Coordinated recruitment of Spir actin nucleators and myosin V motors to Rab11 vesicle membranes
There is growing evidence for a coupling of actin assembly and myosin motor activity in cells. However, mechanisms for recruitment of actin nucleators and motors on specific membrane compartments remain unclear. Here we report how Spir actin nucleators and myosin V motors coordinate their specific m...
| Main Authors: | , , , , , , , , , , , , , , , , , , |
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| Format: | Article |
| Published: |
eLife Sciences Publications
2016
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| Online Access: | https://eprints.nottingham.ac.uk/48805/ |
| _version_ | 1848797852101246976 |
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| author | Pylypenko, Olena Welz, Tobias Tittel, Janine Kollmar, Martin Chardon, Florian Malherbe, Gilles Weiss, Sabine Michel, Carina Ida Luise Samol-Wolf, Annette Grasskamp, Andreas Till Hume, Alistair Goud, Bruno Baron, Bruno England, Patrick Titus, Margaret A. Schwille, Petra Weidemann, Thomas Houdusse, Anne Kerkhoff, Eugen |
| author_facet | Pylypenko, Olena Welz, Tobias Tittel, Janine Kollmar, Martin Chardon, Florian Malherbe, Gilles Weiss, Sabine Michel, Carina Ida Luise Samol-Wolf, Annette Grasskamp, Andreas Till Hume, Alistair Goud, Bruno Baron, Bruno England, Patrick Titus, Margaret A. Schwille, Petra Weidemann, Thomas Houdusse, Anne Kerkhoff, Eugen |
| author_sort | Pylypenko, Olena |
| building | Nottingham Research Data Repository |
| collection | Online Access |
| description | There is growing evidence for a coupling of actin assembly and myosin motor activity in cells. However, mechanisms for recruitment of actin nucleators and motors on specific membrane compartments remain unclear. Here we report how Spir actin nucleators and myosin V motors coordinate their specific membrane recruitment. The myosin V globular tail domain (MyoV-GTD) interacts directly with an evolutionarily conserved Spir sequence motif. We determined crystal structures of MyoVa-GTD bound either to the Spir-2 motif or to Rab11 and show that a Spir-2:MyoVa:Rab11 complex can form. The ternary complex architecture explains how Rab11 vesicles support coordinated F-actin nucleation and myosin force generation for vesicle transport and tethering. New insights are also provided into how myosin activation can be coupled with the generation of actin tracks. Since MyoV binds several Rab GTPases, synchronized nucleator and motor targeting could provide a common mechanism to control force generation and motility in different cellular processes. |
| first_indexed | 2025-11-14T20:10:27Z |
| format | Article |
| id | nottingham-48805 |
| institution | University of Nottingham Malaysia Campus |
| institution_category | Local University |
| last_indexed | 2025-11-14T20:10:27Z |
| publishDate | 2016 |
| publisher | eLife Sciences Publications |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | nottingham-488052020-05-04T18:12:38Z https://eprints.nottingham.ac.uk/48805/ Coordinated recruitment of Spir actin nucleators and myosin V motors to Rab11 vesicle membranes Pylypenko, Olena Welz, Tobias Tittel, Janine Kollmar, Martin Chardon, Florian Malherbe, Gilles Weiss, Sabine Michel, Carina Ida Luise Samol-Wolf, Annette Grasskamp, Andreas Till Hume, Alistair Goud, Bruno Baron, Bruno England, Patrick Titus, Margaret A. Schwille, Petra Weidemann, Thomas Houdusse, Anne Kerkhoff, Eugen There is growing evidence for a coupling of actin assembly and myosin motor activity in cells. However, mechanisms for recruitment of actin nucleators and motors on specific membrane compartments remain unclear. Here we report how Spir actin nucleators and myosin V motors coordinate their specific membrane recruitment. The myosin V globular tail domain (MyoV-GTD) interacts directly with an evolutionarily conserved Spir sequence motif. We determined crystal structures of MyoVa-GTD bound either to the Spir-2 motif or to Rab11 and show that a Spir-2:MyoVa:Rab11 complex can form. The ternary complex architecture explains how Rab11 vesicles support coordinated F-actin nucleation and myosin force generation for vesicle transport and tethering. New insights are also provided into how myosin activation can be coupled with the generation of actin tracks. Since MyoV binds several Rab GTPases, synchronized nucleator and motor targeting could provide a common mechanism to control force generation and motility in different cellular processes. eLife Sciences Publications 2016-09-13 Article PeerReviewed Pylypenko, Olena, Welz, Tobias, Tittel, Janine, Kollmar, Martin, Chardon, Florian, Malherbe, Gilles, Weiss, Sabine, Michel, Carina Ida Luise, Samol-Wolf, Annette, Grasskamp, Andreas Till, Hume, Alistair, Goud, Bruno, Baron, Bruno, England, Patrick, Titus, Margaret A., Schwille, Petra, Weidemann, Thomas, Houdusse, Anne and Kerkhoff, Eugen (2016) Coordinated recruitment of Spir actin nucleators and myosin V motors to Rab11 vesicle membranes. eLife, 5 . e17523/1-e17523/25. ISSN 2050-084X https://elifesciences.org/articles/17523 doi:10.7554/eLife.17523 doi:10.7554/eLife.17523 |
| spellingShingle | Pylypenko, Olena Welz, Tobias Tittel, Janine Kollmar, Martin Chardon, Florian Malherbe, Gilles Weiss, Sabine Michel, Carina Ida Luise Samol-Wolf, Annette Grasskamp, Andreas Till Hume, Alistair Goud, Bruno Baron, Bruno England, Patrick Titus, Margaret A. Schwille, Petra Weidemann, Thomas Houdusse, Anne Kerkhoff, Eugen Coordinated recruitment of Spir actin nucleators and myosin V motors to Rab11 vesicle membranes |
| title | Coordinated recruitment of Spir actin nucleators and myosin V motors to Rab11 vesicle membranes |
| title_full | Coordinated recruitment of Spir actin nucleators and myosin V motors to Rab11 vesicle membranes |
| title_fullStr | Coordinated recruitment of Spir actin nucleators and myosin V motors to Rab11 vesicle membranes |
| title_full_unstemmed | Coordinated recruitment of Spir actin nucleators and myosin V motors to Rab11 vesicle membranes |
| title_short | Coordinated recruitment of Spir actin nucleators and myosin V motors to Rab11 vesicle membranes |
| title_sort | coordinated recruitment of spir actin nucleators and myosin v motors to rab11 vesicle membranes |
| url | https://eprints.nottingham.ac.uk/48805/ https://eprints.nottingham.ac.uk/48805/ https://eprints.nottingham.ac.uk/48805/ |