Integration of the Rac1- and actin-binding properties of Coronin-1C
The coronin family of actin-binding proteins regulate actin branching by inhibiting Arp2/3. We recently reported 2 interactions that were unique to coronin-1C: binding of a Rac1 inhibitor, RCC2, to the unique linker region and Rac1 itself to the propeller domain in a manner that differs from that pr...
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| Veröffentlicht in: | Small GTPases 2015-01, Vol.6 (1), p.36-42 |
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| creator | Tilley, Frances C Williamson, Rosalind C Race, Paul R Rendall, Thomas C Bass, Mark D |
| description | The coronin family of actin-binding proteins regulate actin branching by inhibiting Arp2/3. We recently reported 2 interactions that were unique to coronin-1C: binding of a Rac1 inhibitor, RCC2, to the unique linker region and Rac1 itself to the propeller domain in a manner that differs from that proposed for other coronins. Through these interactions coronin-1C redistributes Rac1 from the back of the cell to the leading edge for either activation or sequestration by the associated Rac1-inhibitor, RCC2. Here we investigate the relationship between the Rac1- and actin-binding properties of coronin-1C and find that, although actin appears to be involved in the retrafficking of Rac1, signaling by Rac1 lies upstream of the stress fiber-formation, for which the coronins were originally characterized. |
| doi_str_mv | 10.4161/21541248.2014.992259 |
| format | Article |
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We recently reported 2 interactions that were unique to coronin-1C: binding of a Rac1 inhibitor, RCC2, to the unique linker region and Rac1 itself to the propeller domain in a manner that differs from that proposed for other coronins. Through these interactions coronin-1C redistributes Rac1 from the back of the cell to the leading edge for either activation or sequestration by the associated Rac1-inhibitor, RCC2. Here we investigate the relationship between the Rac1- and actin-binding properties of coronin-1C and find that, although actin appears to be involved in the retrafficking of Rac1, signaling by Rac1 lies upstream of the stress fiber-formation, for which the coronins were originally characterized.</description><identifier>ISSN: 2154-1248</identifier><identifier>EISSN: 2154-1256</identifier><identifier>DOI: 10.4161/21541248.2014.992259</identifier><identifier>PMID: 25862165</identifier><language>eng</language><publisher>United States: Taylor & Francis</publisher><subject>actin ; Actins - genetics ; Actins - metabolism ; Amino Acid Sequence ; Animals ; Coronin-1C ; endocytosis ; Humans ; Letter to the Editor ; Mice ; Microfilament Proteins - chemistry ; Microfilament Proteins - genetics ; Microfilament Proteins - metabolism ; Molecular Sequence Data ; Protein Binding ; Protein Transport ; Rac1 ; rac1 GTP-Binding Protein - genetics ; rac1 GTP-Binding Protein - metabolism ; Sequence Alignment ; trafficking</subject><ispartof>Small GTPases, 2015-01, Vol.6 (1), p.36-42</ispartof><rights>2015 The Author(s). Published with license by Taylor & Francis Group, LLC © Frances C Tilley, Rosalind C Williamson, Paul R Race, Thomas C Rendall, and Mark D Bass 2015</rights><rights>2015 The Author(s). 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We recently reported 2 interactions that were unique to coronin-1C: binding of a Rac1 inhibitor, RCC2, to the unique linker region and Rac1 itself to the propeller domain in a manner that differs from that proposed for other coronins. Through these interactions coronin-1C redistributes Rac1 from the back of the cell to the leading edge for either activation or sequestration by the associated Rac1-inhibitor, RCC2. 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| subjects | actin Actins - genetics Actins - metabolism Amino Acid Sequence Animals Coronin-1C endocytosis Humans Letter to the Editor Mice Microfilament Proteins - chemistry Microfilament Proteins - genetics Microfilament Proteins - metabolism Molecular Sequence Data Protein Binding Protein Transport Rac1 rac1 GTP-Binding Protein - genetics rac1 GTP-Binding Protein - metabolism Sequence Alignment trafficking |
| title | Integration of the Rac1- and actin-binding properties of Coronin-1C |
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