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.
journal_name
Mol Biol Celljournal_title
Molecular biology of the cellauthors
Applewhite DA,Grode KD,Duncan MC,Rogers SLdoi
10.1091/mbc.E12-11-0798subject
Has Abstractpub_date
2013-09-01 00:00:00pages
2885-93issue
18eissn
1059-1524issn
1939-4586pii
mbc.E12-11-0798journal_volume
24pub_type
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