CPI motif interaction is necessary for capping protein function in cells

Marc Edwards, Patrick McConnell, Dorothy A. Schafer and John A. Cooper ()
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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

Nature Communications, 2015, vol. 6, issue 1, 1-10

Abstract: 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.

Date: 2015
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms9415

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DOI: 10.1038/ncomms9415

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