Actin-severing activity copurifies with phosphofructokinase.

A Füchtbauer; B M Jockusch; E Leberer; D Pette

doi:10.1073/pnas.83.24.9502

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Actin-severing activity copurifies with phosphofructokinase.

A Füchtbauer·B M Jockusch·E Leberer·D Pette

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Abstract

Microinjection of muscle 6-phosphofructokinase (PFK; EC 2.7.1.11) into tissue culture cells led to a reversible disintegration of microfilament bundles (stress fibers). The mode of disruption as well as of recovery of stress fibers was very similar to that found previously in experiments performed with the actin-severing protein brevin, an extracellular variant of gelsolin. PFK, like brevin, was also capable of disrupting stress fibers in detergent-extracted cells and in ethanol-fixed cells, in a Ca2+-dependent manner. When compared with heart muscle gelsolin, PFK comigrated with the 85- to 90-kDa band. Antibodies against PFK crossreacted with gelsolin from the same species. These results point to a tight association between polypeptides with similar biochemical and immunological parameters present in both preparations. They suggest hitherto unexpected cellular control mechanisms for both microfilament functions and glycolysis.

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Actin Cytoskeleton Animals Calcium-Binding Proteins Cell Line Chick Embryo Cross Reactions Cytoskeleton Dipodomys Fluorescent Antibody Technique Gelsolin Isoelectric Point Microfilament Proteins Molecular Weight Phosphofructokinase-1 Journal Article Research Support, Non-U.S. Gov't

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A Füchtbauer, B M Jockusch, E Leberer, D Pette. 1986. Actin-severing activity copurifies with phosphofructokinase.. https://doi.org/10.1073/pnas.83.24.9502

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