Functional interdependence of the actin nucleator Cobl and Cobl-like in dendritic arbor development
Local actin filament formation is indispensable for development of the dendritic arbor of neurons. We show that, surprisingly, the action of single actin filament-promoting factors was insufficient for powering dendritogenesis. Instead, this required the actin nucleator Cobl and its only evolutionar...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2021-07-01
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| Series: | eLife |
| Subjects: | |
| Online Access: | https://elifesciences.org/articles/67718 |
| _version_ | 1797997605405327360 |
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| author | Maryam Izadi Eric Seemann Dirk Schlobinski Lukas Schwintzer Britta Qualmann Michael M Kessels |
| author_facet | Maryam Izadi Eric Seemann Dirk Schlobinski Lukas Schwintzer Britta Qualmann Michael M Kessels |
| author_sort | Maryam Izadi |
| collection | DOAJ |
| description | Local actin filament formation is indispensable for development of the dendritic arbor of neurons. We show that, surprisingly, the action of single actin filament-promoting factors was insufficient for powering dendritogenesis. Instead, this required the actin nucleator Cobl and its only evolutionary distant ancestor Cobl-like acting interdependently. This coordination between Cobl-like and Cobl was achieved by physical linkage by syndapins. Syndapin I formed nanodomains at convex plasma membrane areas at the base of protrusive structures and interacted with three motifs in Cobl-like, one of which was Ca2+/calmodulin-regulated. Consistently, syndapin I, Cobl-like’s newly identified N terminal calmodulin-binding site and the single Ca2+/calmodulin-responsive syndapin-binding motif all were critical for Cobl-like’s functions. In dendritic arbor development, local Ca2+/CaM-controlled actin dynamics thus relies on regulated and physically coordinated interactions of different F-actin formation-promoting factors and only together they have the power to bring about the sophisticated neuronal morphologies required for neuronal network formation in mammals. |
| first_indexed | 2024-04-11T10:35:26Z |
| format | Article |
| id | doaj.art-1f6b440f96a64ce78a80bc81a2560c6c |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-11T10:35:26Z |
| publishDate | 2021-07-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-1f6b440f96a64ce78a80bc81a2560c6c2022-12-22T04:29:18ZengeLife Sciences Publications LtdeLife2050-084X2021-07-011010.7554/eLife.67718Functional interdependence of the actin nucleator Cobl and Cobl-like in dendritic arbor developmentMaryam Izadi0Eric Seemann1Dirk Schlobinski2Lukas Schwintzer3Britta Qualmann4https://orcid.org/0000-0002-5743-5764Michael M Kessels5https://orcid.org/0000-0001-5967-0744Institute of Biochemistry I, Jena University Hospital/Friedrich-Schiller-University Jena, Jena, GermanyInstitute of Biochemistry I, Jena University Hospital/Friedrich-Schiller-University Jena, Jena, GermanyInstitute of Biochemistry I, Jena University Hospital/Friedrich-Schiller-University Jena, Jena, GermanyInstitute of Biochemistry I, Jena University Hospital/Friedrich-Schiller-University Jena, Jena, GermanyInstitute of Biochemistry I, Jena University Hospital/Friedrich-Schiller-University Jena, Jena, GermanyInstitute of Biochemistry I, Jena University Hospital/Friedrich-Schiller-University Jena, Jena, GermanyLocal actin filament formation is indispensable for development of the dendritic arbor of neurons. We show that, surprisingly, the action of single actin filament-promoting factors was insufficient for powering dendritogenesis. Instead, this required the actin nucleator Cobl and its only evolutionary distant ancestor Cobl-like acting interdependently. This coordination between Cobl-like and Cobl was achieved by physical linkage by syndapins. Syndapin I formed nanodomains at convex plasma membrane areas at the base of protrusive structures and interacted with three motifs in Cobl-like, one of which was Ca2+/calmodulin-regulated. Consistently, syndapin I, Cobl-like’s newly identified N terminal calmodulin-binding site and the single Ca2+/calmodulin-responsive syndapin-binding motif all were critical for Cobl-like’s functions. In dendritic arbor development, local Ca2+/CaM-controlled actin dynamics thus relies on regulated and physically coordinated interactions of different F-actin formation-promoting factors and only together they have the power to bring about the sophisticated neuronal morphologies required for neuronal network formation in mammals.https://elifesciences.org/articles/67718actin nucleatorsfunctional cooperation of actin nucleatorsCa2+-steeredF-actin-supported neuronal morphogenesisF-BAR domain protein syndapin Idendritic branch initiation sites |
| spellingShingle | Maryam Izadi Eric Seemann Dirk Schlobinski Lukas Schwintzer Britta Qualmann Michael M Kessels Functional interdependence of the actin nucleator Cobl and Cobl-like in dendritic arbor development eLife actin nucleators functional cooperation of actin nucleators Ca2+-steered F-actin-supported neuronal morphogenesis F-BAR domain protein syndapin I dendritic branch initiation sites |
| title | Functional interdependence of the actin nucleator Cobl and Cobl-like in dendritic arbor development |
| title_full | Functional interdependence of the actin nucleator Cobl and Cobl-like in dendritic arbor development |
| title_fullStr | Functional interdependence of the actin nucleator Cobl and Cobl-like in dendritic arbor development |
| title_full_unstemmed | Functional interdependence of the actin nucleator Cobl and Cobl-like in dendritic arbor development |
| title_short | Functional interdependence of the actin nucleator Cobl and Cobl-like in dendritic arbor development |
| title_sort | functional interdependence of the actin nucleator cobl and cobl like in dendritic arbor development |
| topic | actin nucleators functional cooperation of actin nucleators Ca2+-steered F-actin-supported neuronal morphogenesis F-BAR domain protein syndapin I dendritic branch initiation sites |
| url | https://elifesciences.org/articles/67718 |
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