The actin-microtubule cross-linking activity of Drosophila Short stop is regulated by intramolecular inhibition.
Mol Biol Cell
; 24(18): 2885-93, 2013 Sep.
Article
em En
| MEDLINE
| ID: mdl-23885120
ABSTRACT
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.
Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Actinas
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Reagentes de Ligações Cruzadas
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Proteínas de Drosophila
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Drosophila melanogaster
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Proteínas dos Microfilamentos
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Microtúbulos
Idioma:
En
Ano de publicação:
2013
Tipo de documento:
Article