2012年8月
Tropomodulin Protects alpha-Catenin-Dependent Junctional-Actin Networks under Stress during Epithelial Morphogenesis
CURRENT BIOLOGY
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- 巻
- 22
- 号
- 16
- 開始ページ
- 1500
- 終了ページ
- 1505
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/j.cub.2012.06.025
- 出版者・発行元
- CELL PRESS
alpha-catenin is central to recruitment of actin networks to the cadherin-catenin complex [1, 2], but how such networks are subsequently stabilized against stress applied during morphogenesis is poorly understood. To identify proteins that functionally interact with alpha-catenin in this process, we performed enhancer screening using a weak allele of the C. elegans alpha-catenin, hmp-1, thereby identifying UNC-94/tropomodulin. Tropomodulins (Tmods) cap the minus ends of F-actin in sarcomeres [3]. They also regulate lamellipodia [4], can promote actin nucleation [5], and are required for normal cardiovascular development [6, 7] and neuronal growth-cone morphology [8]. Tmods regulate the morphology of cultured epithelial cells [9], but their role in epithelia in vivo remains unexplored. We find that UNC-94 is enriched within a HMP-1-dependent junctional-actin network at epidermal adherens junctions subject to stress during morphogenesis. Loss of UNC-94 leads to discontinuity of this network, and high-speed filming of hmp-1(fe4);unc-94(RNAi) embryos reveals large junctional displacements that depend on the Rho pathway. In vitro, UNC-94 acts in combination with HMP-1, leading to longer actin bundles than with HMP-1 alone. Our data suggest that Tmods protect actin filaments recruited by alpha-catenin from minus-end subunit loss, enabling them to withstand the stresses of morphogenesis.
- リンク情報
- ID情報
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- DOI : 10.1016/j.cub.2012.06.025
- ISSN : 0960-9822
- Web of Science ID : WOS:000307795000023