Golgi vesicle proteins are linked to the assembly of an actin complex defined by mAbp1
Recent studies indicate that regulation of the actin cytoskeleton is important for protein trafficking, but its precise role is unclear. We have characterized the ARF1-dependent assembly of actin on the Golgi apparatus. Actin recruitment involves Cdc42/Rac and requires the activation of the Arp2/3 c...
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| Veröffentlicht in: | Molecular biology of the cell 2002-02, Vol.13 (2), p.621-631 |
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| container_title | Molecular biology of the cell |
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| creator | Fucini, Raymond V Chen, Ji-Long Sharma, Catherine Kessels, Michael M Stamnes, Mark |
| description | Recent studies indicate that regulation of the actin cytoskeleton is important for protein trafficking, but its precise role is unclear. We have characterized the ARF1-dependent assembly of actin on the Golgi apparatus. Actin recruitment involves Cdc42/Rac and requires the activation of the Arp2/3 complex. Although the actin-binding proteins mAbp1 (SH3p7) and drebrin share sequence homology, they are differentially segregated into two distinct ARF-dependent actin complexes. The binding of Cdc42 and mAbp1, which localize to the Golgi apparatus, but not drebrin, is blocked by occupation of the p23 cargo-protein-binding site on coatomer. Exogenously expressed mAbp1 is mislocalized and inhibits Golgi transport in whole cells. The ability of ARF, vesicle-coat proteins, and cargo to direct the assembly of cytoskeletal structures helps explain how only a handful of vesicle types can mediate the numerous trafficking steps in the cell. |
| doi_str_mv | 10.1091/mbc.01-11-0547 |
| format | Article |
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We have characterized the ARF1-dependent assembly of actin on the Golgi apparatus. Actin recruitment involves Cdc42/Rac and requires the activation of the Arp2/3 complex. Although the actin-binding proteins mAbp1 (SH3p7) and drebrin share sequence homology, they are differentially segregated into two distinct ARF-dependent actin complexes. The binding of Cdc42 and mAbp1, which localize to the Golgi apparatus, but not drebrin, is blocked by occupation of the p23 cargo-protein-binding site on coatomer. Exogenously expressed mAbp1 is mislocalized and inhibits Golgi transport in whole cells. The ability of ARF, vesicle-coat proteins, and cargo to direct the assembly of cytoskeletal structures helps explain how only a handful of vesicle types can mediate the numerous trafficking steps in the cell.</description><subject>Actins - physiology</subject><subject>ADP-Ribosylation Factor 1 - physiology</subject><subject>Animals</subject><subject>Cattle</subject><subject>cdc42 GTP-Binding Protein - physiology</subject><subject>Cytoskeleton - physiology</subject><subject>Golgi Apparatus - physiology</subject><subject>Macromolecular Substances</subject><subject>Membrane Proteins - physiology</subject><subject>Microfilament Proteins - physiology</subject><subject>Rats</subject><subject>rho GTP-Binding Proteins - physiology</subject><subject>Secretory Vesicles - physiology</subject><subject>src Homology Domains</subject><issn>1059-1524</issn><issn>1939-4586</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkc1PwzAMxSMEYjC4ckQ5ceuI26RJJS7TxJc0iQtwjdLUhUDalKab2H9PJyY-Trbk37Of_Ag5AzYDVsBlU9oZgwQgYYLLPXIERVYkXKh8f-yZKBIQKZ-Q4xjfGAPOc3lIJgBKcA7yiDzfBv_i6Bqjsx5p14cBXRup6ZF6175jRYdAh1ekJkZsSr-hoaampcYOrqU2NJ3HT1ph7dqRLTe0mZcdnJCD2viIp7s6JU8314-Lu2T5cHu_mC8TyxUbkipNGeQKFUeWYl5kKpMFKlYZkxUSpRBY8zozSuaQZkoaaQBribYqwVYFZFNy9b23W5UNVhbboTded71rTL_RwTj9f9K6V_0S1joXueCj_GIn78PHCuOgGxctem9aDKuoJXAhObARnH2Dtg8x9lj_nACmt0HoMQjNQAPobRCj4PyvsV989_nsC3aZhVw</recordid><startdate>20020201</startdate><enddate>20020201</enddate><creator>Fucini, Raymond V</creator><creator>Chen, Ji-Long</creator><creator>Sharma, Catherine</creator><creator>Kessels, Michael M</creator><creator>Stamnes, Mark</creator><general>The American Society for Cell Biology</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><scope>5PM</scope></search><sort><creationdate>20020201</creationdate><title>Golgi vesicle proteins are linked to the assembly of an actin complex defined by mAbp1</title><author>Fucini, Raymond V ; Chen, Ji-Long ; Sharma, Catherine ; Kessels, Michael M ; Stamnes, Mark</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c480t-d220168e84e02e6938379e80daa397e755ef4f3a87612387a7a1ef7ecdb1cd913</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Actins - physiology</topic><topic>ADP-Ribosylation Factor 1 - physiology</topic><topic>Animals</topic><topic>Cattle</topic><topic>cdc42 GTP-Binding Protein - physiology</topic><topic>Cytoskeleton - physiology</topic><topic>Golgi Apparatus - physiology</topic><topic>Macromolecular Substances</topic><topic>Membrane Proteins - physiology</topic><topic>Microfilament Proteins - physiology</topic><topic>Rats</topic><topic>rho GTP-Binding Proteins - physiology</topic><topic>Secretory Vesicles - physiology</topic><topic>src Homology Domains</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fucini, Raymond V</creatorcontrib><creatorcontrib>Chen, Ji-Long</creatorcontrib><creatorcontrib>Sharma, Catherine</creatorcontrib><creatorcontrib>Kessels, Michael M</creatorcontrib><creatorcontrib>Stamnes, Mark</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Molecular biology of the cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fucini, Raymond V</au><au>Chen, Ji-Long</au><au>Sharma, Catherine</au><au>Kessels, Michael M</au><au>Stamnes, Mark</au><au>Bonifacino, Juan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Golgi vesicle proteins are linked to the assembly of an actin complex defined by mAbp1</atitle><jtitle>Molecular biology of the cell</jtitle><addtitle>Mol Biol Cell</addtitle><date>2002-02-01</date><risdate>2002</risdate><volume>13</volume><issue>2</issue><spage>621</spage><epage>631</epage><pages>621-631</pages><issn>1059-1524</issn><eissn>1939-4586</eissn><abstract>Recent studies indicate that regulation of the actin cytoskeleton is important for protein trafficking, but its precise role is unclear. 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| subjects | Actins - physiology ADP-Ribosylation Factor 1 - physiology Animals Cattle cdc42 GTP-Binding Protein - physiology Cytoskeleton - physiology Golgi Apparatus - physiology Macromolecular Substances Membrane Proteins - physiology Microfilament Proteins - physiology Rats rho GTP-Binding Proteins - physiology Secretory Vesicles - physiology src Homology Domains |
| title | Golgi vesicle proteins are linked to the assembly of an actin complex defined by mAbp1 |
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