Characterization of TSET, an ancient and widespread membrane trafficking complex
The heterotetrameric AP and F-COPI complexes help to define the cellular map of modern eukaryotes. To search for related machinery, we developed a structure-based bioinformatics tool, and identified the core subunits of TSET, a 'missing link' between the APs and COPI. Studies in Dictyostel...
| Main Authors: | , , , , , , , , |
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2014-05-01
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| Series: | eLife |
| Subjects: | |
| Online Access: | https://elifesciences.org/articles/02866 |
| _version_ | 1811253331378569216 |
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| author | Jennifer Hirst Alexander Schlacht John P Norcott David Traynor Gareth Bloomfield Robin Antrobus Robert R Kay Joel B Dacks Margaret S Robinson |
| author_facet | Jennifer Hirst Alexander Schlacht John P Norcott David Traynor Gareth Bloomfield Robin Antrobus Robert R Kay Joel B Dacks Margaret S Robinson |
| author_sort | Jennifer Hirst |
| collection | DOAJ |
| description | The heterotetrameric AP and F-COPI complexes help to define the cellular map of modern eukaryotes. To search for related machinery, we developed a structure-based bioinformatics tool, and identified the core subunits of TSET, a 'missing link' between the APs and COPI. Studies in Dictyostelium indicate that TSET is a heterohexamer, with two associated scaffolding proteins. TSET is non-essential in Dictyostelium, but may act in plasma membrane turnover, and is essentially identical to the recently described TPLATE complex, TPC. However, whereas TPC was reported to be plant-specific, we can identify a full or partial complex in every eukaryotic supergroup. An evolutionary path can be deduced from the earliest origins of the heterotetramer/scaffold coat to its multiple manifestations in modern organisms, including the mammalian muniscins, descendants of the TSET medium subunits. Thus, we have uncovered the machinery for an ancient and widespread pathway, which provides new insights into early eukaryotic evolution. |
| first_indexed | 2024-04-12T16:49:15Z |
| format | Article |
| id | doaj.art-d506c478fe3b462da88d88a2ffe4d1c7 |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-12T16:49:15Z |
| publishDate | 2014-05-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-d506c478fe3b462da88d88a2ffe4d1c72022-12-22T03:24:28ZengeLife Sciences Publications LtdeLife2050-084X2014-05-01310.7554/eLife.02866Characterization of TSET, an ancient and widespread membrane trafficking complexJennifer Hirst0Alexander Schlacht1John P Norcott2David Traynor3Gareth Bloomfield4Robin Antrobus5Robert R Kay6Joel B Dacks7Margaret S Robinson8Cambridge Institute for Medical Research, University of Cambridge, Cambridge, United KingdomDepartment of Cell Biology, University of Alberta, Edmonton, CanadaDepartment of Engineering, University of Cambridge, Cambridge, United KingdomCell Biology, MRC Laboratory of Molecular Biology, Cambridge, United KingdomCell Biology, MRC Laboratory of Molecular Biology, Cambridge, United KingdomCambridge Institute for Medical Research, University of Cambridge, Cambridge, United KingdomCell Biology, MRC Laboratory of Molecular Biology, Cambridge, United KingdomDepartment of Cell Biology, University of Alberta, Edmonton, CanadaCambridge Institute for Medical Research, University of Cambridge, Cambridge, United KingdomThe heterotetrameric AP and F-COPI complexes help to define the cellular map of modern eukaryotes. To search for related machinery, we developed a structure-based bioinformatics tool, and identified the core subunits of TSET, a 'missing link' between the APs and COPI. Studies in Dictyostelium indicate that TSET is a heterohexamer, with two associated scaffolding proteins. TSET is non-essential in Dictyostelium, but may act in plasma membrane turnover, and is essentially identical to the recently described TPLATE complex, TPC. However, whereas TPC was reported to be plant-specific, we can identify a full or partial complex in every eukaryotic supergroup. An evolutionary path can be deduced from the earliest origins of the heterotetramer/scaffold coat to its multiple manifestations in modern organisms, including the mammalian muniscins, descendants of the TSET medium subunits. Thus, we have uncovered the machinery for an ancient and widespread pathway, which provides new insights into early eukaryotic evolution.https://elifesciences.org/articles/02866membrane trafficclathrinTPLATETPCmuniscinFCHo |
| spellingShingle | Jennifer Hirst Alexander Schlacht John P Norcott David Traynor Gareth Bloomfield Robin Antrobus Robert R Kay Joel B Dacks Margaret S Robinson Characterization of TSET, an ancient and widespread membrane trafficking complex eLife membrane traffic clathrin TPLATE TPC muniscin FCHo |
| title | Characterization of TSET, an ancient and widespread membrane trafficking complex |
| title_full | Characterization of TSET, an ancient and widespread membrane trafficking complex |
| title_fullStr | Characterization of TSET, an ancient and widespread membrane trafficking complex |
| title_full_unstemmed | Characterization of TSET, an ancient and widespread membrane trafficking complex |
| title_short | Characterization of TSET, an ancient and widespread membrane trafficking complex |
| title_sort | characterization of tset an ancient and widespread membrane trafficking complex |
| topic | membrane traffic clathrin TPLATE TPC muniscin FCHo |
| url | https://elifesciences.org/articles/02866 |
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