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Biophys J, June 2000, p. 2863-2877, Vol. 78, No. 6
and
*Max-Planck-Institut für biophysikalische Chemie, D-37077
Göttingen, Germany; Max-Planck-Institut für
medizinische Forschung, D-69120 Heidelberg, Germany;
European Molecular Biology Laboratory, D-69012
Heidelberg, Germany; and §Vollum Institute,
Portland, Oregon 97201-3098 USA
In neuroendocrine PC-12 cells, evanescent-field
fluorescence microscopy was used to track motions of green fluorescent
protein (GFP)-labeled actin or GFP-labeled secretory granules in a thin layer of cytoplasm where cells adhered to glass. The layer contained abundant filamentous actin (F-actin) locally condensed into stress fibers. More than 90% of the granules imaged lay within the F-actin layer. One-third of the granules did not move detectably, while two-thirds moved randomly; the average diffusion coefficient was 23 × 10
4 µm2/s. A small minority
(<3%) moved rapidly and in a directed fashion over distances more
than a micron. Staining of F-actin suggests that such movement occurred
along actin bundles. The seemingly random movement of most other
granules was not due to diffusion since it was diminished by the myosin
inhibitor butanedione monoxime, and blocked by chelating intracellular
Mg2+ and replacing ATP with AMP-PNP. Mobility was blocked
also when F-actin was stabilized with phalloidin, and was diminished
when the actin cortex was degraded with latrunculin B. We conclude that
the movement of granules requires metabolic energy, and that it is
mediated as well as limited by the actin cortex. Opposing actions of
the actin cortex on mobility may explain why its degradation has
variable effects on secretion.
Biophys J, June 2000, p. 2863-2877, Vol. 78, No. 6
© 2000 by the Biophysical Society 0006-3495/00/06/2863/15 $2.00
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