subject>Synapses - ultrastructure</subject><subject>Synaptic Membranes - metabolism</subject><subject>Synaptic Membranes - ultrastructure</subject><subject>Synaptophysin - pharmacology</subject><subject>Viral Envelope Proteins - pharmacology</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkDtPwzAURi0EoqUwsiGUiS3F1684DJWqikKlAgMwR47j0ESJXeKkUv89QS2viekO5-jo00XoHPAYsKTXpU7HBGPAFIAeoCFwhkMJDB-iIcYEwpgTPkAn3pcYYxYxeowGAJJEsWRDNHk0ui3sTTC1wTRbGV84Gzy4yuiuMsHCbly1MVlQ2GDumlq1n9jlwfPWqrU3_hQd5ary5mx_R-h1fvsyuw-XT3eL2XQZlhRYG1IepbGihDOIsMgFybDRPCOGKAWCQAqEiJwLSZRWGmJtuIy0TDloGVOu6QhNdt11l9Ym08a2jaqSdVPUqtkmThXJX2KLVfLmNgmBiFIS9YGrfaBx753xbVIXXpuqUta4zicRMIpjoP-KIKmIKRO9ePl70veWr9_2wsVOKH3rmh8uCJZ95QN0pIQa</recordid><startdate>20020204</startdate><enddate>20020204</enddate><creator>Mizoguchi, Akira</creator><creator>Nakanishi, Hiroyuki</creator><creator>Kimura, Kazushi</creator><creator>Matsubara, Kaho</creator><creator>Ozaki-Kuroda, Kumi</creator><creator>Katata, Tatsuo</creator><creator>Honda, Tomoyuki</creator><creator>Kiyohara, Yoshimoto</creator><creator>Heo, Kyun</creator><creator>Higashi, Mikito</creator><creator>Tsutsumi, Tomonari</creator><creator>Sonoda, Satomi</creator><creator>Ide, Chizuka</creator><creator>Takai, Yoshimi</creator><general>Rockefeller University Press</general><general>The Rockefeller University Press</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7TK</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20020204</creationdate><title>Nectin: An Adhesion Molecule Involved in Formation of Synapses</title><author>Mizoguchi, Akira ; Nakanishi, Hiroyuki ; Kimura, Kazushi ; Matsubara, Kaho ; Ozaki-Kuroda, Kumi ; Katata, Tatsuo ; Honda, Tomoyuki ; Kiyohara, Yoshimoto ; Heo, Kyun ; Higashi, Mikito ; Tsutsumi, Tomonari ; Sonoda, Satomi ; Ide, Chizuka ; Takai, Yoshimi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-j314t-357b9a32541706f62d0ec5d2e2aa1621b1226f5682acac19ce587c8b51c8935c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Adherens junctions</topic><topic>Adherens Junctions - drug effects</topic><topic>Adherens Junctions - metabolism</topic><topic>Adherens Junctions - ultrastructure</topic><topic>Animals</topic><topic>Cadherins</topic><topic>Cell Adhesion - drug effects</topic><topic>Cell Adhesion - physiology</topic><topic>Cell Adhesion Molecules - antagonists & inhibitors</topic><topic>Cell Adhesion Molecules - metabolism</topic><topic>Cell Differentiation - drug effects</topic><topic>Cell Differentiation - physiology</topic><topic>Dendrites</topic><topic>Dendrites - metabolism</topic><topic>Dendrites - ultrastructure</topic><topic>Dose-Response Relationship, Drug</topic><topic>Epithelial cells</topic><topic>Fetus</topic><topic>Hippocampus</topic><topic>Immunohistochemistry</topic><topic>Kinesin</topic><topic>Microfilament Proteins - metabolism</topic><topic>Microscopy</topic><topic>Microscopy, Electron</topic><topic>Mossy Fibers, Hippocampal - embryology</topic><topic>Mossy Fibers, Hippocampal - metabolism</topic><topic>Mossy Fibers, Hippocampal - ultrastructure</topic><topic>Myosins</topic><topic>Nectins</topic><topic>Neurons</topic><topic>Protein Structure, Tertiary - physiology</topic><topic>Pyramidal cells</topic><topic>Pyramidal Cells - metabolism</topic><topic>Pyramidal Cells - ultrastructure</topic><topic>Rats</topic><topic>Receptors</topic><topic>Synapses</topic><topic>Synapses - drug effects</topic><topic>Synapses - metabolism</topic><topic>Synapses - ultrastructure</topic><topic>Synaptic Membranes - metabolism</topic><topic>Synaptic Membranes - ultrastructure</topic><topic>Synaptophysin - pharmacology</topic><topic>Viral Envelope Proteins - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mizoguchi, Akira</creatorcontrib><creatorcontrib>Nakanishi, Hiroyuki</creatorcontrib><creatorcontrib>Kimura, Kazushi</creatorcontrib><creatorcontrib>Matsubara, Kaho</creatorcontrib><creatorcontrib>Ozaki-Kuroda, Kumi</creatorcontrib><creatorcontrib>Katata, Tatsuo</creatorcontrib><creatorcontrib>Honda, Tomoyuki</creatorcontrib><creatorcontrib>Kiyohara, Yoshimoto</creatorcontrib><creatorcontrib>Heo, Kyun</creatorcontrib><creatorcontrib>Higashi, Mikito</creatorcontrib><creatorcontrib>Tsutsumi, Tomonari</creatorcontrib><creatorcontrib>Sonoda, Satomi</creatorcontrib><creatorcontrib>Ide, Chizuka</creatorcontrib><creatorcontrib>Takai, Yoshimi</creatorcontrib><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><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mizoguchi, Akira</au><au>Nakanishi, Hiroyuki</au><au>Kimura, Kazushi</au><au>Matsubara, Kaho</au><au>Ozaki-Kuroda, Kumi</au><au>Katata, Tatsuo</au><au>Honda, Tomoyuki</au><au>Kiyohara, Yoshimoto</au><au>Heo, Kyun</au><au>Higashi, Mikito</au><au>Tsutsumi, Tomonari</au><au>Sonoda, Satomi</au><au>Ide, Chizuka</au><au>Takai, Yoshimi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Nectin: An Adhesion Molecule Involved in Formation of Synapses</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>2002-02-04</date><risdate>2002</risdate><volume>156</volume><issue>3</issue><spage>555</spage><epage>565</epage><pages>555-565</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><abstract>The nectin-afadin system is a novel cell-cell adhesion system that organizes adherens junctions cooperatively with the cadherin-catenin system in epithelial cells. Nectin is an immunoglobulin-like adhesion molecule, and afadin is an actin filament-binding protein that connects nectin to the actin cytoskeleton. Nectin has four isoforms (-1, -2, -3, and -4). Each nectin forms a homo-cis-dimer followed by formation of a homo-trans-dimer, but nectin-3 furthermore forms a hetero-trans-dimer with nectin-1 or -2, and the formation of each hetero-trans-dimer is stronger than that of each homo-trans-dimer. We show here that at the synapses between the mossy fiber terminals and dendrites of pyramidal cells in the CA3 area of adult mouse hippocampus, the nectin-afadin system colocalizes with the cadherin-catenin system, and nectin-1 and -3 asymmetrically localize at the pre- and postsynaptic sides of puncta adherentia junctions, respectively. During development, nectin-1 and -3 asymmetrically localize not only at puncta adherentia junctions but also at synaptic junctions. Inhibition of the nectin-based adhesion by an inhibitor of nectin-1 in cultured rat hippocampal neurons results in a decrease in synapse size and a concomitant increase in synapse number. These results indicate an important role of the nectin-afadin system in the formation of synapses.</abstract><cop>United States</cop><pub>Rockefeller University Press</pub><pmid>11827984</pmid><doi>10.1083/jcb.200103113</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adherens junctions Adherens Junctions - drug effects Adherens Junctions - metabolism Adherens Junctions - ultrastructure Animals Cadherins Cell Adhesion - drug effects Cell Adhesion - physiology Cell Adhesion Molecules - antagonists & inhibitors Cell Adhesion Molecules - metabolism Cell Differentiation - drug effects Cell Differentiation - physiology Dendrites Dendrites - metabolism Dendrites - ultrastructure Dose-Response Relationship, Drug Epithelial cells Fetus Hippocampus Immunohistochemistry Kinesin Microfilament Proteins - metabolism Microscopy Microscopy, Electron Mossy Fibers, Hippocampal - embryology Mossy Fibers, Hippocampal - metabolism Mossy Fibers, Hippocampal - ultrastructure Myosins Nectins Neurons Protein Structure, Tertiary - physiology Pyramidal cells Pyramidal Cells - metabolism Pyramidal Cells - ultrastructure Rats Receptors Synapses Synapses - drug effects Synapses - metabolism Synapses - ultrastructure Synaptic Membranes - metabolism Synaptic Membranes - ultrastructure Synaptophysin - pharmacology Viral Envelope Proteins - pharmacology |
| title | Nectin: An Adhesion Molecule Involved in Formation of Synapses |
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