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Vol. 12, Issue 12, 4013-4029, December 2001
Centre National de la Recherche Scientifique, *
Morphogenèse et Signalisation Cellulaires, Unité
Mixte de Recherche 144, Institut Curie; An earlier report suggested that actin and myosin I alpha (MMIUnité Mixte
de Recherche 176, Institut Curie, 75248 Paris Cedex 05, France
),
a myosin associated with endosomes and lysosomes, were involved in the
delivery of internalized molecules to lysosomes. To determine whether actin and MMI were involved in the movement of lysosomes, we
analyzed by time-lapse video microscopy the dynamic of lysosomes in
living mouse hepatoma cells (BWTG3 cells), producing green fluorescent
protein actin or a nonfunctional domain of MMI. In GFP-actin
cells, lysosomes displayed a combination of rapid long-range directional movements dependent on microtubules, short random movements, and pauses, sometimes on actin filaments. We showed that the
inhibition of the dynamics of actin filaments by cytochalasin D
increased pauses of lysosomes on actin structures, while
depolymerization of actin filaments using latrunculin A increased the
mobility of lysosomes but impaired the directionality of their
long-range movements. The production of a nonfunctional domain of
MMI impaired the intracellular distribution of lysosomes and the
directionality of their long-range movements. Altogether, our
observations indicate for the first time that both actin filaments and
MMI contribute to the movement of lysosomes in cooperation with
microtubules and their associated molecular motors.
Corresponding author. E-mail address:
coudrier{at}curie.fr.
Online version of this article contains video
material for Figures 2, 5, 7, and 9. Online version is
available at www.molbiolcell.org.
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