Dynamin and its partners: a progress report
Dynamin's role in clathrin-mediated endocytosis is now well established. Here we review new evidence from the past two years for the function of dynamin and related GTPases in other intracellular trafficking events. We then summarize current information on the domain structure and function of t...
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Veröffentlicht in: | Current opinion in cell biology 1998-08, Vol.10 (4), p.504-512 |
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creator | Schmid, Sandra L McNiven, Mark A Camilli, Pietro De |
description | Dynamin's role in clathrin-mediated endocytosis is now well established. Here we review new evidence from the past two years for the function of dynamin and related GTPases in other intracellular trafficking events. We then summarize current information on the domain structure and function of this multidomain GTPase. Finally, we describe dynamin partners and their function in the context of clathrin-mediated endocytosis. |
doi_str_mv | 10.1016/S0955-0674(98)80066-5 |
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Here we review new evidence from the past two years for the function of dynamin and related GTPases in other intracellular trafficking events. We then summarize current information on the domain structure and function of this multidomain GTPase. 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Here we review new evidence from the past two years for the function of dynamin and related GTPases in other intracellular trafficking events. We then summarize current information on the domain structure and function of this multidomain GTPase. Finally, we describe dynamin partners and their function in the context of clathrin-mediated endocytosis.</description><subject>Alternative Splicing</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Dynamins</subject><subject>Endocytosis</subject><subject>GTP Phosphohydrolases - metabolism</subject><subject>GTP Phosphohydrolases - physiology</subject><subject>Hydrogen-Ion Concentration</subject><subject>Intracellular Membranes - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Phosphatidylinositols - metabolism</subject><subject>Proteins - metabolism</subject><issn>0955-0674</issn><issn>1879-0410</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1LAzEQhoMotVZ_QmFPosjqZDefXkTqJxQ8qOeQZicS6e7WZCv037v9oFdPc5jnnZd5CBlTuKZAxc07aM5zEJJdaHWpAITI-QEZUiV1DozCIRnukWNyktI39BAUekAGWlKtZDEkVw-rxtahyWxTZaFL2cLGrsGYbjObLWL7FTGlLOKijd0pOfJ2nvBsN0fk8-nxY_KST9-eXyf309yVArrclt7NqPKcs0KhtJSjc5XTrGBWVNaB9LRkQlvqKaCTzitrkSnuhWeOQjki59u7ff_PElNn6pAczue2wXaZjCyVAk6LHuRb0MU2pYjeLGKobVwZCmYtyWwkmbUBo5XZSDK8z413BctZjdU-tbPS7--2e-y__A0YTXIBG4dViOg6U7Xhn4Y_Cwl2QA</recordid><startdate>19980801</startdate><enddate>19980801</enddate><creator>Schmid, Sandra L</creator><creator>McNiven, Mark A</creator><creator>Camilli, Pietro De</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>19980801</creationdate><title>Dynamin and its partners: a progress report</title><author>Schmid, Sandra L ; McNiven, Mark A ; Camilli, Pietro De</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c360t-a3fcb18f55428e7a15eccdc9424a6dac07f13469a1f10ec7cf8aae485f6f4c103</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Alternative Splicing</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Binding Sites</topic><topic>Dynamins</topic><topic>Endocytosis</topic><topic>GTP Phosphohydrolases - metabolism</topic><topic>GTP Phosphohydrolases - physiology</topic><topic>Hydrogen-Ion Concentration</topic><topic>Intracellular Membranes - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Phosphatidylinositols - metabolism</topic><topic>Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schmid, Sandra L</creatorcontrib><creatorcontrib>McNiven, Mark A</creatorcontrib><creatorcontrib>Camilli, Pietro De</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>Current opinion in cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schmid, Sandra L</au><au>McNiven, Mark A</au><au>Camilli, Pietro De</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Dynamin and its partners: a progress report</atitle><jtitle>Current opinion in cell biology</jtitle><addtitle>Curr Opin Cell Biol</addtitle><date>1998-08-01</date><risdate>1998</risdate><volume>10</volume><issue>4</issue><spage>504</spage><epage>512</epage><pages>504-512</pages><issn>0955-0674</issn><eissn>1879-0410</eissn><abstract>Dynamin's role in clathrin-mediated endocytosis is now well established. 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subjects | Alternative Splicing Amino Acid Sequence Animals Binding Sites Dynamins Endocytosis GTP Phosphohydrolases - metabolism GTP Phosphohydrolases - physiology Hydrogen-Ion Concentration Intracellular Membranes - metabolism Molecular Sequence Data Phosphatidylinositols - metabolism Proteins - metabolism |
title | Dynamin and its partners: a progress report |
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