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The actin-microtubule cross-linking activity of Drosophila Short stop is regulated by intramolecular inhibition
Actin and microtubule dynamics must be precisely coordinated during cell migration, mitosis, and morphogenesis—much of this coordination is mediated by proteins that physically bridge the two cytoskeletal networks. We have investigated the regulation of the Drosophila actin-microtubule cross-linker...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3771950/ https://www.ncbi.nlm.nih.gov/pubmed/23885120 http://dx.doi.org/10.1091/mbc.E12-11-0798 |
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author | Applewhite, Derek A. Grode, Kyle D. Duncan, Mara C. Rogers, Stephen L. |
author_facet | Applewhite, Derek A. Grode, Kyle D. Duncan, Mara C. Rogers, Stephen L. |
author_sort | Applewhite, Derek A. |
collection | PubMed |
description | Actin and microtubule dynamics must be precisely coordinated during cell migration, mitosis, and morphogenesis—much of this coordination is mediated by proteins that physically bridge the two cytoskeletal networks. We have investigated the regulation of the Drosophila actin-microtubule cross-linker Short stop (Shot), a member of the spectraplakin family. Our data suggest that Shot's cytoskeletal cross-linking activity is regulated by an intramolecular inhibitory mechanism. In its inactive conformation, Shot adopts a “closed” conformation through interactions between its NH(2)-terminal actin-binding domain and COOH-terminal EF-hand-GAS2 domain. This inactive conformation is targeted to the growing microtubule plus end by EB1. On activation, Shot binds along the microtubule through its COOH-terminal GAS2 domain and binds to actin with its NH(2)-terminal tandem CH domains. We propose that this mechanism allows Shot to rapidly cross-link dynamic microtubules in response to localized activating signals at the cell cortex. |
format | Online Article Text |
id | pubmed-3771950 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-37719502013-11-30 The actin-microtubule cross-linking activity of Drosophila Short stop is regulated by intramolecular inhibition Applewhite, Derek A. Grode, Kyle D. Duncan, Mara C. Rogers, Stephen L. Mol Biol Cell Articles Actin and microtubule dynamics must be precisely coordinated during cell migration, mitosis, and morphogenesis—much of this coordination is mediated by proteins that physically bridge the two cytoskeletal networks. We have investigated the regulation of the Drosophila actin-microtubule cross-linker Short stop (Shot), a member of the spectraplakin family. Our data suggest that Shot's cytoskeletal cross-linking activity is regulated by an intramolecular inhibitory mechanism. In its inactive conformation, Shot adopts a “closed” conformation through interactions between its NH(2)-terminal actin-binding domain and COOH-terminal EF-hand-GAS2 domain. This inactive conformation is targeted to the growing microtubule plus end by EB1. On activation, Shot binds along the microtubule through its COOH-terminal GAS2 domain and binds to actin with its NH(2)-terminal tandem CH domains. We propose that this mechanism allows Shot to rapidly cross-link dynamic microtubules in response to localized activating signals at the cell cortex. The American Society for Cell Biology 2013-09-15 /pmc/articles/PMC3771950/ /pubmed/23885120 http://dx.doi.org/10.1091/mbc.E12-11-0798 Text en © 2013 Applewhite et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell Biology. |
spellingShingle | Articles Applewhite, Derek A. Grode, Kyle D. Duncan, Mara C. Rogers, Stephen L. The actin-microtubule cross-linking activity of Drosophila Short stop is regulated by intramolecular inhibition |
title | The actin-microtubule cross-linking activity of Drosophila Short stop is regulated by intramolecular inhibition |
title_full | The actin-microtubule cross-linking activity of Drosophila Short stop is regulated by intramolecular inhibition |
title_fullStr | The actin-microtubule cross-linking activity of Drosophila Short stop is regulated by intramolecular inhibition |
title_full_unstemmed | The actin-microtubule cross-linking activity of Drosophila Short stop is regulated by intramolecular inhibition |
title_short | The actin-microtubule cross-linking activity of Drosophila Short stop is regulated by intramolecular inhibition |
title_sort | actin-microtubule cross-linking activity of drosophila short stop is regulated by intramolecular inhibition |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3771950/ https://www.ncbi.nlm.nih.gov/pubmed/23885120 http://dx.doi.org/10.1091/mbc.E12-11-0798 |
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