ENTH/ANTH proteins and clathrin-mediated membrane budding
The epsin N-terminal homology (ENTH) domain is an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. Structural analyses and ligand-binding studies have shown that a set of proteins previously designated as harboring an ENTH domain...
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| Veröffentlicht in: | Journal of cell science 2004-01, Vol.117 (Pt 1), p.9-18 |
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| container_issue | Pt 1 |
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| container_title | Journal of cell science |
| container_volume | 117 |
| creator | Legendre-Guillemin, Valerie Wasiak, Sylwia Hussain, Natasha K Angers, Annie McPherson, Peter S |
| description | The epsin N-terminal homology (ENTH) domain is an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. Structural analyses and ligand-binding studies have shown that a set of proteins previously designated as harboring an ENTH domain in fact contain a highly similar, yet unique module referred to as an AP180 N-terminal homology (ANTH) domain. ENTH and ANTH (E/ANTH) domains bind both inositol phospholipids and proteins and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. E/ANTH-bearing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the trans-Golgi network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding. |
| doi_str_mv | 10.1242/jcs.00928 |
| format | Article |
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Structural analyses and ligand-binding studies have shown that a set of proteins previously designated as harboring an ENTH domain in fact contain a highly similar, yet unique module referred to as an AP180 N-terminal homology (ANTH) domain. ENTH and ANTH (E/ANTH) domains bind both inositol phospholipids and proteins and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. E/ANTH-bearing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the trans-Golgi network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding.</description><subject>Adaptor Proteins, Vesicular Transport</subject><subject>Animals</subject><subject>Carrier Proteins - metabolism</subject><subject>Clathrin - metabolism</subject><subject>Endocytosis - physiology</subject><subject>Golgi Apparatus - metabolism</subject><subject>Humans</subject><subject>Membrane Fusion - physiology</subject><subject>Membrane Lipids - metabolism</subject><subject>Models, Molecular</subject><subject>Monomeric Clathrin Assembly Proteins - metabolism</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>Neuropeptides - metabolism</subject><subject>Phosphatidylinositols - metabolism</subject><subject>Phosphoric Monoester Hydrolases - metabolism</subject><subject>Protein Binding</subject><subject>Protein Folding</subject><subject>Protein Structure, Tertiary</subject><subject>Vesicular Transport Proteins</subject><issn>0021-9533</issn><issn>1477-9137</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkD1PwzAQhi0EoqEw8AdQJiSGtOePxPZYVYUiVbCU2XIcG1Llo9jJwL-voZFY7oZ79Oq9B6F7DAtMGFkeTFgASCIuUIIZ55nElF-iBIDgTOaUztBNCAcA4ETyazTDrMg5KWSC5OZtv12u4kiPvh9s3YVUd1VqGj18-brLWlvVerBV2tq29LqzaTlWVd193qIrp5tg76Y9Rx_Pm_16m-3eX17Xq11mGM6HrHTGGDDaakKwoRIw8BxoKUQsCpYJG09ScAKOF1xgIA4YcdqJihWUcTpHj-fc2O97tGFQbR2MbZrYpR-D4jgv4rsygk9n0Pg-BG-dOvq61f5HYVC_nlT0pP48RfZhCh3L-OE_OYmhJ3zKYVg</recordid><startdate>20040101</startdate><enddate>20040101</enddate><creator>Legendre-Guillemin, Valerie</creator><creator>Wasiak, Sylwia</creator><creator>Hussain, Natasha K</creator><creator>Angers, Annie</creator><creator>McPherson, Peter S</creator><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>20040101</creationdate><title>ENTH/ANTH proteins and clathrin-mediated membrane budding</title><author>Legendre-Guillemin, Valerie ; Wasiak, Sylwia ; Hussain, Natasha K ; Angers, Annie ; McPherson, Peter S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c415t-bfccc0caea221c390107503b884770e48eaea98720f7678102f042faf8d463473</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Adaptor Proteins, Vesicular Transport</topic><topic>Animals</topic><topic>Carrier Proteins - metabolism</topic><topic>Clathrin - metabolism</topic><topic>Endocytosis - physiology</topic><topic>Golgi Apparatus - metabolism</topic><topic>Humans</topic><topic>Membrane Fusion - physiology</topic><topic>Membrane Lipids - metabolism</topic><topic>Models, Molecular</topic><topic>Monomeric Clathrin Assembly Proteins - metabolism</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>Neuropeptides - metabolism</topic><topic>Phosphatidylinositols - metabolism</topic><topic>Phosphoric Monoester Hydrolases - metabolism</topic><topic>Protein Binding</topic><topic>Protein Folding</topic><topic>Protein Structure, Tertiary</topic><topic>Vesicular Transport Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Legendre-Guillemin, Valerie</creatorcontrib><creatorcontrib>Wasiak, Sylwia</creatorcontrib><creatorcontrib>Hussain, Natasha K</creatorcontrib><creatorcontrib>Angers, Annie</creatorcontrib><creatorcontrib>McPherson, Peter S</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 cell science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Legendre-Guillemin, Valerie</au><au>Wasiak, Sylwia</au><au>Hussain, Natasha K</au><au>Angers, Annie</au><au>McPherson, Peter S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>ENTH/ANTH proteins and clathrin-mediated membrane budding</atitle><jtitle>Journal of cell science</jtitle><addtitle>J Cell Sci</addtitle><date>2004-01-01</date><risdate>2004</risdate><volume>117</volume><issue>Pt 1</issue><spage>9</spage><epage>18</epage><pages>9-18</pages><issn>0021-9533</issn><eissn>1477-9137</eissn><abstract>The epsin N-terminal homology (ENTH) domain is an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. 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| subjects | Adaptor Proteins, Vesicular Transport Animals Carrier Proteins - metabolism Clathrin - metabolism Endocytosis - physiology Golgi Apparatus - metabolism Humans Membrane Fusion - physiology Membrane Lipids - metabolism Models, Molecular Monomeric Clathrin Assembly Proteins - metabolism Nerve Tissue Proteins - metabolism Neuropeptides - metabolism Phosphatidylinositols - metabolism Phosphoric Monoester Hydrolases - metabolism Protein Binding Protein Folding Protein Structure, Tertiary Vesicular Transport Proteins |
| title | ENTH/ANTH proteins and clathrin-mediated membrane budding |
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