VASP-mediated actin dynamics activate and recruit a filopodia myosin
Filopodia are thin, actin-based structures that cells use to interact with their environments. Filopodia initiation requires a suite of conserved proteins but the mechanism remains poorly understood. The actin polymerase VASP and a MyTH-FERM (MF) myosin, DdMyo7 in amoeba, are essential for filopodia...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
| Published: |
eLife Sciences Publications Ltd
2021-05-01
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| Series: | eLife |
| Subjects: | |
| Online Access: | https://elifesciences.org/articles/68082 |
| _version_ | 1811202583816044544 |
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| author | Ashley L Arthur Amy Crawford Anne Houdusse Margaret A Titus |
| author_facet | Ashley L Arthur Amy Crawford Anne Houdusse Margaret A Titus |
| author_sort | Ashley L Arthur |
| collection | DOAJ |
| description | Filopodia are thin, actin-based structures that cells use to interact with their environments. Filopodia initiation requires a suite of conserved proteins but the mechanism remains poorly understood. The actin polymerase VASP and a MyTH-FERM (MF) myosin, DdMyo7 in amoeba, are essential for filopodia initiation. DdMyo7 is localized to dynamic regions of the actin-rich cortex. Analysis of VASP mutants and treatment of cells with anti-actin drugs shows that myosin recruitment and activation in Dictyostelium requires localized VASP-dependent actin polymerization. Targeting of DdMyo7 to the cortex alone is not sufficient for filopodia initiation; VASP activity is also required. The actin regulator locally produces a cortical actin network that activates myosin and together they shape the actin network to promote extension of parallel bundles of actin during filopodia formation. This work reveals how filopodia initiation requires close collaboration between an actin-binding protein, the state of the actin cytoskeleton and MF myosin activity. |
| first_indexed | 2024-04-12T02:41:10Z |
| format | Article |
| id | doaj.art-b8fc969d8cb74e69ae1bd0fcea1eaad6 |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-12T02:41:10Z |
| publishDate | 2021-05-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-b8fc969d8cb74e69ae1bd0fcea1eaad62022-12-22T03:51:18ZengeLife Sciences Publications LtdeLife2050-084X2021-05-011010.7554/eLife.68082VASP-mediated actin dynamics activate and recruit a filopodia myosinAshley L Arthur0https://orcid.org/0000-0001-8661-2873Amy Crawford1https://orcid.org/0000-0001-6147-7716Anne Houdusse2https://orcid.org/0000-0002-8566-0336Margaret A Titus3https://orcid.org/0000-0002-7583-9092Department of Genetics, Cell Biology, and Development, University of Minnesota, Minneapolis, United StatesDepartment of Genetics, Cell Biology, and Development, University of Minnesota, Minneapolis, United StatesStructural Motility, Institut Curie, Paris Université Sciences et Lettres, Sorbonne Université, Paris, FranceDepartment of Genetics, Cell Biology, and Development, University of Minnesota, Minneapolis, United StatesFilopodia are thin, actin-based structures that cells use to interact with their environments. Filopodia initiation requires a suite of conserved proteins but the mechanism remains poorly understood. The actin polymerase VASP and a MyTH-FERM (MF) myosin, DdMyo7 in amoeba, are essential for filopodia initiation. DdMyo7 is localized to dynamic regions of the actin-rich cortex. Analysis of VASP mutants and treatment of cells with anti-actin drugs shows that myosin recruitment and activation in Dictyostelium requires localized VASP-dependent actin polymerization. Targeting of DdMyo7 to the cortex alone is not sufficient for filopodia initiation; VASP activity is also required. The actin regulator locally produces a cortical actin network that activates myosin and together they shape the actin network to promote extension of parallel bundles of actin during filopodia formation. This work reveals how filopodia initiation requires close collaboration between an actin-binding protein, the state of the actin cytoskeleton and MF myosin activity.https://elifesciences.org/articles/68082filopodiaactin dynamicsMyTH-FERM myosinVASPmyosin autoinhibition |
| spellingShingle | Ashley L Arthur Amy Crawford Anne Houdusse Margaret A Titus VASP-mediated actin dynamics activate and recruit a filopodia myosin eLife filopodia actin dynamics MyTH-FERM myosin VASP myosin autoinhibition |
| title | VASP-mediated actin dynamics activate and recruit a filopodia myosin |
| title_full | VASP-mediated actin dynamics activate and recruit a filopodia myosin |
| title_fullStr | VASP-mediated actin dynamics activate and recruit a filopodia myosin |
| title_full_unstemmed | VASP-mediated actin dynamics activate and recruit a filopodia myosin |
| title_short | VASP-mediated actin dynamics activate and recruit a filopodia myosin |
| title_sort | vasp mediated actin dynamics activate and recruit a filopodia myosin |
| topic | filopodia actin dynamics MyTH-FERM myosin VASP myosin autoinhibition |
| url | https://elifesciences.org/articles/68082 |
| work_keys_str_mv | AT ashleylarthur vaspmediatedactindynamicsactivateandrecruitafilopodiamyosin AT amycrawford vaspmediatedactindynamicsactivateandrecruitafilopodiamyosin AT annehoudusse vaspmediatedactindynamicsactivateandrecruitafilopodiamyosin AT margaretatitus vaspmediatedactindynamicsactivateandrecruitafilopodiamyosin |