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Regulation of actin dynamics through phosphorylation of cofilin by LIM-kinase

Author

Listed:
  • Silvia Arber

    (Friedrich Miescher Institute
    Columbia University)

  • Freda A. Barbayannis

    (Walter and Eliza Hall Institute of Medical Research)

  • Hartwig Hanser

    (Friedrich Miescher Institute)

  • Corinna Schneider

    (Friedrich Miescher Institute)

  • Clement A. Stanyon

    (Walter and Eliza Hall Institute of Medical Research)

  • Ora Bernard

    (Walter and Eliza Hall Institute of Medical Research)

  • Pico Caroni

    (Friedrich Miescher Institute)

Abstract

Cell division, cell motility and the formation and maintenance of specialized structures in differentiated cells depend directly on the regulated dynamics of the actin cytoskeleton1,2. To understand the mechanisms of these basic cellular processes, the signalling pathways that link external signals to the regulation of the actin cytoskeleton need to be characterized2,3. Here we identify a pathway for the regulation of cofilin, a ubiquitous actin-binding protein that is essential for effective depolymerization of actin filaments4,5,6,7,8. LIM-kinase 1, also known as KIZ, is a protein kinase with two amino-terminal LIM motifs9,10,11 that induces stabilization of F-actin structures in transfected cells. Dominant-negative LIM-kinase1 inhibits the accumulation of the F-actin. Phosphorylation experiments in vivo and in vitro provide evidence that cofilin is a physiological substrate of LIM-kinase 1. Phosphorylation by LIM-kinase 1 inactivates cofilin, leading to accumulation of actin filaments. Constitutively active Rac augmented cofilin phosphorylation and LIM-kinase 1 autophosphorylation whereas phorbol ester inhibited these processes. Our results define a mechanism for the regulation of cofilin and hence of actin dynamics in vivo. By modulating the stability of actin cytoskeletal structures, this pathway should play a central role in regulating cell motility and morphogenesis.

Suggested Citation

  • Silvia Arber & Freda A. Barbayannis & Hartwig Hanser & Corinna Schneider & Clement A. Stanyon & Ora Bernard & Pico Caroni, 1998. "Regulation of actin dynamics through phosphorylation of cofilin by LIM-kinase," Nature, Nature, vol. 393(6687), pages 805-809, June.
  • Handle: RePEc:nat:nature:v:393:y:1998:i:6687:d:10.1038_31729
    DOI: 10.1038/31729
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    Cited by:

    1. Tamara Advedissian & Stéphane Frémont & Arnaud Echard, 2024. "Cytokinetic abscission requires actin-dependent microtubule severing," Nature Communications, Nature, vol. 15(1), pages 1-17, December.
    2. Caroline Dour & Maria Chatzifrangkeskou & Coline Macquart & Maria M. Magiera & Cécile Peccate & Charlène Jouve & Laura Virtanen & Tiina Heliö & Katriina Aalto-Setälä & Silvia Crasto & Bruno Cadot & Dé, 2022. "Actin-microtubule cytoskeletal interplay mediated by MRTF-A/SRF signaling promotes dilated cardiomyopathy caused by LMNA mutations," Nature Communications, Nature, vol. 13(1), pages 1-21, December.
    3. Jiacheng Wu & Xiaoqing Xu & Jiaqi Duan & Yangyang Chai & Jiaying Song & Dongsheng Gong & Bingjing Wang & Ye Hu & Taotao Han & Yuanyuan Ding & Yin Liu & Jingnan Li & Xuetao Cao, 2024. "EFHD2 suppresses intestinal inflammation by blocking intestinal epithelial cell TNFR1 internalization and cell death," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    4. Vincent On & Atena Zahedi & Iryna M Ethell & Bir Bhanu, 2017. "Automated spatio-temporal analysis of dendritic spines and related protein dynamics," PLOS ONE, Public Library of Science, vol. 12(8), pages 1-23, August.
    5. Gabriela Casanova-Sepúlveda & Joel A. Sexton & Benjamin E. Turk & Titus J. Boggon, 2023. "Autoregulation of the LIM kinases by their PDZ domain," Nature Communications, Nature, vol. 14(1), pages 1-13, December.

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