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In vivo epidermal migration requires focal adhesion targeting of ACF7

Author

Listed:
  • Jiping Yue

    (The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA)

  • Yao Zhang

    (State Key Laboratory Cultivation Base for the Chemistry and Molecular Engineering of Medicinal Resources, Ministry of Science and Technology of China, Guanxi Normal University)

  • Wenguang G. Liang

    (The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA)

  • Xuewen Gou

    (The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA)

  • Philbert Lee

    (The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA)

  • Han Liu

    (The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA)

  • Wanqing Lyu

    (The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA)

  • Wei-Jen Tang

    (The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA)

  • Shao-Yu Chen

    (University of Louisville Health Science Center)

  • Feng Yang

    (State Key Laboratory Cultivation Base for the Chemistry and Molecular Engineering of Medicinal Resources, Ministry of Science and Technology of China, Guanxi Normal University)

  • Hong Liang

    (State Key Laboratory Cultivation Base for the Chemistry and Molecular Engineering of Medicinal Resources, Ministry of Science and Technology of China, Guanxi Normal University)

  • Xiaoyang Wu

    (The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA)

Abstract

Turnover of focal adhesions allows cell retraction, which is essential for cell migration. The mammalian spectraplakin protein, ACF7 (Actin-Crosslinking Factor 7), promotes focal adhesion dynamics by targeting of microtubule plus ends towards focal adhesions. However, it remains unclear how the activity of ACF7 is regulated spatiotemporally to achieve focal adhesion-specific guidance of microtubule. To explore the potential mechanisms, we resolve the crystal structure of ACF7’s NT (amino-terminal) domain, which mediates F-actin interactions. Structural analysis leads to identification of a key tyrosine residue at the calponin homology (CH) domain of ACF7, whose phosphorylation by Src/FAK (focal adhesion kinase) complex is essential for F-actin binding of ACF7. Using skin epidermis as a model system, we further demonstrate that the phosphorylation of ACF7 plays an indispensable role in focal adhesion dynamics and epidermal migration in vitro and in vivo. Together, our findings provide critical insights into the molecular mechanisms underlying coordinated cytoskeletal dynamics during cell movement.

Suggested Citation

  • Jiping Yue & Yao Zhang & Wenguang G. Liang & Xuewen Gou & Philbert Lee & Han Liu & Wanqing Lyu & Wei-Jen Tang & Shao-Yu Chen & Feng Yang & Hong Liang & Xiaoyang Wu, 2016. "In vivo epidermal migration requires focal adhesion targeting of ACF7," Nature Communications, Nature, vol. 7(1), pages 1-15, September.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms11692
    DOI: 10.1038/ncomms11692
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    Cited by:

    1. Reena Kumari & Katharina Ven & Megan Chastney & Shrikant B. Kokate & Johan Peränen & Jesse Aaron & Konstantin Kogan & Leonardo Almeida-Souza & Elena Kremneva & Renaud Poincloux & Teng-Leong Chew & Pet, 2024. "Focal adhesions contain three specialized actin nanoscale layers," Nature Communications, Nature, vol. 15(1), pages 1-20, December.

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