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Tyrosine phosphorylation in plant bending

Nature volume 407, page 37 (07 September 2000) | Download Citation

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Abstract

The phosphorylation of the amino acid tyrosine in animal proteins acts as an on–off switch in numerous pathways that regulate growth, differentiation and oncogenesis1,2. In the unicellular slime mould Dictyostelium , tyrosine-phosphorylation of actin controls cell-shape changes and spore activity3,4, but the significance of protein-tyrosine phosphorylation in plants is unknown5. Here we show that actin in the contact-sensitive plant Mimosa pudica L. is heavily tyrosine-phosphorylated and that changes in the extent of phosphorylation correlate with the degree of bending of the plant's petioles. We propose that tyrosine-phosphorylation of actin controls movements in plants.

Puckering in a ticklish plant is controlled by dephosphorylation of its actin.

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Affiliations

  1. *Department of Chemistry, Faculty of Science and Technology, Sophia University, 7-1 Kioicho, Chiyoda-ku, Tokyo 102-8554, Japan

    • Kazuhisa Kameyama
    • , Masanori Yoshimura
    • , Nobuyuki Kanzawa
    •  & Takahide Tsuchiya
  2. †Department of Cell Biology, Tokyo Metropolitan Institute of Medical Science, Tokyo Metropolitan Organization for Medical Research, 3-18-22 Honkomagome, Bunkyo-ku , Tokyo 171-0021, Japan

    • Yoshiro Kishi
    •  & Masazumi Sameshima

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Correspondence to Takahide Tsuchiya.

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DOI

https://doi.org/10.1038/35024149

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