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CPI motif interaction is necessary for capping protein function in cells

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  • Marc Edwards

    (Washington University School of Medicine)

  • Patrick McConnell

    (Washington University School of Medicine)

  • Dorothy A. Schafer

    (University of Virginia)

  • John A. Cooper

    (Washington University School of Medicine)

Abstract

Capping protein (CP) has critical roles in actin assembly in vivo and in vitro. CP binds with high affinity to the barbed end of actin filaments, blocking the addition and loss of actin subunits. Heretofore, models for actin assembly in cells generally assumed that CP is constitutively active, diffusing freely to find and cap barbed ends. However, CP can be regulated by binding of the ‘capping protein interaction’ (CPI) motif, found in a diverse and otherwise unrelated set of proteins that decreases, but does not abolish, the actin-capping activity of CP and promotes uncapping in biochemical experiments. Here, we report that CP localization and the ability of CP to function in cells requires interaction with a CPI-motif-containing protein. Our discovery shows that cells target and/or modulate the capping activity of CP via CPI motif interactions in order for CP to localize and function in cells.

Suggested Citation

  • Marc Edwards & Patrick McConnell & Dorothy A. Schafer & John A. Cooper, 2015. "CPI motif interaction is necessary for capping protein function in cells," Nature Communications, Nature, vol. 6(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms9415
    DOI: 10.1038/ncomms9415
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